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 02-SEP-2026, entry version 208. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_006522883.5. [P97792-1] DR RefSeq; XP_006522947.1; XM_006522884.5. [P97792-2] DR RefSeq; XP_030104816.1; XM_030248956.1. [P97792-1] DR PDB; 3JZ7; X-ray; 2.19 A; A=20-233. DR PDB; 3MJ7; X-ray; 2.80 A; B=18-236. DR AlphaFoldDB; P97792; -. DR SMR; P97792; -. DR BioGRID; 198986; 13. DR CORUM; P97792; -. DR DIP; DIP-41457N; -. DR FunCoup; P97792; 518. DR IntAct; P97792; 4. DR MINT; P97792; -. DR STRING; 10090.ENSMUSP00000023572; -. DR GlyConnect; P97792; 1 N-Linked glycan (1 site). DR GlyCosmos; P97792; 2 sites, 1 glycan. DR GlyGen; P97792; 4 sites, 4 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P97792; -. DR PhosphoSitePlus; P97792; -. DR SwissPalm; P97792; -. DR jPOST; P97792; -. DR PaxDb; 10090-ENSMUSP00000023572; -. DR PeptideAtlas; P97792; -. DR ProteomicsDB; 277926; -. [P97792-1] DR ProteomicsDB; 277927; -. [P97792-2] DR ProteomicsDB; 277928; -. [P97792-3] DR DNASU; 13052; -. DR Ensembl; ENSMUST00000023572.15; ENSMUSP00000023572.8; ENSMUSG00000022865.15. [P97792-1] DR Ensembl; ENSMUST00000114229.4; ENSMUSP00000109867.3; ENSMUSG00000022865.15. [P97792-2] DR Ensembl; ENSMUST00000231356.2; ENSMUSP00000156281.2; ENSMUSG00000022865.15. [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 AGR; MGI:1201679; -. 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; GTKPMQY; -. DR OrthoDB; 8902063at2759; -. DR PhylomeDB; P97792; -. 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 77 CRISPR screens. DR EvolutionaryTrace; P97792; -. DR PRO; PR:P97792; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; P97792; protein. DR Bgee; ENSMUSG00000022865; Expressed in cortical plate and 283 other cell types or tissues. DR ExpressionAtlas; P97792; baseline and differential. 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:GO_Central. DR GO; GO:0005911; C:cell-cell junction; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; ISO:GO_Central. DR GO; GO:0030175; C:filopodium; IDA:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0030426; C:growth cone; IDA:UniProtKB. 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:GO_Central. DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; ISO:GO_Central. 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:GO_Central. DR GO; GO:0005178; F:integrin binding; ISO:GO_Central. DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; ISO:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; 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: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:GO_Central. 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; 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:1900242; P:regulation of synaptic vesicle endocytosis; IDA:SynGO. DR GO; GO:0070633; P:transepithelial transport; ISO:GO_Central. DR CDD; cd20960; IgV_CAR_like; 1. DR CDD; cd12087; TM_EGFR-like; 1. DR FunFam; 2.60.40.10:FF:000493; Coxsackievirus and adenovirus receptor homolog; 1. DR FunFam; 2.60.40.10:FF:000095; immunoglobulin superfamily member 11 isoform X1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR052307; EJ_Adhesion_Regulator. 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 PANTHER; PTHR44468:SF3; COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR; 1. DR PANTHER; PTHR44468; COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR-RELATED; 1. DR Pfam; PF13895; Ig_2; 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; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR PDBsum; 3JZ7; -. DR PDBsum; 3MJ7; -. 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..282 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 HELIX 44..46 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 //