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Protein

Junctional adhesion molecule A

Gene

F11R

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11489913). The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (PubMed:11812992). Involved in platelet activation (PubMed:10753840).By similarity3 Publications
(Microbial infection) Acts as a receptor for Mammalian reovirus sigma-1.1 Publication
(Microbial infection) Acts as a receptor for Human Rotavirus strain Wa.1 Publication

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • PDZ domain binding Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • actomyosin structure organization Source: UniProtKB
  • bicellular tight junction assembly Source: Reactome
  • cell adhesion Source: Ensembl
  • establishment of endothelial intestinal barrier Source: UniProtKB
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • inflammatory response Source: ProtInc
  • intestinal absorption Source: UniProtKB
  • leukocyte migration Source: Reactome
  • negative regulation of GTPase activity Source: UniProtKB
  • positive regulation of blood pressure Source: Ensembl
  • positive regulation of GTPase activity Source: UniProtKB
  • regulation of actin cytoskeleton reorganization Source: UniProtKB
  • regulation of cytokine production Source: Ensembl
  • regulation of membrane permeability Source: UniProtKB
  • response to radiation Source: Ensembl
  • transforming growth factor beta receptor signaling pathway Source: Reactome

Keywordsi

Molecular functionHost cell receptor for virus entry, Receptor
Biological processHost-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-HSA-420029. Tight junction interactions.
SIGNORiQ9Y624.

Names & Taxonomyi

Protein namesi
Recommended name:
Junctional adhesion molecule A
Short name:
JAM-A
Alternative name(s):
Junctional adhesion molecule 1
Short name:
JAM-1
Platelet F11 receptor
Platelet adhesion molecule 1
Short name:
PAM-1
CD_antigen: CD321
Gene namesi
Name:F11R
Synonyms:JAM1, JCAM
ORF Names:UNQ264/PRO301
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14685. F11R.

Subcellular locationi

  • Cell junctiontight junction 1 Publication
  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: Localized at tight junctions of both epithelial and endothelial cells.1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 238ExtracellularSequence analysisAdd BLAST211
Transmembranei239 – 259HelicalSequence analysisAdd BLAST21
Topological domaini260 – 299CytoplasmicSequence analysisAdd BLAST40

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • cell-cell junction Source: ProtInc
  • cell junction Source: Reactome
  • cytoplasmic vesicle Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: LIFEdb
  • slit diaphragm Source: Ensembl

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Organism-specific databases

DisGeNETi50848.
OpenTargetsiENSG00000158769.
PharmGKBiPA29991.

Polymorphism and mutation databases

BioMutaiF11R.
DMDMi10720061.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Combined sources3 PublicationsAdd BLAST27
ChainiPRO_000001506628 – 299Junctional adhesion molecule AAdd BLAST272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 1091 Publication
Disulfide bondi153 ↔ 2121 Publication
Glycosylationi185N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi191N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei281PhosphoserineCombined sources1
Modified residuei284PhosphoserineCombined sources1
Modified residuei287PhosphoserineCombined sources1

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9Y624.
PaxDbiQ9Y624.
PeptideAtlasiQ9Y624.
PRIDEiQ9Y624.

PTM databases

iPTMnetiQ9Y624.
PhosphoSitePlusiQ9Y624.
SwissPalmiQ9Y624.

Expressioni

Tissue specificityi

Expressed in endothelium, epithelium and leukocytes (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000158769.
CleanExiHS_F11R.
ExpressionAtlasiQ9Y624. baseline and differential.
GenevisibleiQ9Y624. HS.

Organism-specific databases

HPAiCAB004671.
HPA043616.
HPA061700.

Interactioni

Subunit structurei

Interacts with the ninth PDZ domain of MPDZ (PubMed:11489913). Interacts with the first PDZ domain of PARD3 (PubMed:11489913). The association between PARD3 and PARD6B probably disrupts this interaction (By similarity). Interacts with ITGAL (via I-domain) (PubMed:15528364).By similarity2 Publications
(Microbial infection) Interacts with Mammalian reovirus sigma-1 capsid protein.1 Publication
(Microbial infection) Interacts with Human Rotavirus strain Wa vp4 capsid protein.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • PDZ domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119153. 16 interactors.
IntActiQ9Y624. 7 interactors.
MINTiMINT-154235.
STRINGi9606.ENSP00000289779.

