CXAR_HUMAN
ID CXAR_HUMAN Reviewed; 365 AA.
AC P78310; B2R8V8; B7WPI3; D3YHP0; O00694; Q8WWT6; Q8WWT7; Q8WWT8; Q9UKV4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Coxsackievirus and adenovirus receptor;
DE Short=CAR;
DE Short=hCAR;
DE AltName: Full=CVB3-binding protein;
DE AltName: Full=Coxsackievirus B-adenovirus receptor;
DE AltName: Full=HCVADR;
DE Flags: Precursor;
GN Name=CXADR; Synonyms=CAR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A VIRUS RECEPTOR, AND
RP TISSUE SPECIFICITY.
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).
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 [GENOMIC DNA].
RX PubMed=10543405; DOI=10.1007/s004399900136;
RA Bowles K.R., Gibson J., Wu J., Shaffer L.G., Towbin J.A., Bowles N.E.;
RT "Genomic organization and chromosomal localization of the human
RT Coxsackievirus B-adenovirus receptor gene.";
RL Hum. Genet. 105:354-359(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11573093; DOI=10.1038/nsb1001-874;
RA He Y., Chipman P.R., Howitt J., Bator C.M., Whitt M.A., Baker T.S.,
RA Kuhn R.J., Anderson C.W., Freimuth P., Rossmann M.G.;
RT "Interaction of coxsackievirus B3 with the full length coxsackievirus-
RT adenovirus receptor.";
RL Nat. Struct. Biol. 8:874-878(2001).
RN [5]
RP FUNCTION (MICROBIAL INFECTION), NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4
RP AND 5), INTERACTION WITH COXSACKIEVIRUS TYPE B3, AND SUBCELLULAR LOCATION.
RX PubMed=14978041; DOI=10.1074/jbc.m311754200;
RA Doerner A., Xiong D., Couch K., Yajima T., Knowlton K.U.;
RT "Alternatively spliced soluble coxsackie-adenovirus receptors inhibit
RT coxsackievirus infection.";
RL J. Biol. Chem. 279:18497-18503(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Andersson B., Tomko R.P., Andersson K., Darban H., Oncu D., Mizra M.,
RA Sollerbrant K., Sonnhammer E., Philipson L.;
RT "Putative regulatory domains in the human and mouse CAR genes.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
RA Dietel M.;
RT "Identification and characterisation of CAR 4/6 as a new splice variant of
RT the Coxsackie adenovirus receptor (CAR).";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [14]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC 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 [15]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS
RP SUBGROUPS A/C/D/E/F FIBER PROTEINS.
RX PubMed=9733828; DOI=10.1128/jvi.72.10.7909-7915.1998;
RA Roelvink P.W., Lizonova A., Lee J.G.M., Li Y., Bergelson J.M.,
RA Finberg R.W., Brough D.E., Kovesdi I., Wickham T.J.;
RT "The coxsackievirus-adenovirus receptor protein can function as a cellular
RT attachment protein for adenovirus serotypes from subgroups A, C, D, E, and
RT F.";
RL J. Virol. 72:7909-7915(1998).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ADENOVIRUS FIBER
RP PROTEIN, AND MUTAGENESIS OF 70-VAL--ILE-72.
RX PubMed=10666333; DOI=10.1006/excr.1999.4761;
RA Tomko R.P., Johansson C.B., Totrov M., Abagyan R., Frisen J., Philipson L.;
RT "Expression of the adenovirus receptor and its interaction with the fiber
RT knob.";
RL Exp. Cell Res. 255:47-55(2000).
RN [17]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS GROUP B
RP CAPSID PROTEINS.
RX PubMed=10814575; DOI=10.1006/viro.2000.0324;
RA Martino T.A., Petric M., Weingartl H., Bergelson J.M., Opavsky M.A.,
RA Richardson C.D., Modlin J.F., Finberg R.W., Kain K.C., Willis N.,
RA Gauntt C.J., Liu P.P.;
RT "The coxsackie-adenovirus receptor (CAR) is used by reference strains and
RT clinical isolates representing all six serotypes of coxsackievirus group B
RT and by swine vesicular disease virus.";
RL Virology 271:99-108(2000).
