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Protein

Coxsackievirus and adenovirus receptor homolog

Gene

Cxadr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair.4 Publications

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB
  • cell adhesive protein binding involved in AV node cell-bundle of His cell communication Source: BHF-UCL
  • connexin binding Source: UniProtKB
  • integrin binding Source: MGI
  • PDZ domain binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • AV node cell-bundle of His cell adhesion involved in cell communication Source: BHF-UCL
  • AV node cell to bundle of His cell communication Source: UniProtKB
  • cardiac muscle fiber development Source: MGI
  • cell-cell junction organization Source: MGI
  • epithelial structure maintenance Source: UniProtKB
  • gamma-delta T cell activation Source: UniProtKB
  • germ cell migration Source: UniProtKB
  • heart development Source: MGI
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • homotypic cell-cell adhesion Source: UniProtKB
  • mitochondrion organization Source: MGI
  • negative regulation of cardiac muscle cell proliferation Source: MGI
  • neutrophil chemotaxis Source: UniProtKB
  • positive regulation of epithelial cell proliferation involved in wound healing Source: UniProtKB
  • regulation of AV node cell action potential Source: BHF-UCL
  • single organismal cell-cell adhesion Source: UniProtKB
  • transepithelial transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Coxsackievirus and adenovirus receptor homolog
Short name:
CAR
Short name:
mCAR
Gene namesi
Name:Cxadr
Synonyms:Car
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1201679. Cxadr.

Subcellular locationi

Isoform 1 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 237ExtracellularSequence analysisAdd BLAST218
Transmembranei238 – 258HelicalSequence analysisAdd BLAST21
Topological domaini259 – 365CytoplasmicSequence analysisAdd BLAST107

GO - Cellular componenti

  • acrosomal vesicle Source: MGI
  • adherens junction Source: UniProtKB
  • apicolateral plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB
  • bicellular tight junction Source: UniProtKB
  • cell body Source: UniProtKB
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • cell surface Source: GO_Central
  • cytoplasm Source: UniProtKB
  • extracellular region Source: UniProtKB-SubCell
  • filopodium Source: UniProtKB
  • growth cone Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intercalated disc Source: UniProtKB
  • membrane raft Source: UniProtKB
  • neuron projection Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001474020 – 365Coxsackievirus and adenovirus receptor homologAdd BLAST346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 120Combined sources2 Publications
Glycosylationi106N-linked (GlcNAc...)1 Publication1
Disulfide bondi146 ↔ 223Combined sources2 Publications
Disulfide bondi162 ↔ 212Combined sources2 Publications
Lipidationi259S-palmitoyl cysteineBy similarity1
Lipidationi260S-palmitoyl cysteineBy similarity1
Modified residuei297PhosphoserineCombined sources1
Modified residuei304PhosphoserineCombined sources1
Modified residuei306PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Modified residuei332PhosphoserineBy similarity1
Modified residuei363PhosphoserineCombined sources1

Post-translational modificationi

Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP97792.
PaxDbiP97792.
PeptideAtlasiP97792.
PRIDEiP97792.

PTM databases

iPTMnetiP97792.
PhosphoSitePlusiP97792.
SwissPalmiP97792.

Expressioni

Tissue specificityi

Expressed in liver, kidney, heart, lung, and brain. In skeletal muscle is found at the neuromuscular junction. In cardiac muscle, isoform 1 and isoform 2 are found at intercalated disks.4 Publications

Developmental stagei

Expression starts in the embryonic ectoderm in the uterus on E6.5. Then it is strongly expressed in the neuroepithelium of the neural tube, the developing brain and the spinal cord from E8.5 to postnatal day 7 (P7), in the cranial motor nerves from E9.5 to E11.5, and in the optic nerve from E13.5 to P7. Expression increases until perinatal period and decreases postnatally. Expressed in the immature neuroepithelium including progenitor cells it still occurs in a few proliferating cells of the hippocampal dentate gyrus, the subventricular zone of the lateral ventricles, and the rostral migratory stream over P21. Also expressed in heart, kidney and liver of newborn mice.2 Publications

Gene expression databases

BgeeiENSMUSG00000022865.
CleanExiMM_CXADR.
GenevisibleiP97792. MM.