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 32Combined sources3
Beta strandi36 – 41Combined sources6
Beta strandi47 – 49Combined sources3
Beta strandi51 – 54Combined sources4
Beta strandi56 – 66Combined sources11
Beta strandi69 – 75Combined sources7
Beta strandi76 – 79Combined sources4
Turni81 – 86Combined sources6
Beta strandi88 – 90Combined sources3
Beta strandi93 – 95Combined sources3
Helixi101 – 103Combined sources3
Beta strandi105 – 113Combined sources9
Beta strandi123 – 125Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi140 – 144Combined sources5
Beta strandi149 – 151Combined sources3
Beta strandi163 – 168Combined sources6
Beta strandi177 – 182Combined sources6
Turni192 – 194Combined sources3
Beta strandi197 – 201Combined sources5
Helixi204 – 206Combined sources3
Beta strandi210 – 215Combined sources6
Beta strandi217 – 219Combined sources3
Beta strandi230 – 232Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NBQX-ray2.90A/B27-233[»]
3EOYX-ray3.40G/H/I/J/K/L28-129[»]
3TSZX-ray2.50B288-299[»]
4ODBX-ray3.20D/E/F28-129[»]
ProteinModelPortaliQ9Y624.
SMRiQ9Y624.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y624.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 125Ig-like V-type 1Add BLAST98
Domaini135 – 228Ig-like V-type 2Add BLAST94

Domaini

The Ig-like V-type 2 domain is necessary and sufficient for interaction with integrin alpha-L/beta-2.1 Publication

Sequence similaritiesi

Belongs to the immunoglobulin superfamily.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IWUE. Eukaryota.
ENOG410YHHV. LUCA.
GeneTreeiENSGT00730000110678.
HOVERGENiHBG000518.
InParanoidiQ9Y624.
KOiK06089.
OMAiNRAFSNS.
OrthoDBiEOG091G05PI.
PhylomeDBiQ9Y624.
TreeFamiTF343984.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiView protein in InterPro
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
PfamiView protein in Pfam
PF07686. V-set. 1 hit.
SMARTiView protein in SMART
SM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiView protein in PROSITE
PS50835. IG_LIKE. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y624-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC
60 70 80 90 100
AYSGFSSPRV EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT
110 120 130 140 150
REDTGTYTCM VSEEGGNSYG EVKVKLIVLV PPSKPTVNIP SSATIGNRAV
160 170 180 190 200
LTCSEQDGSP PSEYTWFKDG IVMPTNPKST RAFSNSSYVL NPTTGELVFD
210 220 230 240 250
PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV AAVLVTLILL
260 270 280 290
GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLV
Length:299
Mass (Da):32,583
Last modified:November 1, 1999 - v1
Checksum:iD95DE2FEA23D2851
GO
Isoform 2 (identifier: Q9Y624-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-129: Missing.

Note: No experimental confirmation available.
Show »
Length:250
Mass (Da):27,208
Checksum:i548D39B300559F53
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05621881 – 129Missing in isoform 2. 1 PublicationAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF111713 mRNA. Translation: AAD42050.1.
AF207907 mRNA. Translation: AAF22829.1.
AF172398 mRNA. Translation: AAD48877.1.
AL136649 mRNA. Translation: CAB66584.1.
AY358896 mRNA. Translation: AAQ89255.1.
AK304412 mRNA. Translation: BAH14177.1.
AL591806 Genomic DNA. No translation available.
BC001533 mRNA. Translation: AAH01533.1.
CCDSiCCDS1213.1. [Q9Y624-1]
PIRiA59406. S56749.
RefSeqiNP_001335020.1. NM_001348091.1. [Q9Y624-2]
NP_058642.1. NM_016946.5. [Q9Y624-1]
UniGeneiHs.517293.

Genome annotation databases

EnsembliENST00000368026; ENSP00000357005; ENSG00000158769. [Q9Y624-1]
ENST00000537746; ENSP00000440812; ENSG00000158769. [Q9Y624-2]
GeneIDi50848.
KEGGihsa:50848.
UCSCiuc009wtt.4. human. [Q9Y624-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiJAM1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y624
Secondary accession number(s): B7Z941
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 5, 2017
This is version 179 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families