ALPHASUITEATLASTM
LY96 · Q9Y6Y9Homo sapiens
PROTEIN OVERVIEW

LY96Lymphocyte antigen 96

Q9Y6Y9Homo sapiensReviewed · UniProt

Binds bacterial lipopolysaccharide (LPS).

Sequence160 aa
Source mass18.55 kDa
Recorded PDB entries9
Isoforms listed2

UniProt locations Secreted, extracellular space · Secreted

01

Function

Binds bacterial lipopolysaccharide (LPS) [12, 11]. Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria [8, 9]. Enhances TLR4-dependent activation of NF-kappa-B [1].

Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS [1]

Experimental evidence 5 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10359581"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11160242"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11593030"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17569869"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17803912"
        }
      ],
      "value": "Binds bacterial lipopolysaccharide (LPS) (PubMed:17569869, PubMed:17803912). Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria (PubMed:11160242, PubMed:11593030). Enhances TLR4-dependent activation of NF-kappa-B (PubMed:10359581). Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS (PubMed:10359581)"
    }
  ],
  "commentType": "FUNCTION"
}

GO functions & biological processes

response to lipopolysaccharideacts upstream of or withinUniProtKB:Q9Y6Y9
GO
GO:0032496 · evidence & context
  • ECO:0000314 PMID:12594207 ↗ IDA · MGI · 20100606
    qualifier: acts_upstream_of_or_within
lipopolysaccharide bindingenablesUniProtKB:Q9Y6Y9
GO
GO:0001530 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR039217"}]}]
lipopolysaccharide immune receptor activityenablesUniProtKB:Q9Y6Y9
GO
GO:0001875 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190213
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000390890"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6Y9"}]}]
  • ECO:0000314 PMID:19252480 ↗ IDA · UniProt · 20090602
    qualifier: enables
protein bindingenablesUniProtKB:Q9Y6Y9
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:15728506 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206"}]}]
  • ECO:0000353 PMID:17803912 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206"}]}]
  • ECO:0000353 PMID:19060881 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206-1"}]}]
  • ECO:0000353 PMID:19060881 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49278"}]}]
  • ECO:0000353 PMID:19252480 ↗ IPI · UniProt · 20090602
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206"}]}]
  • ECO:0000353 PMID:19252480 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206-1"}]}]
  • ECO:0000353 PMID:20547845 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206"}]}]
  • ECO:0000353 PMID:22474354 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206-1"}]}]
  • ECO:0000353 PMID:22532668 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00206-1"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P80188"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14696"}]}]
coreceptor activityenablesUniProtKB:Q9Y6Y9
GO
GO:0015026 · evidence & context
All recorded function and process assertions (18)
Toll-like receptor 4 bindingenablesUniProtKB:Q9Y6Y9
GO
GO:0035662 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR039217"}]}]
pattern recognition receptor signaling pathwayinvolved inUniProtKB:Q9Y6Y9
GO
GO:0002221 · evidence & context
  • ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00033911"}]}]
toll-like receptor signaling pathwayinvolved inUniProtKB:Q9Y6Y9
GO
GO:0002224 · evidence & context
cellular defense responseinvolved inUniProtKB:Q9Y6Y9
GO
GO:0006968 · evidence & context
cell surface receptor signaling pathwayinvolved inUniProtKB:Q9Y6Y9
GO
GO:0007166 · evidence & context
lipopolysaccharide-mediated signaling pathwayinvolved inUniProtKB:Q9Y6Y9
GO
GO:0031663 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00087514"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9JHF9"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000026881"}]}]
positive regulation of lipopolysaccharide-mediated signaling pathwayinvolved inUniProtKB:Q9Y6Y9
GO
GO:0031666 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190213
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:1341909"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000390890"}]}]
response to lipopolysaccharideinvolved inUniProtKB:Q9Y6Y9
GO
GO:0032496 · evidence & context
detection of lipopolysaccharideinvolved inUniProtKB:Q9Y6Y9
GO
GO:0032497 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190213
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000390890"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6Y9"}]}]
  • ECO:0000314 PMID:19252480 ↗ IDA · UniProt · 20090602
    qualifier: involved_in
positive regulation of tumor necrosis factor productioninvolved inUniProtKB:Q9Y6Y9
GO
GO:0032760 · evidence & context
  • ECO:0000250 GO_REF:0000024 ISS · UniProt · 20150720
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9JHF9"}]}]
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9JHF9"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000026881"}]}]
toll-like receptor 4 signaling pathwayinvolved inUniProtKB:Q9Y6Y9
GO
GO:0034142 · evidence & context
  • ECO:0000250 GO_REF:0000024 ISS · UniProt · 20150720
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9JHF9"}]}]
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190213
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:1341909"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000390890"}]}]
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9JHF9"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000026881"}]}]
innate immune responseinvolved inUniProtKB:Q9Y6Y9
GO
GO:0045087 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR039217"}]}]
  • ECO:0005547 PMID:33576548 ↗ NAS · ComplexPortal · 20240827
    qualifier: involved_in
cellular response to lipopolysaccharideinvolved inUniProtKB:Q9Y6Y9
GO
GO:0071222 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:1341909"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000390890"}]}, {"connectedXrefs": [{"db": "RGD", "id": "1302993"}]}]
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9JHF9"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000026881"}]}]
02