Interactioni

Subunit structurei

Monomer. May form homodimer. Interacts with LNX, BAIAP1, DLG4, PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ to intercellular contact sites. Interacts with JAML (homodimeric form).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ActbP607106EBI-7429264,EBI-353957

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB
  • cell adhesive protein binding involved in AV node cell-bundle of His cell communication Source: BHF-UCL
  • connexin binding Source: UniProtKB
  • integrin binding Source: MGI
  • PDZ domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198986. 1 interactor.
DIPiDIP-41457N.
IntActiP97792. 2 interactors.
MINTiMINT-253068.
STRINGi10090.ENSMUSP00000023572.

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 32Combined sources7
Beta strandi37 – 39Combined sources3
Beta strandi54 – 65Combined sources12
Beta strandi68 – 75Combined sources8
Beta strandi78 – 80Combined sources3
Helixi85 – 87Combined sources3
Turni88 – 90Combined sources3
Beta strandi91 – 94Combined sources4
Helixi98 – 100Combined sources3
Beta strandi105 – 107Combined sources3
Helixi112 – 114Combined sources3
Beta strandi116 – 124Combined sources9
Beta strandi127 – 138Combined sources12
Beta strandi145 – 150Combined sources6
Beta strandi158 – 163Combined sources6
Beta strandi172 – 177Combined sources6
Helixi186 – 191Combined sources6
Beta strandi194 – 199Combined sources6
Helixi204 – 206Combined sources3
Beta strandi208 – 215Combined sources8
Beta strandi220 – 227Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JZ7X-ray2.19A20-233[»]
3MJ7X-ray2.80B18-236[»]
ProteinModelPortaliP97792.
SMRiP97792.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97792.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 136Ig-like C2-type 1Add BLAST117
Domaini141 – 228Ig-like C2-type 2Add BLAST88

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi360 – 365PDZ-bindingBy similarity6

Domaini

The Ig-like C2-type 1 domain mediates homodimerization and interaction with JAML.1 Publication
The PDZ-binding motif mediates interaction with MPDZ and BAIAP1.By similarity

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IGDG. Eukaryota.
ENOG4110WP1. LUCA.
GeneTreeiENSGT00760000119145.
HOGENOMiHOG000111222.
HOVERGENiHBG105787.
InParanoidiP97792.
KOiK06788.
OMAiVGNKKIQ.
OrthoDBiEOG091G05PI.
PhylomeDBiP97792.
TreeFamiTF330875.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P97792-1) [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
MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ
60 70 80 90 100
GPLDIEWLIS PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS
110 120 130 140 150
GDASINVTNL QLSDIGTYQC KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG
160 170 180 190 200
SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD SQTMPTPWLA EMTSPVISVK
210 220 230 240 250
NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA GAVIGTLLAL
260 270 280 290 300
VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
310 320 330 340 350
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA
360
VPVMIPAQSK DGSIV
Length:365
Mass (Da):39,948
Last modified:May 1, 1997 - v1
Checksum:i5445B4B52A34B2A2
GO
Isoform 2 (identifier: P97792-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-365: VAAPNLSRMGAVPVMIPAQSKDGSIV → FKYAYKTDGITVV

Show »
Length:352
Mass (Da):38,843
Checksum:i2BD8CBD25D8CE123
GO
Isoform 3 (identifier: P97792-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-164: VKPSGTRCFVDGSEEIGNDFKLKCEP → GKSSFLLSTGVEWGGGAELQGGREGG
     165-365: Missing.