RN [18]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=11549277; DOI=10.1006/bbrc.2001.5535;
RA Thoelen I., Magnusson C., Tagerud S., Polacek C., Lindberg M.,
RA Van Ranst M.;
RT "Identification of alternative splice products encoded by the human
RT coxsackie-adenovirus receptor gene.";
RL Biochem. Biophys. Res. Commun. 287:216-222(2001).
RN [19]
RP TISSUE SPECIFICITY.
RX PubMed=11457744; DOI=10.1161/01.cir.104.3.275;
RA Noutsias M., Fechner H., de Jonge H., Wang X., Dekkers D.,
RA Houtsmuller A.B., Pauschinger M., Bergelson J.M., Warraich R., Yacoub M.,
RA Hetzer R., Lamers J.M.J., Schultheiss H.-P., Poller W.;
RT "Human coxsackie-adenovirus receptor is colocalized with integrins
RT alpha(v)beta(3) and alpha(v)beta(5) on the cardiomyocyte sarcolemma and
RT upregulated in dilated cardiomyopathy: implications for cardiotropic viral
RT infections.";
RL Circulation 104:275-280(2001).
RN [20]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-318 AND 345-LEU--MET-348.
RX PubMed=11316797; DOI=10.1074/jbc.m009531200;
RA Cohen C.J., Gaetz J., Ohman T., Bergelson J.M.;
RT "Multiple regions within the coxsackievirus and adenovirus receptor
RT cytoplasmic domain are required for basolateral sorting.";
RL J. Biol. Chem. 276:25392-25398(2001).
RN [21]
RP SUBCELLULAR LOCATION, INTERACTION WITH TJP1, AND FUNCTION.
RX PubMed=11734628; DOI=10.1073/pnas.261452898;
RA Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T.,
RA Bergelson J.M.;
RT "The coxsackievirus and adenovirus receptor is a transmembrane component of
RT the tight junction.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001).
RN [22]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, INTERACTION WITH
RP CTNNB1, AND INTERACTION WITH HUMAN ADENOVIRUS FIBER PROTEIN.
RX PubMed=12297051; DOI=10.1016/s0092-8674(02)00912-1;
RA Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J.;
RT "Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing
RT virus escape.";
RL Cell 110:789-799(2002).
RN [23]
RP PALMITOYLATION AT CYS-259 AND CYS-260, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 259-CYS-CYS-260.
RX PubMed=12021372; DOI=10.1128/jvi.76.12.6382-6386.2002;
RA van't Hof W., Crystal R.G.;
RT "Fatty acid modification of the coxsackievirus and adenovirus receptor.";
RL J. Virol. 76:6382-6386(2002).
RN [24]
RP INTERACTION WITH LNX.
RX PubMed=12468544; DOI=10.1074/jbc.m205927200;
RA Sollerbrant K., Raschperger E., Mirza M., Engstroem U., Philipson L.,
RA Ljungdahl P.O., Pettersson R.F.;
RT "The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the
RT PDZ domain-containing protein ligand-of-numb protein-X (LNX).";
RL J. Biol. Chem. 278:7439-7444(2003).
RN [25]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
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 [26]
RP INTERACTION WITH MPDZ, AND SUBCELLULAR LOCATION.
RX PubMed=15364909; DOI=10.1074/jbc.m409061200;
RA Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.;
RT "The coxsackievirus and adenovirus receptor interacts with the multi-PDZ
RT domain protein-1 (MUPP-1) within the tight junction.";
RL J. Biol. Chem. 279:48079-48084(2004).
RN [27]
RP INTERACTION WITH MAGI1; DLG4 AND PRKCABP.