Names & Taxonomy

Recommended name
Lymphocyte antigen 96
Gene
LY96
Accession / entry
Q9Y6Y9 · LY96_HUMAN
Species
Homo sapiens · NCBI 9606
Recorded aliases
ESOP-1 · ESOP1 · MD2 · Protein MD-2
Full taxonomy & recorded names

Eukaryota → Metazoa → Chordata → Craniata → Vertebrata → Euteleostomi → Mammalia → Eutheria → Euarchontoglires → Primates → Haplorrhini → Catarrhini → Hominidae → Homo

{
  "names": {
    "recommendedName": {
      "fullName": {
        "value": "Lymphocyte antigen 96"
      },
      "shortNames": [
        {
          "value": "Ly-96"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "evidences": [
            {
              "evidenceCode": "ECO:0000303",
              "source": "PubMed",
              "id": "10891475"
            }
          ],
          "value": "ESOP-1"
        }
      },
      {
        "fullName": {
          "evidences": [
            {
              "evidenceCode": "ECO:0000303",
              "source": "PubMed",
              "id": "10359581"
            }
          ],
          "value": "Protein MD-2"
        }
      }
    ],
    "flag": "Precursor"
  },
  "genes": [
    {
      "geneName": {
        "value": "LY96"
      },
      "synonyms": [
        {
          "value": "ESOP1"
        },
        {
          "value": "MD2"
        }
      ]
    }
  ]
}
03

Subcellular Location

UniProt locations and GO cellular-component assertions. Relations and contexts remain distinct; “part of” is not automatically a residence claim.

Secreted, extracellular spaceReported location

Retained in the extracellular space at the cell surface by interaction with TLR4 [1]

UniProt
Experimental evidenceCurator inference 3 publications
Evidence & references
SecretedReported location

Retained in the extracellular space at the cell surface by interaction with TLR4 [1]

