P78310 · CXAR_HUMAN
- ProteinCoxsackievirus and adenovirus receptor
- GeneCXADR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCoxsackievirus and adenovirus receptor
- Short namesCAR; hCAR
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP78310
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 3
Isoform 4
Isoform 5
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-237 | Extracellular | ||||
Sequence: LSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPPSNKAG | ||||||
Transmembrane | 238-258 | Helical | ||||
Sequence: LIAGAIIGTLLALALIGLIIF | ||||||
Topological domain | 259-365 | Cytoplasmic | ||||
Sequence: CCRKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTPQSPTLPPAKVAAPNLSRMGAIPVMIPAQSKDGSIV |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 70-72 | Abolishes binding to adenovirus type 5. | ||||
Sequence: VII → AID | ||||||
Mutagenesis | 259-260 | Loss of palmitoylation and altered localization. | ||||
Sequence: CC → AA | ||||||
Mutagenesis | 318 | Affects basolateral localization in airway epithelial cells. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_049871 | 323 | in dbSNP:rs34727960 | |||
Sequence: S → R | ||||||
Mutagenesis | 345-348 | Affects basolateral localization in airway epithelial cells. | ||||
Sequence: LSRM → AAAA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 386 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-19 | UniProt | |||||
Sequence: MALLLCFVLLCGVVDFARS | |||||||
Chain | PRO_0000014739 | 20-365 | UniProt | Coxsackievirus and adenovirus receptor | |||
Sequence: LSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPPSNKAGLIAGAIIGTLLALALIGLIIFCCRKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTPQSPTLPPAKVAAPNLSRMGAIPVMIPAQSKDGSIV | |||||||
Disulfide bond | 41↔120 | UniProt | |||||
Sequence: CKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQC | |||||||
Glycosylation | 106 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 162↔212 | UniProt | |||||
Sequence: CEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSC | |||||||
Glycosylation | 201 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Lipidation | 259 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 260 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 297 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 304 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 306 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 313 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 323 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 332 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 334 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 359 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 363 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P78310 | ANKRD46 Q86W74-2 | 3 | EBI-747931, EBI-12109402 | |
BINARY | P78310 | FAM3C Q92520 | 3 | EBI-747931, EBI-2876774 | |
BINARY | P78310 | MAL P21145 | 3 | EBI-747931, EBI-3932027 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-134 | Ig-like C2-type 1 | ||||
Sequence: LSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIH | ||||||
Domain | 141-228 | Ig-like C2-type 2 | ||||
Sequence: PSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLN | ||||||
Compositional bias | 269-285 | Basic and acidic residues | ||||
Sequence: YEKEVHHDIREDVPPPK | ||||||
Region | 269-343 | Disordered | ||||
Sequence: YEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTPQSPTLPPAKVAAP | ||||||
Compositional bias | 286-330 | Polar residues | ||||
Sequence: SRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTP | ||||||
Motif | 360-365 | PDZ-binding | ||||
Sequence: KDGSIV |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 7 isoforms produced by Alternative splicing.
P78310-1
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.
- Name1
- SynonymsSIV
- Length365
- Mass (Da)40,030
- Last updated1997-05-01 v1
- ChecksumAB01C6346CB7FE64
P78310-2
- Name2
- SynonymsCAR2, HCAR2, TVV
P78310-3
- Name3
- SynonymsCAR2/7, Gamma
P78310-4
- Name4
- SynonymsCAR3/7
P78310-5
- Name5
- SynonymsCAR4/7, Beta
P78310-6
- Name6
- Differences from canonical
- 340-365: VAAPNLSRMGAIPVMIPAQSKDGSIV → FKYPYKTDGITVV
P78310-7
- Name7
- SynonymsCAR 4/6
- Differences from canonical
- 191-232: EMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPP → A
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_014819 | 71-89 | in isoform 3 | |||
Sequence: IILYSGDKIYDDYYPDLKG → GRCATSKEPYVHCQKLHRQ | ||||||
Alternative sequence | VSP_014820 | 90-365 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_014821 | 139 | in isoform 4 | |||
Sequence: V → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR | ||||||
Alternative sequence | VSP_014822 | 140-365 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_014823 | 191 | in isoform 5 | |||
Sequence: E → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR | ||||||
Alternative sequence | VSP_047729 | 191-232 | in isoform 7 | |||
Sequence: EMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPP → A | ||||||
Alternative sequence | VSP_014824 | 192-365 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 269-285 | Basic and acidic residues | ||||
Sequence: YEKEVHHDIREDVPPPK | ||||||
Compositional bias | 286-330 | Polar residues | ||||
Sequence: SRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTP | ||||||
Alternative sequence | VSP_014825 | 340-345 | in isoform 2 | |||
Sequence: VAAPNL → FKYPY | ||||||
Alternative sequence | VSP_047357 | 340-365 | in isoform 6 | |||
Sequence: VAAPNLSRMGAIPVMIPAQSKDGSIV → FKYPYKTDGITVV | ||||||
Sequence conflict | 343 | In isoform P78310-2; in Ref. 14; AAD31772 | ||||
Sequence: P → A | ||||||
Alternative sequence | VSP_014826 | 346-365 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U90716 EMBL· GenBank· DDBJ | AAC51234.1 EMBL· GenBank· DDBJ | mRNA | ||
Y07593 EMBL· GenBank· DDBJ | CAA68868.1 EMBL· GenBank· DDBJ | mRNA | ||
AF169366 EMBL· GenBank· DDBJ | AAF05908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF169360 EMBL· GenBank· DDBJ | AAF05908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF169361 EMBL· GenBank· DDBJ | AAF05908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF169362 EMBL· GenBank· DDBJ | AAF05908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF169363 EMBL· GenBank· DDBJ | AAF05908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF169364 EMBL· GenBank· DDBJ | AAF05908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF169365 EMBL· GenBank· DDBJ | AAF05908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF200465 EMBL· GenBank· DDBJ | AAF24344.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY072910 EMBL· GenBank· DDBJ | AAL68878.1 EMBL· GenBank· DDBJ | mRNA | ||
AY072911 EMBL· GenBank· DDBJ | AAL68879.1 EMBL· GenBank· DDBJ | mRNA | ||
AY072912 EMBL· GenBank· DDBJ | AAL68880.1 EMBL· GenBank· DDBJ | mRNA | ||
AF242865 EMBL· GenBank· DDBJ | AAG01088.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF242862 EMBL· GenBank· DDBJ | AAG01088.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF242864 EMBL· GenBank· DDBJ | AAG01088.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
GU474812 EMBL· GenBank· DDBJ | ADC84500.1 EMBL· GenBank· DDBJ | mRNA | ||
CR617256 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BT019876 EMBL· GenBank· DDBJ | AAV38679.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313526 EMBL· GenBank· DDBJ | BAG36305.1 EMBL· GenBank· DDBJ | mRNA | ||
AP000963 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP000967 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471079 EMBL· GenBank· DDBJ | EAX10031.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003684 EMBL· GenBank· DDBJ | AAH03684.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010536 EMBL· GenBank· DDBJ | AAH10536.1 EMBL· GenBank· DDBJ | mRNA | ||
AF124598 EMBL· GenBank· DDBJ | AAD31772.1 EMBL· GenBank· DDBJ | mRNA |