RX PubMed=15304526; DOI=10.1242/jcs.01300;
RA Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L.,
RA Zabner J.;
RT "A role for the PDZ-binding domain of the coxsackie B virus and adenovirus
RT receptor (CAR) in cell adhesion and growth.";
RL J. Cell Sci. 117:4401-4409(2004).
RN [28]
RP INTERACTION WITH JAML, DOMAIN, AND FUNCTION.
RX PubMed=15800062; DOI=10.1091/mbc.e05-01-0036;
RA Zen K., Liu Y., McCall I.C., Wu T., Lee W., Babbin B.A., Nusrat A.,
RA Parkos C.A.;
RT "Neutrophil migration across tight junctions is mediated by adhesive
RT interactions between epithelial CAR and a JAM-like protein on
RT neutrophils.";
RL Mol. Biol. Cell 16:2694-2703(2005).
RN [29]
RP FUNCTION IN LEUKOCYTE MIGRATION, AND INTERACTION WITH JAML.
RX PubMed=19064666; DOI=10.1083/jcb.200805061;
RA Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.;
RT "JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis
RT by alpha4beta1 integrin activation.";
RL J. Cell Biol. 183:1159-1173(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-332, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-323 AND SER-332, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-144 IN COMPLEX WITH HUMAN
RP ADENOVIRUS 12 FIBER PROTEIN, AND DISULFIDE BONDS.
RX PubMed=10567268; DOI=10.1126/science.286.5444.1579;
RA Bewley M.C., Springer K., Zhang Y.-B., Freimuth P., Flanagan J.M.;
RT "Structural analysis of the mechanism of adenovirus binding to its human
RT cellular receptor, CAR.";
RL Science 286:1579-1583(1999).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-140, DOMAIN, AND DISULFIDE
RP BOND.
RX PubMed=11080637; DOI=10.1016/s0969-2126(00)00528-1;
RA van Raaij M.J., Chouin E., van der Zandt H., Bergelson J.M., Cusack S.;
RT "Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain
RT at 1.7 A resolution.";
RL Structure 8:1147-1155(2000).
RN [37]
RP STRUCTURE BY NMR OF 21-144, AND DISULFIDE BONDS.
RX PubMed=14967025; DOI=10.1021/bi035490x;
RA Jiang S., Jacobs A., Laue T.M., Caffrey M.;
RT "Solution structure of the coxsackievirus and adenovirus receptor domain
RT 1.";
RL Biochemistry 43:1847-1853(2004).
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:11734628,
CC ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:15800062,
CC ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:9096397}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for adenovirus type
CC C. {ECO:0000269|PubMed:10567268, ECO:0000269|PubMed:10666333,
CC ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:9733828}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus
CC B1 to B6. {ECO:0000269|PubMed:10814575, ECO:0000269|PubMed:14978041}.
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 Secreted isoform 3, isoform 4 and isoform 5 can interact with the
CC extracellular domain of the receptor. {ECO:0000269|PubMed:11734628,
CC ECO:0000269|PubMed:12468544, ECO:0000269|PubMed:15304526,
CC ECO:0000269|PubMed:15364909, ECO:0000269|PubMed:15800062,
CC ECO:0000269|PubMed:19064666}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus subgroups A,
CC C, D, E and F fiber proteins as well as coxsackievirus B1, B2, B3, B4,
CC B5 and B6 capsid proteins (PubMed:14978041, PubMed:9733828,
CC PubMed:10666333, PubMed:10814575, PubMed:12297051, PubMed:10567268).
CC {ECO:0000269|PubMed:10567268, ECO:0000269|PubMed:10666333,
CC ECO:0000269|PubMed:10814575, ECO:0000269|PubMed:12297051,
CC ECO:0000269|PubMed:14978041, ECO:0000269|PubMed:9733828}.