UniProt
Experimental evidence 1 publication
Evidence & references
extracellular regionlocated in
GO
Experimental evidence 1 publication
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027128"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0112"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0243"}]}]
  • ECO:0000269 PMID:11593030 ↗ EXP · UniProt · 20251027
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9707594 TAS · Reactome · 20201119
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9707659 TAS · Reactome · 20201119
    qualifier: located_in
plasma membranelocated in
GO
3 publications
Evidence & references
  • ECO:0000304 PMID:10359581 ↗ TAS · PINC · 20031120
    qualifier: located_in
  • ECO:0000314 PMID:11274165 ↗ IDA · UniProt · 20150716
    qualifier: located_in
  • ECO:0005547 PMID:33576548 ↗ NAS · ComplexPortal · 20240827
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166041 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166072 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166082 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166091 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166119 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166284 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166286 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166362 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166363 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2201293 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2201316 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2201322 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2262775 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2262777 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2559414 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5432825 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5432849 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5432852 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5602353 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5602383 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5602606 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6805943 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8870678 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-937022 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-937059 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-937079 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9836227 TAS · Reactome · 20150219
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9921458 TAS · Reactome · 20150219
    qualifier: located_in
endosome membranelocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-166168 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166175 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166245 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-166271 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-168915 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-168921 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2201293 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2201338 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2213017 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2559568 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2562541 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2562564 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2569057 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-450358 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5362486 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5362500 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-936947 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-936951 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-936952 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-936985 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-937029 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-937075 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9823904 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9823906 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9823910 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9823932 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9823934 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9823939 TAS · Reactome · 20130528
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9824882 TAS · Reactome · 20130528
    qualifier: located_in
signaling receptor complexpart of
GO
1 publication
Evidence & references
lipopolysaccharide receptor complexpart of
GO
2 publications
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20190213
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:1341909"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000390890"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6Y9"}]}]
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00092195"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9JHF9"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000026881"}]}]
  • ECO:0000314 PMID:11274165 ↗ IDA · UniProt · 20150716
    qualifier: part_of
  • ECO:0000314 PMID:19252480 ↗ IDA · UniProt · 20090602
    qualifier: part_of

Membrane topology 0

No annotation is recorded in this UniProt entry.

04

Disease & Variants

Source annotations; a recorded variant is not automatically a clinical classification.

No annotation is recorded in this UniProt entry.

Natural variants 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
R56GVAR_05003056in dbSNP:rs6472812
R → G
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
P157SVAR_024532157in dbSNP:rs11466004
P → S
Evidence & references

No separate evidence record is supplied for this statement.

1/1 residues mapped to 8WO1

Laboratory mutagenesis 1

Scroll across the table for evidence and actions.

1 recorded rows

FeaturePositionDescriptionEvidenceInspect
C95Y95Abolishes LPS-response.
C → Y
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 8WO1
05

PTM/Processing

N-glycosylated; high-mannose

Experimental evidence 2 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11593030"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17569869"
        }
      ],
      "value": "N-glycosylated; high-mannose"
    }
  ],
  "commentType": "PTM"
}

Processed chains & precursor regions 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
Signal1–18Signal
Sequence analysis
Evidence & references
  • ECO:0000255
No verified residues in this structure
ChainPRO_000001861919–160Lymphocyte antigen 96
Evidence & references

No separate evidence record is supplied for this statement.

139/142 residues mapped to 8WO1

Modifications 5

Scroll across the table for evidence and actions.

5 recorded rows

FeaturePositionDescriptionEvidenceInspect
Glycosylation26N-linked (GlcNAc...) asparagine
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 8WO1
Glycosylation114N-linked (GlcNAc...) asparagine
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 8WO1
Disulfide bond25, 51Disulfide bond
Experimental evidence 2 publications
Evidence & references
2/2 residues mapped to 8WO1
Disulfide bond37, 148Disulfide bond
Experimental evidence 2 publications
Evidence & references
2/2 residues mapped to 8WO1
Disulfide bond95, 105Disulfide bond
Experimental evidence 2 publications
Evidence & references
2/2 residues mapped to 8WO1
06

Expression

No annotation is recorded in this UniProt entry.

07

Interaction

Documented interaction partners

UniProt’s filtered IntAct records. Experiment counts describe reported experiments, not binding strength or independent publications. Separate products remain separate rows.

5 records
Partner / productSpeciesExperimentsEvidence & actions
LCN2P80188With Q9Y6Y9Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: Q9Y6Y9. Partner: P80188. Reported experiment count: 3.

