CXAR_MOUSE
ID CXAR_MOUSE Reviewed; 365 AA.
AC P97792; O09052; Q3ULD0; Q91W66; Q99KG0; Q9DBJ8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Coxsackievirus and adenovirus receptor homolog;
DE Short=CAR;
DE Short=mCAR;
DE Flags: Precursor;
GN Name=Cxadr; Synonyms=Car;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=C3H/Mai;
RX PubMed=9096397; DOI=10.1073/pnas.94.7.3352;
RA Tomko R.P., Xu R., Philipson L.;
RT "HCAR and MCAR: the human and mouse cellular receptors for subgroup C
RT adenoviruses and group B coxsackieviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3352-3356(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRUS RECEPTOR.
RC STRAIN=C57BL/6J; TISSUE=Colon, and Liver;
RX PubMed=9036860; DOI=10.1126/science.275.5304.1320;
RA Bergelson J.M., Cunningham J.A., Droguett G., Kurt-Jones E., Krithivas A.,
RA Hong J.S., Horwitz M.S., Crowell R.L., Finberg R.W.;
RT "Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2
RT and 5.";
RL Science 275:1320-1323(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION AS A VIRUS RECEPTOR.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=9420240; DOI=10.1128/jvi.72.1.415-419.1998;
RA Bergelson J.M., Krithivas A., Celi L., Droguett G., Horwitz M.S.,
RA Wickham T., Crowell R.L., Finberg R.W.;
RT "The murine CAR homolog is a receptor for coxsackie B viruses and
RT adenoviruses.";
RL J. Virol. 72:415-419(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION, AND FUNCTION.
RX PubMed=10814828; DOI=10.1016/s0169-328x(00)00036-x;
RA Honda T., Saitoh H., Masuko M., Katagiri-Abe T., Tominaga K., Kozakai I.,
RA Kobayashi K., Kumanishi T., Watanabe Y.G., Odani S., Kuwano R.;
RT "The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule
RT in the developing mouse brain.";
RL Brain Res. Mol. Brain Res. 77:19-28(2000).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12763576; DOI=10.1016/s0165-3806(03)00035-x;
RA Hotta Y., Honda T., Naito M., Kuwano R.;
RT "Developmental distribution of coxsackie virus and adenovirus receptor
RT localized in the nervous system.";
RL Brain Res. Dev. Brain Res. 143:1-13(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15533241; DOI=10.1186/1471-2121-5-42;
RA Shaw C.A., Holland P.C., Sinnreich M., Allen C., Sollerbrant K.,
RA Karpati G., Nalbantoglu J.;
RT "Isoform-specific expression of the Coxsackie and adenovirus receptor (CAR)
RT in neuromuscular junction and cardiac intercalated discs.";
RL BMC Cell Biol. 5:42-42(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-304; SER-306;
RP SER-323 AND SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION IN T-CELL ACTIVATION, AND INTERACTION WITH CXADR.
RX PubMed=20813954; DOI=10.1126/science.1192698;
RA Witherden D.A., Verdino P., Rieder S.E., Garijo O., Mills R.E., Teyton L.,
RA Fischer W.H., Wilson I.A., Havran W.L.;
RT "The junctional adhesion molecule JAML is a costimulatory receptor for
RT epithelial gammadelta T cell activation.";
RL Science 329:1205-1210(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 20-233, AND DISULFIDE BONDS.
RX PubMed=20181587; DOI=10.1523/jneurosci.5725-09.2010;
RA Patzke C., Max K.E., Behlke J., Schreiber J., Schmidt H., Dorner A.A.,
RA Kroger S., Henning M., Otto A., Heinemann U., Rathjen F.G.;
RT "The coxsackievirus-adenovirus receptor reveals complex homophilic and
RT heterophilic interactions on neural cells.";
RL J. Neurosci. 30:2897-2910(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-236 IN COMPLEX WITH JAML,
RP DOMAIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-106.
RX PubMed=20813955; DOI=10.1126/science.1187996;
RA Verdino P., Witherden D.A., Havran W.L., Wilson I.A.;
RT "The molecular interaction of CAR and JAML recruits the central cell signal
RT transducer PI3K.";
RL Science 329:1210-1214(2010).