CC -!- INTERACTION:
CC P78310; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-747931, EBI-12109402;
CC P78310; Q92520: FAM3C; NbExp=3; IntAct=EBI-747931, EBI-2876774;
CC P78310; P21145: MAL; NbExp=3; IntAct=EBI-747931, EBI-3932027;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:15533241}; Single-pass type I membrane protein
CC {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:11316797,
CC ECO:0000269|PubMed:12021372, ECO:0000269|PubMed:12297051,
CC ECO:0000269|PubMed:15364909}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell junction, tight junction
CC {ECO:0000269|PubMed:11734628, ECO:0000269|PubMed:12297051}. Cell
CC junction, adherens junction {ECO:0000269|PubMed:12297051}. Note=In
CC epithelial cells localizes to the apical junction complex composed of
CC tight and adherens junctions (PubMed:12297051). In airway epithelial
CC cells localized to basolateral membrane but not to apical surface
CC (PubMed:11316797). {ECO:0000269|PubMed:11316797,
CC ECO:0000269|PubMed:12297051}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC {ECO:0000269|PubMed:14978041}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted
CC {ECO:0000269|PubMed:14978041}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted
CC {ECO:0000269|PubMed:14978041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=SIV;
CC IsoId=P78310-1; Sequence=Displayed;
CC Name=2; Synonyms=CAR2, HCAR2, TVV;
CC IsoId=P78310-2; Sequence=VSP_014825, VSP_014826;
CC Name=3; Synonyms=CAR2/7, Gamma;
CC IsoId=P78310-3; Sequence=VSP_014819, VSP_014820;
CC Name=4; Synonyms=CAR3/7;
CC IsoId=P78310-4; Sequence=VSP_014821, VSP_014822;
CC Name=5; Synonyms=CAR4/7, Beta;
CC IsoId=P78310-5; Sequence=VSP_014823, VSP_014824;
CC Name=6;
CC IsoId=P78310-6; Sequence=VSP_047357;
CC Name=7; Synonyms=CAR 4/6;
CC IsoId=P78310-7; Sequence=VSP_047729;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, brain, heart, small
CC intestine, testis, prostate and at a lower level in liver and lung.
CC Isoform 5 is ubiquitously expressed. Isoform 3 is expressed in heart,
CC lung and pancreas. In skeletal muscle, isoform 1 is found at the
CC neuromuscular junction and isoform 2 is found in blood vessels. In
CC cardiac muscle, isoform 1 and isoform 2 are found at intercalated
CC disks. In heart expressed in subendothelial layers of the vessel wall
CC but not in the luminal endothelial surface. Expression is elevated in
CC hearts with dilated cardiomyopathy. {ECO:0000269|PubMed:10490761,
CC ECO:0000269|PubMed:11457744, ECO:0000269|PubMed:11549277,
CC ECO:0000269|PubMed:9096397}.
CC -!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
CC interaction with JAML.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and MAGI1.
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:0000269|PubMed:12021372}.
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DR EMBL; U90716; AAC51234.1; -; mRNA.
DR EMBL; Y07593; CAA68868.1; -; mRNA.
DR EMBL; AF169366; AAF05908.1; -; Genomic_DNA.
DR EMBL; AF169360; AAF05908.1; JOINED; Genomic_DNA.
DR EMBL; AF169361; AAF05908.1; JOINED; Genomic_DNA.
DR EMBL; AF169362; AAF05908.1; JOINED; Genomic_DNA.
DR EMBL; AF169363; AAF05908.1; JOINED; Genomic_DNA.
DR EMBL; AF169364; AAF05908.1; JOINED; Genomic_DNA.
DR EMBL; AF169365; AAF05908.1; JOINED; Genomic_DNA.
DR EMBL; AF200465; AAF24344.1; -; Genomic_DNA.
DR EMBL; AY072910; AAL68878.1; -; mRNA.
DR EMBL; AY072911; AAL68879.1; -; mRNA.
DR EMBL; AY072912; AAL68880.1; -; mRNA.
DR EMBL; AF242865; AAG01088.1; -; Genomic_DNA.
DR EMBL; AF242862; AAG01088.1; JOINED; Genomic_DNA.
DR EMBL; AF242864; AAG01088.1; JOINED; Genomic_DNA.