Open protein ↗
MESDQ14696With Q9Y6Y9Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: Q9Y6Y9. Partner: Q14696. Reported experiment count: 3.

Open protein ↗
TLR4O00206With Q9Y6Y9Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: Q9Y6Y9. Partner: O00206. Reported experiment count: 7.

Open protein ↗
TLR4O00206-1With Q9Y6Y9Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: Q9Y6Y9. Partner: O00206-1. Reported experiment count: 5.

Open protein ↗
DERP2P49278With Q9Y6Y9Dermatophagoides pteronyssinusCross-species2
IntAct evidence

Pair evidence in IntAct ↗

Source product: Q9Y6Y9. Partner: P49278. Reported experiment count: 2.

Open protein ↗

Complex membership & assembly descriptions

Co-membership does not by itself prove direct binding between every pair.

LY96-TLR4 toll-like receptor complex CPX-2545 Complex Portal

Homo sapiens; 9606 · Heterotetramer

Evidence: physical interaction evidence

  • LY96 · Q9Y6Y9 · minValue: 2, maxValue: 2
  • TLR4 · O00206 · minValue: 2, maxValue: 2

Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids. In the early step of bacterial infection, serum lipopolysaccharide (LPS, CHEBI:16412) binds to the N-terminal of LBP (P18428), LPS is then presented to CD14 (P08571) and transferred to LY96 or the LY96-TLR4 toll-like receptor complex. This induces the dimerization of TLR4 TIR domains, initiating CD14-dependent TLR4 endocytosis, and TICAM1/TRIF(Q8IUC6)-dependent signal transduction to promote inflammation caused by LPS.

Source & references ↗

UniProt subunit description

Heterogeneous homomer formed from homodimers; disulfide-linked [9, 10]. Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 [7]. Binds to the extracellular domains of TLR2 and TLR4 [1, 9, 11].

Ligand binding induces interaction with TLR4 and oligomerization of the complex

Experimental evidence 5 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10359581"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11274165"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11593030"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17569869"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17803912"
        }
      ],
      "value": "Heterogeneous homomer formed from homodimers; disulfide-linked (PubMed:11593030, PubMed:12642668). Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:11274165). Binds to the extracellular domains of TLR2 and TLR4 (PubMed:10359581, PubMed:11593030, PubMed:17803912). Ligand binding induces interaction with TLR4 and oligomerization of the complex"
    }
  ],
  "commentType": "SUBUNIT"
}

Other association resources

Resource links only; their association networks and counts are not added to the partner table.

BioGRID · 117170 ↗IntAct · Q9Y6Y9 ↗STRING · 9606.ENSP00000284818 ↗
08

Structure

SELECTED EXPERIMENTAL STRUCTURE

8WO1 · Cryo-EM Structure of Human TLR4/MD-2/DLAM5 Complex

Method
Electron microscopy
Resolution
2.24 Å
Assembly 1
Hetero 4-mer · A2B2
Symmetry
C2
Deposited / released
06/10/2023 / 09/10/2024
Entry version
3.1 · 14/05/2025
160aa · full canonical protein
142aa · deposited protein construct(s)
139canonical residues verified in coordinates

Verified residue selection uses chain(s) C. Deposited construct lengths are per protein entity, not the full precursor or a total across assembly copies.

139/139 residues mapped to 8WO1

Components & chains

Chain labels below are mmCIF identifiers used by the viewer. Assembly membership does not establish direct binding.

ComponentIdentity / lengthChainsInspect
Toll-like receptor 4Protein / polymer · Entity 1Homo sapiensO00206605 aaA, B
Lymphocyte antigen 96Protein / polymer · Entity 2Homo sapiensQ9Y6Y9142 aaC, D
beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranoseGlycan · Entity 3GlyCosmos G15407YE ↗CCD BMA ↗ CCD NAG ↗
Component chemical diagrams · RCSB PDB

Individual sugar components; this is not a diagram of glycan linkages.