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. {ECO:0000269|PubMed:10814828,
CC ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:9036860,
CC ECO:0000269|PubMed:9420240}.
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).
CC {ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:20813955}.
CC -!- INTERACTION:
CC P97792; P60710: Actb; NbExp=6; IntAct=EBI-7429264, EBI-353957;
CC P97792-1; P19793: RXRA; Xeno; NbExp=2; IntAct=EBI-15903843, EBI-78598;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:15533241}; Single-pass type I membrane protein
CC {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane protein
CC {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 -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P97792-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97792-2; Sequence=VSP_014829;
CC Name=3;
CC IsoId=P97792-3; Sequence=VSP_014827, VSP_014828;
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, heart, lung, and brain.
CC In skeletal muscle is found at the neuromuscular junction. In cardiac
CC muscle, isoform 1 and isoform 2 are found at intercalated disks.
CC {ECO:0000269|PubMed:10814828, ECO:0000269|PubMed:12763576,
CC ECO:0000269|PubMed:15533241, ECO:0000269|PubMed:9096397}.
CC -!- DEVELOPMENTAL STAGE: Expression starts in the embryonic ectoderm in the
CC uterus on 6.5 dpc. Then it is strongly expressed in the neuroepithelium
CC of the neural tube, the developing brain and the spinal cord from 8.5
CC dpc to postnatal day 7 (P7), in the cranial motor nerves from 9.5 dpc
CC to 11.5 dpc, and in the optic nerve from 13.5 dpc to P7. Expression
CC increases until perinatal period and decreases postnatally. Expressed
CC in the immature neuroepithelium including progenitor cells it still
CC occurs in a few proliferating cells of the hippocampal dentate gyrus,
CC the subventricular zone of the lateral ventricles, and the rostral
CC migratory stream over P21. Also expressed in heart, kidney and liver of
CC newborn mice. {ECO:0000269|PubMed:10814828,
CC ECO:0000269|PubMed:12763576}.
CC -!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
CC interaction with JAML. {ECO:0000269|PubMed:20813955}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and MAGI1.
CC {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; U90715; AAC53148.1; -; mRNA.
DR EMBL; Y10320; CAA71368.1; -; mRNA.
DR EMBL; Y11929; CAA72679.1; -; mRNA.
DR EMBL; AK004908; BAB23660.2; -; mRNA.
DR EMBL; AK145569; BAE26518.1; -; mRNA.
DR EMBL; BC004680; AAH04680.1; -; mRNA.
DR EMBL; BC016457; AAH16457.1; -; mRNA.
DR CCDS; CCDS28276.1; -. [P97792-1]
DR CCDS; CCDS37379.1; -. [P97792-2]
DR CCDS; CCDS88952.1; -. [P97792-3]
DR RefSeq; NP_001020363.1; NM_001025192.3. [P97792-1]
DR RefSeq; NP_001263192.1; NM_001276263.1. [P97792-3]
DR RefSeq; NP_034118.1; NM_009988.4. [P97792-2]
DR RefSeq; XP_006522946.1; XM_006522883.3. [P97792-1]
DR RefSeq; XP_006522947.1; XM_006522884.3. [P97792-2]
DR PDB; 3JZ7; X-ray; 2.19 A; A=20-233.
DR PDB; 3MJ7; X-ray; 2.80 A; B=18-236.
DR PDBsum; 3JZ7; -.
DR PDBsum; 3MJ7; -.
DR AlphaFoldDB; P97792; -.
DR SMR; P97792; -.
DR BioGRID; 198986; 2.
DR CORUM; P97792; -.
DR DIP; DIP-41457N; -.
DR IntAct; P97792; 4.
DR MINT; P97792; -.
DR STRING; 10090.ENSMUSP00000023572; -.
DR GlyConnect; 2238; 1 N-Linked glycan (1 site).
DR GlyGen; P97792; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P97792; -.
DR PhosphoSitePlus; P97792; -.
DR SwissPalm; P97792; -.
DR EPD; P97792; -.
DR jPOST; P97792; -.
DR MaxQB; P97792; -.
