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Protein

Coxsackievirus and adenovirus receptor homolog

Gene

Cxadr

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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:
rCAR
Gene namesi
Name:Cxadr
Synonyms:Car
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi619794. Cxadr.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Basolateral cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell junctiontight junction By similarity
  • Cell junctionadherens junction By similarity

  • Note: In epithelial cells localizes to the apical junction complex composed of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 238219ExtracellularSequence analysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Topological domaini260 – 365106CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 365346Coxsackievirus and adenovirus receptor homologPRO_0000014742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 120PROSITE-ProRule annotation
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi146 ↔ 223PROSITE-ProRule annotation
Disulfide bondi162 ↔ 212PROSITE-ProRule annotation
Lipidationi259 – 2591S-palmitoyl cysteineBy similarity
Lipidationi260 – 2601S-palmitoyl cysteineBy similarity
Modified residuei297 – 2971PhosphoserineBy similarity
Modified residuei304 – 3041PhosphoserineBy similarity
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei323 – 3231PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineCombined sources
Modified residuei363 – 3631PhosphoserineBy similarity

Post-translational modificationi

N-glycosylated.By similarity
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

PaxDbiQ9R066.
PRIDEiQ9R066.

PTM databases

SwissPalmiQ9R066.

Expressioni

Tissue specificityi

Expressed in heart, brain, spleen, lung, liver, muscle, kidney, testis, spleen and skeletal muscle.1 Publication

Gene expression databases

GenevisibleiQ9R066. RN.

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) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000041873.

Structurei

3D structure databases

ProteinModelPortaliQ9R066.
SMRiQ9R066. Positions 21-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 136117Ig-like C2-type 1Add
BLAST
Domaini141 – 22888Ig-like C2-type 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi360 – 3656PDZ-bindingBy similarity

Domaini

The Ig-like C2-type 1 domain mediates homodimerization and interaction with JAML.By similarity
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.
InParanoidiQ9R066.
KOiK06788.
OMAiVGNKKIQ.
OrthoDBiEOG7MH0Z1.
PhylomeDBiQ9R066.
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 (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: Q9R066-1) [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
MALLLCFVLL CGVADFTSSL SITTPEQRIE KAKGETAYLP CKFTLEPEDQ
60 70 80 90 100
GPLDIEWLIS PSDNQKVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS
110 120 130 140 150
GDASINVTNL QLSDIGTYQC KVKKAPGVAN RKFLLTVLVK PSGTRCFVDG
160 170 180 190 200
SGEIGNDFKL KCEPKEGSLP LQYEWQKLSD SQKMPTPWLA EMTSPVISVK
210 220 230 240 250
NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA GAVIGTLLAL
260 270 280 290 300
VLIGAILFCC HKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
310 320 330 340 350
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA
360
VPVMIPAQSK DGSIV
Length:365
Mass (Da):39,949
Last modified:July 19, 2005 - v2
Checksum:i66D34B92B7F97363
GO
Isoform 2 (identifier: Q9R066-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-352: VAAPNLSRMGAVP → FKYAYLTDGIAVV
     353-365: Missing.

Show »
Length:352
Mass (Da):38,799
Checksum:iAC3A0D35EED8C866
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei340 – 35213VAAPN…MGAVP → FKYAYLTDGIAVV in isoform 2. CuratedVSP_014815Add
BLAST
Alternative sequencei353 – 36513Missing in isoform 2. CuratedVSP_014816Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03078554 Genomic DNA. No translation available.
AABR03079390 Genomic DNA. No translation available.
AF109643 mRNA. Translation: AAF01254.1.
AF109644 mRNA. Translation: AAF01255.1.
BC088313 mRNA. Translation: AAH88313.1.
RefSeqiNP_446022.1. NM_053570.1. [Q9R066-2]
XP_006248062.1. XM_006248000.2. [Q9R066-1]
UniGeneiRn.113837.

Genome annotation databases

EnsembliENSRNOT00000050701; ENSRNOP00000041873; ENSRNOG00000001557. [Q9R066-2]
GeneIDi89843.
KEGGirno:89843.
UCSCiRGD:619794. rat. [Q9R066-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03078554 Genomic DNA. No translation available.
AABR03079390 Genomic DNA. No translation available.
AF109643 mRNA. Translation: AAF01254.1.
AF109644 mRNA. Translation: AAF01255.1.
BC088313 mRNA. Translation: AAH88313.1.
RefSeqiNP_446022.1. NM_053570.1. [Q9R066-2]
XP_006248062.1. XM_006248000.2. [Q9R066-1]
UniGeneiRn.113837.

3D structure databases

ProteinModelPortaliQ9R066.
SMRiQ9R066. Positions 21-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000041873.

PTM databases

SwissPalmiQ9R066.

Proteomic databases

PaxDbiQ9R066.
PRIDEiQ9R066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000050701; ENSRNOP00000041873; ENSRNOG00000001557. [Q9R066-2]
GeneIDi89843.
KEGGirno:89843.
UCSCiRGD:619794. rat. [Q9R066-1]

Organism-specific databases

CTDi1525.
RGDi619794. Cxadr.

Phylogenomic databases

eggNOGiENOG410IGDG. Eukaryota.
ENOG4110WP1. LUCA.
GeneTreeiENSGT00760000119145.
HOGENOMiHOG000111222.
HOVERGENiHBG105787.
InParanoidiQ9R066.
KOiK06788.
OMAiVGNKKIQ.
OrthoDBiEOG7MH0Z1.
PhylomeDBiQ9R066.
TreeFamiTF330875.

Miscellaneous databases

NextBioi617772.
PROiQ9R066.

Gene expression databases

GenevisibleiQ9R066. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Expression of Coxsackie-adenovirus-receptor and alpha v-integrin does not correlate with adenovector targeting in vivo indicating anatomical vector barriers."
    Fechner H., Haack A., Wang H., Wang X., Eizema K., Pauschinger M., Schoemaker R.G., van Veghel R., Houtsmuller A.B., Schultheiss H.-P., Lamers J.M.J., Poller W.
    Gene Ther. 6:1520-1535(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-358 (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCXAR_RAT
AccessioniPrimary (citable) accession number: Q9R066
Secondary accession number(s): Q5M817, Q9R067
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 11, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.