RCSB chemical diagram of BMA
BMA
RCSB chemical diagram of NAG
NAG
BMA · NAG3 sugar unitsE, F, H, I
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranoseGlycan · Entity 4GlyCosmos G42666HT ↗CCD NAG ↗
Component chemical diagrams · RCSB PDB

Individual sugar components; this is not a diagram of glycan linkages.

RCSB chemical diagram of NAG
NAG
NAG2 sugar unitsG, J
2-acetamido-2-deoxy-beta-D-glucopyranoseLigand / ion · Entity 5CCD NAG ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of NAG
NAG
NAGK, L, N, O, Q, VAuthor: A, B, C, D
2-amino-2-deoxy-4-O-phosphono-alpha-D-glucopyranoseLigand / ion · Entity 6CCD GP4 ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of GP4
GP4
GP4M, PAuthor: A, B
(3R)-3-(dodecanoyloxy)tetradecanoic acidLigand / ion · Entity 7CCD 2IL ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of 2IL
2IL
2ILR, WAuthor: C, D
(3R)-3-(tetradecanoyloxy)tetradecanoic acidLigand / ion · Entity 8CCD 0IL ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of 0IL
0IL
0ILS, XAuthor: C, D
[(2~{R},3~{S},4~{R},5~{S})-2-(hydroxymethyl)-5-methoxy-4,6-bis(oxidanyl)oxan-3-yl] dihydrogen phosphateLigand / ion · Entity 9CCD X6N ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of X6N
X6N
X6NT, YAuthor: C, D
(3~{S})-3-decanoyloxytetradecanoic acidLigand / ion · Entity 10CCD A1L01 ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of A1L01
A1L01
A1L01U, ZAuthor: C, D

Chemical diagrams are recorded RCSB component depictions. Glycan names and source identifiers retain the recorded linkage information.

Structure validation

Recorded PDBe metrics describe model geometry. Percentiles compare with the archive; they are not probabilities of correctness. Missing metrics are not zero.

Clashscore7.25

Serious atomic overlaps per 1,000 atoms; lower is better.

Archive percentile: 37.3
Ramachandran outliers0.0%

Backbone conformations outside preferred regions; lower is better.

Archive percentile: 100.0
Side-chain outliers0.0%

Unusual side-chain conformations; lower is better.

Archive percentile: 100.0
Full validation report ↗

Publication

Structural insight into TLR4/MD-2 activation by synthetic LPS mimetics with distinct binding modes.

Paper date: 05/05/2025 · Read publication ↗

Structure references are from the dated source record. Opening another structure follows your existing Atlas account permissions.

Available structures 10

Scroll across the table for evidence and actions.

10 recorded rows

RecordEvidence typeMethodResolutionOpen
2E56experimentalX-ray2.00 AOpen in Atlas ↗
2E59experimentalX-ray2.21 AOpen in Atlas ↗
4G8AexperimentalX-ray2.40 AOpen in Atlas ↗
8WO1experimentalEM2.24 AOpen in Atlas ↗
9J03experimentalEM2.70 AOpen in Atlas ↗
2Z65experimentalX-ray2.70 AOpen in Atlas ↗
8WTAexperimentalEM2.90 AOpen in Atlas ↗
3FXIexperimentalX-ray3.10 AOpen in Atlas ↗
3ULAexperimentalX-ray3.60 AOpen in Atlas ↗
AF-Q9Y6Y9-F1predictedAlphaFoldNot applicableOpen in Atlas ↗
09

Family & Domains

Domain architecture

Canonical sequence1160 aa
Coverage
Domains & repeats
Variants
Processing

Canonical coordinates. Overlapping marks share a lane; individual records and evidence are in the tables below. Gaps in coverage are not selectable in 3D. Use the track links and tables for keyboard inspection.

