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Coxsackievirus and adenovirus receptor homolog (CAR) (rCAR)

 CXAR_RAT                Reviewed;         365 AA.
Q9R066; Q5M817; Q9R067;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
10-MAY-2017, entry version 127.
RecName: Full=Coxsackievirus and adenovirus receptor homolog;
Short=CAR;
Short=rCAR;
Flags: Precursor;
Name=Cxadr; Synonyms=Car;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
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.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-358 (ISOFORM 1), PARTIAL NUCLEOTIDE
SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Liver;
PubMed=10490761; DOI=10.1038/sj.gt.3301030;
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.;
"Expression of Coxsackie-adenovirus-receptor and alpha v-integrin does
not correlate with adenovector targeting in vivo indicating anatomical
vector barriers.";
Gene Ther. 6:1520-1535(1999).
[3]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-332, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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).
{ECO:0000250}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
protein {ECO:0000255}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
protein {ECO:0000255}. Cell junction, tight junction
{ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:P78310}. 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.
{ECO:0000250|UniProtKB:P78310}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9R066-1; Sequence=Displayed;
Name=2;
IsoId=Q9R066-2; Sequence=VSP_014815, VSP_014816;
-!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung,
liver, muscle, kidney, testis, spleen and skeletal muscle.
{ECO:0000269|PubMed:10490761}.
-!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
interaction with JAML. {ECO:0000250}.
-!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and
BAIAP1. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper
localization to the plasma membrane. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AABR03078554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03079390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF109643; AAF01254.1; -; mRNA.
EMBL; AF109644; AAF01255.1; -; mRNA.
EMBL; BC088313; AAH88313.1; -; mRNA.
RefSeq; NP_446022.1; NM_053570.1. [Q9R066-2]
RefSeq; XP_006248062.1; XM_006248000.3. [Q9R066-1]
UniGene; Rn.113837; -.
ProteinModelPortal; Q9R066; -.
SMR; Q9R066; -.
STRING; 10116.ENSRNOP00000041873; -.
iPTMnet; Q9R066; -.
PhosphoSitePlus; Q9R066; -.
SwissPalm; Q9R066; -.
PaxDb; Q9R066; -.
PRIDE; Q9R066; -.
Ensembl; ENSRNOT00000050701; ENSRNOP00000041873; ENSRNOG00000001557. [Q9R066-2]
GeneID; 89843; -.
KEGG; rno:89843; -.
UCSC; RGD:619794; rat. [Q9R066-1]
CTD; 1525; -.
RGD; 619794; Cxadr.
eggNOG; ENOG410IGDG; Eukaryota.
eggNOG; ENOG4110WP1; LUCA.
GeneTree; ENSGT00760000119145; -.
HOGENOM; HOG000111222; -.
HOVERGEN; HBG105787; -.
InParanoid; Q9R066; -.
KO; K06788; -.
OMA; VGNKKIQ; -.
OrthoDB; EOG091G05PI; -.
PhylomeDB; Q9R066; -.
TreeFam; TF330875; -.
PRO; PR:Q9R066; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001557; -.
Genevisible; Q9R066; RN.
GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0044297; C:cell body; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
GO; GO:0071253; F:connexin binding; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISS:UniProtKB.
GO; GO:0086072; P:AV node cell-bundle of His cell adhesion involved in cell communication; IEA:Ensembl.
GO; GO:0048739; P:cardiac muscle fiber development; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
GO; GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB.
GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0098904; P:regulation of AV node cell action potential; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Tight junction; Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 365 Coxsackievirus and adenovirus receptor
homolog.
/FTId=PRO_0000014742.
TOPO_DOM 20 238 Extracellular. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 136 Ig-like C2-type 1.
DOMAIN 141 228 Ig-like C2-type 2.
MOTIF 360 365 PDZ-binding. {ECO:0000250}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:P78310}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
LIPID 259 259 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 260 260 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 120 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 146 223 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 162 212 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 340 352 VAAPNLSRMGAVP -> FKYAYLTDGIAVV (in
isoform 2). {ECO:0000305}.
/FTId=VSP_014815.
VAR_SEQ 353 365 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_014816.
SEQUENCE 365 AA; 39949 MW; 66D34B92B7F97363 CRC64;
MALLLCFVLL CGVADFTSSL SITTPEQRIE KAKGETAYLP CKFTLEPEDQ GPLDIEWLIS
PSDNQKVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC
KVKKAPGVAN RKFLLTVLVK PSGTRCFVDG SGEIGNDFKL KCEPKEGSLP LQYEWQKLSD
SQKMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA
GAVIGTLLAL VLIGAILFCC HKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA VPVMIPAQSK
DGSIV


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