F11R
Junctional adhesion molecule A
Also known as: CD321, JAM-1, JAM-A, JAM1, JAM1_HUMAN, JAMA, JCAM, PAM-1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9Y624
- Gene
- F11R
- Ensembl
- ENSG00000158769
- Chromosome
- 1
- Canonical length
- 299 aa
- Protein class
- CD markers, Plasma proteins, Predicted membrane proteins
- Subcellular location
- Cell Junctions,Microtubules
- Quaternary structure
- Homodimer
OverviewNCBI Gene
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple 5' alternatively spliced variants, encoding the same protein, have been identified but their biological validity has not been established. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
299 residues, UniProt reviewed canonical sequence.
>Q9Y624|F11R
1 MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC AYSGFSSPRV
61 EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT REDTGTYTCM VSEEGGNSYG
121 EVKVKLIVLV PPSKPTVNIP SSATIGNRAV LTCSEQDGSP PSEYTWFKDG IVMPTNPKST
181 RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV
241 AAVLVTLILL GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against F11R can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.39
- Highest tissue expression
- 88 nTPM
Expression across tissuesHPA
Tissue
- esophagus: 88 nTPM
- liver: 69 nTPM
- lung: 67 nTPM
- small intestine: 60 nTPM
- duodenum: 53 nTPM
- salivary gland: 50 nTPM
Single-cell type
- esophageal apical cells: 314 nCPM
- extravillous trophoblasts: 255 nCPM
- ocular epithelial cells: 242 nCPM
- urothelial cells: 235 nCPM
- pancreatic acinar cells: 174 nCPM
- alveolar cells type 1: 165 nCPM
Immune cell
- eosinophil: 166 nTPM
- neutrophil: 114 nTPM
- basophil: 35 nTPM
- classical monocyte: 31 nTPM
- total PBMC: 25 nTPM
- myeloid DC: 25 nTPM
Brain region
- choroid plexus: 14 nTPM
- thalamus: 12 nTPM
- medulla oblongata: 11 nTPM
- midbrain: 9.8 nTPM
- pons: 9.8 nTPM
- cerebral cortex: 9.5 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.01
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.95
- DepMap mean gene effect
- -0.17
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 11% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- actomyosin structure organization
- cell-cell adhesion
- cellular response to mechanical stimulus
- establishment of endothelial intestinal barrier
- inflammatory response
- intestinal absorption
- leukocyte cell-cell adhesion
- maintenance of blood-brain barrier
- memory T cell extravasation
- negative regulation of stress fiber assembly
- positive regulation of establishment of endothelial barrier
- positive regulation of platelet aggregation
- positive regulation of Rho protein signal transduction
- protein localization to bicellular tight junction
- protein localization to plasma membrane
- regulation of actin cytoskeleton organization
- regulation of bicellular tight junction assembly
- regulation of cell shape
- regulation of cytokine production
- regulation of cytoskeleton organization
- regulation of membrane permeability
Molecular functions
- cadherin binding
- integrin binding
- PDZ domain binding
- protein homodimerization activity
- virus receptor activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of F11R in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads F11R as an antibody target. Whether an autoantibody or antibody against F11R could matter depends on whether native F11R is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
F11R is annotated at the cell surface, where native F11R is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label F11R as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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