Atlas domains, motifs & repeats 1

Scroll across the table for evidence and actions.

1 recorded rows

AnnotationPositionSource & interpretationInspect
MD-2-related lipid-recognition domainIPR00317232–153INTERPROdomain

The MD-2-related lipid-recognition (ML) domain is implicated in lipid recognition, particularly in the recognition of pathogen related products. It has an immunoglobulin-like β-sandwich fold similar to that of E-set Ig domains.

Full source description

The MD-2-related lipid-recognition (ML) domain is implicated in lipid recognition, particularly in the recognition of pathogen related products. It has an immunoglobulin-like β-sandwich fold similar to that of E-set Ig domains. This domain is present in proteins from plants, animals and fungi, including the following proteins: Epididymal secretory protein E1 (also known as Niemann-Pick C2 protein -Npc2), which is known to bind cholesterol. Niemann-Pick disease type C2 is a fatal hereditary disease characterised by accumulation of low-density lipoprotein-derived cholesterol in lysosomes. House-dust mite allergen proteins such as Der f 2 from Dermatophagoides farinae and Der p 2 from Dermatophagoides pteronyssinus.

Source entry ↗		121/122 residues mapped to 8WO1

UniProt domains, repeats & motifs 0

No annotation is recorded in this UniProt entry.

Functional sites 0

No annotation is recorded in this UniProt entry.

Sequence regions 1

Scroll across the table for evidence and actions.

1 recorded rows

FeaturePositionDescriptionEvidenceInspect
Region119–123Interaction with lipopolysaccharide
Experimental evidence 2 publications
Evidence & references
5/5 residues mapped to 8WO1
10

Sequence & Isoforms

Sequence & isoforms

UniProt’s canonical sequence is its selected representative. It is not necessarily the dominant isoform in every tissue.

UniProt’s canonical sequence · Q9Y6Y9-1160 aa18,546 Da · source sequence mass

Full precursor sequence, including processing regions. The mass describes this unmodified source sequence, not every mature or modified product.

MLPFLFFSTLFSSIFTEAQKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN

Source isoform notes & selection

Alternative splicing

Complete source annotation
{
  "commentType": "ALTERNATIVE PRODUCTS",
  "events": [
    "Alternative splicing"
  ],
  "isoforms": [
    {
      "name": {
        "value": "1"
      },
      "isoformIds": [
        "Q9Y6Y9-1"
      ],
      "isoformSequenceStatus": "Displayed"
    },
    {
      "name": {
        "value": "2"
      },
      "isoformIds": [
        "Q9Y6Y9-2"
      ],
      "sequenceIds": [
        "VSP_055045"
      ],
      "isoformSequenceStatus": "Described"
    }
  ]
}
  • Q9Y6Y9-1 · 1 · Displayed
    Complete source annotation
    {
  "name": {
    "value": "1"
  },
  "isoformIds": [
    "Q9Y6Y9-1"
  ],
  "isoformSequenceStatus": "Displayed"
}
  • Q9Y6Y9-2 · 2 · Described · VSP_055045
    Complete source annotation
    {
  "name": {
    "value": "2"
  },
  "isoformIds": [
    "Q9Y6Y9-2"
  ],
  "sequenceIds": [
    "VSP_055045"
  ],
  "isoformSequenceStatus": "Described"
}

Isoform sequence differences 1

Scroll across the table for evidence and actions.

1 recorded rows

FeaturePositionDescriptionEvidenceInspect
Alternative sequenceVSP_05504538–68in isoform 2
DKMQYPISINVNPCIELKRSKGLLHIFYIPR → G
Curator inference
Evidence & references
  • ECO:0000305
30/31 residues mapped to 8WO1

Sequence conflicts & cautions 0

No annotation is recorded in this UniProt entry.

Recorded secondary structure 14

Scroll across the table for evidence and actions.

