CXAR_RAT
ID CXAR_RAT Reviewed; 365 AA.
AC Q9R066; Q5M817; Q9R067;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Coxsackievirus and adenovirus receptor homolog;
DE Short=CAR;
DE Short=rCAR;
DE Flags: Precursor;
GN Name=Cxadr; Synonyms=Car;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-358 (ISOFORM 1), PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=10490761; DOI=10.1038/sj.gt.3301030;
RA Fechner H., Haack A., Wang H., Wang X., Eizema K., Pauschinger M.,
RA Schoemaker R.G., van Veghel R., Houtsmuller A.B., Schultheiss H.-P.,
RA Lamers J.M.J., Poller W.;
RT "Expression of Coxsackie-adenovirus-receptor and alpha v-integrin does not
RT correlate with adenovector targeting in vivo indicating anatomical vector
RT barriers.";
RL Gene Ther. 6:1520-1535(1999).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-332, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the epithelial apical junction complex that may
CC function as a homophilic cell adhesion molecule and is essential for
CC tight junction integrity. Also involved in transepithelial migration of
CC leukocytes through adhesive interactions with JAML a transmembrane
CC protein of the plasma membrane of leukocytes. The interaction between
CC both receptors also mediates the activation of gamma-delta T-cells, a
CC subpopulation of T-cells residing in epithelia and involved in tissue
CC homeostasis and repair. Upon epithelial CXADR-binding, JAML induces
CC downstream cell signaling events in gamma-delta T-cells through PI3-
CC kinase and MAP kinases. It results in proliferation and production of
CC cytokines and growth factors by T-cells that in turn stimulate
CC epithelial tissues repair (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. May form homodimer. Interacts with LNX, MAGI1, DLG4,
CC PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ to
CC intercellular contact sites. Interacts with JAML (homodimeric form) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P78310};
CC Single-pass type I membrane protein {ECO:0000255}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
CC protein {ECO:0000255}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P78310}. Note=In epithelial cells localizes to
CC the apical junction complex composed of tight and adherens junctions.
CC In airway epithelial cells localized to basolateral membrane but not to
CC apical surface. {ECO:0000250|UniProtKB:P78310}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9R066-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R066-2; Sequence=VSP_014815, VSP_014816;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC muscle, kidney, testis, spleen and skeletal muscle.
CC {ECO:0000269|PubMed:10490761}.
CC -!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
CC interaction with JAML. {ECO:0000250}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and MAGI1.
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper
CC localization to the plasma membrane. {ECO:0000250}.
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DR EMBL; AABR03078554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03079390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF109643; AAF01254.1; -; mRNA.
DR EMBL; AF109644; AAF01255.1; -; mRNA.
DR EMBL; BC088313; AAH88313.1; -; mRNA.
DR RefSeq; NP_446022.1; NM_053570.1. [Q9R066-2]
DR RefSeq; XP_006248062.1; XM_006248000.3. [Q9R066-1]
DR AlphaFoldDB; Q9R066; -.
DR SMR; Q9R066; -.
DR STRING; 10116.ENSRNOP00000041873; -.
DR GlyGen; Q9R066; 1 site.
DR iPTMnet; Q9R066; -.
DR PhosphoSitePlus; Q9R066; -.
DR SwissPalm; Q9R066; -.
DR PaxDb; Q9R066; -.
DR PRIDE; Q9R066; -.
DR Ensembl; ENSRNOT00000050701; ENSRNOP00000041873; ENSRNOG00000001557. [Q9R066-2]
DR GeneID; 89843; -.
DR KEGG; rno:89843; -.
DR UCSC; RGD:619794; rat. [Q9R066-1]
DR CTD; 1525; -.
DR RGD; 619794; Cxadr.
DR VEuPathDB; HostDB:ENSRNOG00000001557; -.
DR eggNOG; ENOG502QSG0; Eukaryota.
DR GeneTree; ENSGT00940000154829; -.
DR HOGENOM; CLU_040549_0_0_1; -.
DR InParanoid; Q9R066; -.
DR OMA; CQFTLAP; -.
DR OrthoDB; 896005at2759; -.
DR PhylomeDB; Q9R066; -.
DR TreeFam; TF330875; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:Q9R066; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001557; Expressed in jejunum and 18 other tissues.
DR Genevisible; Q9R066; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0071253; F:connexin binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISS:UniProtKB.
DR GO; GO:0086072; P:AV node cell-bundle of His cell adhesion involved in cell communication; ISO:RGD.
DR GO; GO:0055013; P:cardiac muscle cell development; ISS:UniProtKB.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0098904; P:regulation of AV node cell action potential; ISO:RGD.
DR GO; GO:0070633; P:transepithelial transport; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..365
FT /note="Coxsackievirus and adenovirus receptor homolog"
FT /id="PRO_0000014742"
FT TOPO_DOM 20..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..136
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..228
FT /note="Ig-like C2-type 2"
FT REGION 269..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..365
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 269..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97792"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97792"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78310"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97792"
FT LIPID 259
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 260
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 340..352
FT /note="VAAPNLSRMGAVP -> FKYAYLTDGIAVV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014815"
FT VAR_SEQ 353..365
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014816"
SQ 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