Show »
Length:164
Mass (Da):17,781
Checksum:i9DEFCBD456240C73
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_014827139 – 164VKPSG…LKCEP → GKSSFLLSTGVEWGGGAELQ GGREGG in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_014828165 – 365Missing in isoform 3. 1 PublicationAdd BLAST201
Alternative sequenceiVSP_014829340 – 365VAAPN…DGSIV → FKYAYKTDGITVV in isoform 2. 3 PublicationsAdd BLAST26

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90715 mRNA. Translation: AAC53148.1.
Y10320 mRNA. Translation: CAA71368.1.
Y11929 mRNA. Translation: CAA72679.1.
AK004908 mRNA. Translation: BAB23660.2.
AK145569 mRNA. Translation: BAE26518.1.
BC004680 mRNA. Translation: AAH04680.1.
BC016457 mRNA. Translation: AAH16457.1.
CCDSiCCDS28276.1. [P97792-1]
CCDS37379.1. [P97792-2]
RefSeqiNP_001020363.1. NM_001025192.3. [P97792-1]
NP_001263192.1. NM_001276263.1. [P97792-3]
NP_034118.1. NM_009988.4. [P97792-2]
XP_006522946.1. XM_006522883.3. [P97792-1]
XP_006522947.1. XM_006522884.3. [P97792-2]
UniGeneiMm.66222.

Genome annotation databases

EnsembliENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865. [P97792-1]
ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865. [P97792-2]
GeneIDi13052.
KEGGimmu:13052.
UCSCiuc007zsm.2. mouse. [P97792-3]
uc007zsn.2. mouse. [P97792-1]
uc007zso.2. mouse. [P97792-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90715 mRNA. Translation: AAC53148.1.
Y10320 mRNA. Translation: CAA71368.1.
Y11929 mRNA. Translation: CAA72679.1.
AK004908 mRNA. Translation: BAB23660.2.
AK145569 mRNA. Translation: BAE26518.1.
BC004680 mRNA. Translation: AAH04680.1.
BC016457 mRNA. Translation: AAH16457.1.
CCDSiCCDS28276.1. [P97792-1]
CCDS37379.1. [P97792-2]
RefSeqiNP_001020363.1. NM_001025192.3. [P97792-1]
NP_001263192.1. NM_001276263.1. [P97792-3]
NP_034118.1. NM_009988.4. [P97792-2]
XP_006522946.1. XM_006522883.3. [P97792-1]
XP_006522947.1. XM_006522884.3. [P97792-2]
UniGeneiMm.66222.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JZ7X-ray2.19A20-233[»]
3MJ7X-ray2.80B18-236[»]
ProteinModelPortaliP97792.
SMRiP97792.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198986. 1 interactor.
DIPiDIP-41457N.
IntActiP97792. 2 interactors.
MINTiMINT-253068.
STRINGi10090.ENSMUSP00000023572.

PTM databases

iPTMnetiP97792.
PhosphoSitePlusiP97792.
SwissPalmiP97792.

Proteomic databases

MaxQBiP97792.
PaxDbiP97792.
PeptideAtlasiP97792.
PRIDEiP97792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865. [P97792-1]
ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865. [P97792-2]
GeneIDi13052.
KEGGimmu:13052.
UCSCiuc007zsm.2. mouse. [P97792-3]
uc007zsn.2. mouse. [P97792-1]
uc007zso.2. mouse. [P97792-2]

Organism-specific databases

CTDi1525.
MGIiMGI:1201679. Cxadr.

Phylogenomic databases

eggNOGiENOG410IGDG. Eukaryota.
ENOG4110WP1. LUCA.
GeneTreeiENSGT00760000119145.
HOGENOMiHOG000111222.
HOVERGENiHBG105787.
InParanoidiP97792.
KOiK06788.
OMAiVGNKKIQ.
OrthoDBiEOG091G05PI.
PhylomeDBiP97792.
TreeFamiTF330875.

Miscellaneous databases

ChiTaRSiCxadr. mouse.
EvolutionaryTraceiP97792.
PROiP97792.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022865.
CleanExiMM_CXADR.
GenevisibleiP97792. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCXAR_MOUSE
AccessioniPrimary (citable) accession number: P97792
Secondary accession number(s): O09052
, Q3ULD0, Q91W66, Q99KG0, Q9DBJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.