14 recorded rows

FeaturePositionDescriptionEvidenceInspect
Helix18–21Helix
Evidence & references
  • ECO:0007829 PDB:2E56
3/4 residues mapped to 8WO1
Beta strand22–26Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
5/5 residues mapped to 8WO1
Beta strand28–36Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
9/9 residues mapped to 8WO1
Beta strand38–40Beta strand
Evidence & references
  • ECO:0007829 PDB:4G8A
3/3 residues mapped to 8WO1
Beta strand45–50Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
6/6 residues mapped to 8WO1
Beta strand57–65Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
9/9 residues mapped to 8WO1
Beta strand75–82Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
8/8 residues mapped to 8WO1
Beta strand90–93Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
4/4 residues mapped to 8WO1
Beta strand97–101Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
5/5 residues mapped to 8WO1
Helix103–106Helix
Evidence & references
  • ECO:0007829 PDB:2E56
4/4 residues mapped to 8WO1
Beta strand113–121Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
9/9 residues mapped to 8WO1
Beta strand129–139Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
11/11 residues mapped to 8WO1
Turn140–143Turn
Evidence & references
  • ECO:0007829 PDB:2E56
4/4 residues mapped to 8WO1
Beta strand144–155Beta strand
Evidence & references
  • ECO:0007829 PDB:2E56
12/12 residues mapped to 8WO1
12

Homologs

OMA orthologs

Evolutionary relationships assigned by OMA, kept separate from sequence clusters. “1:1” describes an orthology relationship, not percentage identity.

Recorded preview of up to 12 orthologs; not an exhaustive list. Entries without a verified UniProt mapping open their OMA record.

XP_040288186.1Bufo bufo1:1OMA record ↗
XP_066435139.1Eleutherodactylus coqui1:1OMA record ↗
A0A1L8FTB8Xenopus laevis1:1OMA record ↗
A0A8D0LCH1Sphenodon punctatus1:1OMA record ↗
A0AA97L420Eublepharis macularius1:1OMA record ↗
XP_042320449.1Sceloporus undulatus1:1OMA record ↗
A0ABQ7SJV5Phrynosoma platyrhinos1:1OMA record ↗
A0A9F5INY0Python bivittatus1:1OMA record ↗
XP_032079166.1Thamnophis elegans1:1OMA record ↗
A0A6P9D125Pantherophis guttatus1:1OMA record ↗
A0A8C6XMP4Naja naja1:1OMA record ↗
XP_039188015.1Crotalus tigris1:1OMA record ↗
13

Sources & References

Scientific descriptions and evidence come from the named sources. Atlas assembles the presentation and verifies residue mappings; it does not independently curate these claims.

UniProt ↗QuickGO ↗InterPro ↗PDB / PDBe ↗Complex Portal ↗UniRef ↗OMA ↗
Source dates & provenance

Recorded 2026-11-10. Source dates and identifiers are retained below.

Publications in this UniProt entry

1 · MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4.

1999 · J. Exp. Med.

PubMed 10359581 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT GLY-56; FUNCTION; INTERACTION WITH TLR4; SUBCELLULAR LOCATION

Shimazu R., Akashi S., Ogata H., Nagai Y., Fukudome K., Miyake K., Kimoto M.

2 · ESOP-1, a secreted protein expressed in the hematopoietic, nervous, and reproductive systems of embryonic and adult mice.

2000 · Blood

PubMed 10891475 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT GLY-56

Kato K., Morrison A.M., Nakano T., Tashiro K., Honjo T.

3 · Molecular genetic analysis of an endotoxin nonresponder mutant cell line. A point mutation in a conserved region of MD-2 abolishes endotoxin-induced signaling.

2001 · J. Exp. Med.

PubMed 11435474 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); MUTAGENESIS OF CYS-95; VARIANT GLY-56

Schromm A.B., Lien E., Henneke P., Chow J.C., Yoshimura A., Heine H., Latz E., Monks B.G., Schwartz D.A., Miyake K., Golenbock D.T.