DR PaxDb; P97792; -.
DR PeptideAtlas; P97792; -.
DR PRIDE; P97792; -.
DR ProteomicsDB; 277926; -. [P97792-1]
DR ProteomicsDB; 277927; -. [P97792-2]
DR ProteomicsDB; 277928; -. [P97792-3]
DR DNASU; 13052; -.
DR Ensembl; ENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865. [P97792-1]
DR Ensembl; ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865. [P97792-2]
DR Ensembl; ENSMUST00000231356; ENSMUSP00000156281; ENSMUSG00000022865. [P97792-3]
DR GeneID; 13052; -.
DR KEGG; mmu:13052; -.
DR UCSC; uc007zsm.2; mouse. [P97792-3]
DR UCSC; uc007zsn.2; mouse. [P97792-1]
DR UCSC; uc007zso.2; mouse. [P97792-2]
DR CTD; 1525; -.
DR MGI; MGI:1201679; Cxadr.
DR VEuPathDB; HostDB:ENSMUSG00000022865; -.
DR eggNOG; ENOG502QSG0; Eukaryota.
DR GeneTree; ENSGT00940000154829; -.
DR HOGENOM; CLU_040549_0_0_1; -.
DR InParanoid; P97792; -.
DR OMA; CQFTLAP; -.
DR OrthoDB; 896005at2759; -.
DR PhylomeDB; P97792; -.
DR TreeFam; TF330875; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 13052; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cxadr; mouse.
DR EvolutionaryTrace; P97792; -.
DR PRO; PR:P97792; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P97792; protein.
DR Bgee; ENSMUSG00000022865; Expressed in cortical plate and 280 other tissues.
DR ExpressionAtlas; P97792; baseline and differential.
DR Genevisible; P97792; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0086082; F:cell adhesive protein binding involved in AV node cell-bundle of His cell communication; IC:BHF-UCL.
DR GO; GO:0071253; F:connexin binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0086067; P:AV node cell to bundle of His cell communication; IMP:UniProtKB.
DR GO; GO:0086072; P:AV node cell-bundle of His cell adhesion involved in cell communication; IMP:BHF-UCL.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0046629; P:gamma-delta T cell activation; IDA:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IEP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IC:UniProtKB.
DR GO; GO:0098904; P:regulation of AV node cell action potential; IMP:BHF-UCL.
DR GO; GO:0070633; P:transepithelial transport; ISO:MGI.
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 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Tight junction;
KW 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_0000014740"
FT TOPO_DOM 20..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..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:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78310"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000269|PubMed:20813955"
FT DISULFID 41..120
FT /evidence="ECO:0000269|PubMed:20181587,
FT ECO:0000269|PubMed:20813955, ECO:0007744|PDB:3JZ7,
FT ECO:0007744|PDB:3MJ7"
FT DISULFID 146..223
FT /evidence="ECO:0000269|PubMed:20181587,
FT ECO:0000269|PubMed:20813955, ECO:0007744|PDB:3JZ7,
FT ECO:0007744|PDB:3MJ7"
FT DISULFID 162..212
FT /evidence="ECO:0000269|PubMed:20181587,
FT ECO:0000269|PubMed:20813955, ECO:0007744|PDB:3JZ7,
FT ECO:0007744|PDB:3MJ7"
FT VAR_SEQ 139..164
FT /note="VKPSGTRCFVDGSEEIGNDFKLKCEP -> GKSSFLLSTGVEWGGGAELQGG
FT REGG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014827"
FT VAR_SEQ 165..365
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014828"
FT VAR_SEQ 340..365
FT /note="VAAPNLSRMGAVPVMIPAQSKDGSIV -> FKYAYKTDGITVV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9096397, ECO:0000303|PubMed:9420240"
FT /id="VSP_014829"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3JZ7"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3JZ7"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3JZ7"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3JZ7"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 127..138
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3JZ7"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3JZ7"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3JZ7"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:3JZ7"
SQ SEQUENCE 365 AA; 39948 MW; 5445B4B52A34B2A2 CRC64;
MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS
PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC
KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD
SQTMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA
GAVIGTLLAL VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA VPVMIPAQSK
DGSIV