4 · Natural selection in the TLR-related genes in the course of primate evolution.

2008 · Immunogenetics

PubMed 18810425 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT GLY-56

Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.

All source publications (12)
5 · DNA sequence and analysis of human chromosome 8.

2006 · Nature

PubMed 16421571 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.

6 · The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

2004 · Genome Res.

PubMed 15489334 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANT GLY-56

7 · Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex. transfer from CD14 to TLR4 and MD-2.

2001 · J. Biol. Chem.

PubMed 11274165 ↗
Scope & authors

SUBUNIT; SUBCELLULAR LOCATION

da Silva Correia J., Soldau K., Christen U., Tobias P.S., Ulevitch R.J.

8 · MD-2 enables Toll-like receptor 2 (TLR2)-mediated responses to lipopolysaccharide and enhances TLR2-mediated responses to Gram-positive and Gram-negative bacteria and their cell wall components.

2001 · J. Immunol.

PubMed 11160242 ↗
Scope & authors

INTERACTION WITH TLR2 AND TLR4; FUNCTION

Dziarski R., Wang Q., Miyake K., Kirschning C.J., Gupta D.

9 · Secreted MD-2 is a large polymeric protein that efficiently confers lipopolysaccharide sensitivity to Toll-like receptor 4.

2001 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 11593030 ↗
Scope & authors

DISULFIDE BONDS; GLYCOSYLATION; SUBCELLULAR LOCATION; FUNCTION; INTERACTION WITH TLR4

Visintin A., Mazzoni A., Spitzer J.A., Segal D.M.

10 · The role of disulfide bonds in the assembly and function of MD-2.

2003 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 12642668 ↗
Scope & authors

INTERCHAIN DISULFIDE BOND

Mullen G.E.D., Kennedy M.N., Visintin A., Mazzoni A., Leifer C.A., Davies D.R., Segal D.M.

11 · Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran.

2007 · Cell

PubMed 17803912 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH TLR4 AND LIPOPOLYSACCHARIDE ANALOG; SUBUNIT

Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C., Enkhbayar P., Matsushima N., Lee H., Yoo O.J., Lee J.-O.

12 · Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.

2007 · Science

PubMed 17569869 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH LIPID IV-A; DISULFIDE BONDS; GLYCOSYLATION AT ASN-26 AND ASN-114

Ohto U., Fukase K., Miyake K., Satow Y.

Annotation coverage audit

Every recorded UniProt comment and feature has a destination in this page. GO, Atlas annotations and interaction rows retain their separate source counts.

32 source comments and features accounted for.

View annotation inventory
Source recordTypeSection
FUNCTION:0FUNCTIONfunction
SUBUNIT:0SUBUNITinteractions
INTERACTION:0INTERACTIONinteractions
SUBCELLULAR LOCATION:0SUBCELLULAR LOCATIONlocation
ALTERNATIVE PRODUCTS:0ALTERNATIVE PRODUCTSsequence
PTM:0PTMprocessing
feature-0Signalprocessing
feature-1Chainprocessing
feature-2Regiondomains
feature-3Glycosylationprocessing
feature-4Glycosylationprocessing
feature-5Disulfide bondprocessing
feature-6Disulfide bondprocessing
feature-7Disulfide bondprocessing
feature-8Alternative sequencesequence
feature-9Natural variantdisease
feature-10Natural variantdisease
feature-11Mutagenesisdisease
feature-12Helixsequence
feature-13Beta strandsequence
feature-14Beta strandsequence
feature-15Beta strandsequence
feature-16Beta strandsequence
feature-17Beta strandsequence
feature-18Beta strandsequence
feature-19Beta strandsequence
feature-20Beta strandsequence
feature-21Helixsequence
feature-22Beta strandsequence
feature-23Beta strandsequence
feature-24Turnsequence
feature-25Beta strandsequence