DR EMBL; GU474812; ADC84500.1; -; mRNA.
DR EMBL; CR617256; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT019876; AAV38679.1; -; mRNA.
DR EMBL; AK313526; BAG36305.1; -; mRNA.
DR EMBL; AP000963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX10031.1; -; Genomic_DNA.
DR EMBL; BC003684; AAH03684.1; -; mRNA.
DR EMBL; BC010536; AAH10536.1; -; mRNA.
DR EMBL; AF124598; AAD31772.1; -; mRNA.
DR CCDS; CCDS33519.1; -. [P78310-1]
DR CCDS; CCDS56204.1; -. [P78310-6]
DR CCDS; CCDS56205.1; -. [P78310-5]
DR CCDS; CCDS56206.1; -. [P78310-4]
DR CCDS; CCDS56207.1; -. [P78310-3]
DR RefSeq; NP_001193992.1; NM_001207063.1. [P78310-5]
DR RefSeq; NP_001193993.1; NM_001207064.1. [P78310-4]
DR RefSeq; NP_001193994.1; NM_001207065.1. [P78310-3]
DR RefSeq; NP_001193995.1; NM_001207066.1. [P78310-6]
DR RefSeq; NP_001329.1; NM_001338.4. [P78310-1]
DR RefSeq; XP_011527781.1; XM_011529479.1. [P78310-5]
DR PDB; 1EAJ; X-ray; 1.35 A; A/B=15-140.
DR PDB; 1F5W; X-ray; 1.70 A; A/B=15-140.
DR PDB; 1JEW; EM; 22.00 A; R=21-140.
DR PDB; 1KAC; X-ray; 2.60 A; B=22-144.
DR PDB; 1P69; X-ray; 3.10 A; B=22-144.
DR PDB; 1P6A; X-ray; 2.90 A; B=22-144.
DR PDB; 1RSF; NMR; -; A=21-144.
DR PDB; 2J12; X-ray; 1.50 A; B=15-140.
DR PDB; 2J1K; X-ray; 2.30 A; A/B/G/J/K/O/P/T/V/X/Y/Z=15-140.
DR PDB; 2NPL; NMR; -; X=142-235.
DR PDB; 2W9L; X-ray; 2.91 A; A/B/G/J/K/O/P/T/V/X/Y/Z=16-139.
DR PDB; 2WBW; X-ray; 1.55 A; B=15-138.
DR PDB; 3J6L; EM; 9.00 A; B=15-140.
DR PDB; 3J6M; EM; 9.00 A; B=22-144.
DR PDB; 3J6N; EM; 9.00 A; K=20-233.
DR PDB; 3J6O; EM; 9.00 A; S=20-236.
DR PDB; 7DPZ; EM; 3.80 A; K=20-140.
DR PDB; 7DQ1; EM; 3.60 A; K=20-140.
DR PDB; 7VXZ; EM; 3.19 A; E=20-236.
DR PDB; 7VYK; EM; 2.79 A; E=20-236.
DR PDB; 7VYL; EM; 2.79 A; E=20-236.
DR PDB; 7VYM; EM; 3.68 A; E=20-236.
DR PDB; 7W14; EM; 2.20 A; E=20-236.
DR PDBsum; 1EAJ; -.
DR PDBsum; 1F5W; -.
DR PDBsum; 1JEW; -.
DR PDBsum; 1KAC; -.
DR PDBsum; 1P69; -.
DR PDBsum; 1P6A; -.
DR PDBsum; 1RSF; -.
DR PDBsum; 2J12; -.
DR PDBsum; 2J1K; -.
DR PDBsum; 2NPL; -.
DR PDBsum; 2W9L; -.
DR PDBsum; 2WBW; -.
DR PDBsum; 3J6L; -.
DR PDBsum; 3J6M; -.
DR PDBsum; 3J6N; -.
DR PDBsum; 3J6O; -.
DR PDBsum; 7DPZ; -.
DR PDBsum; 7DQ1; -.
DR PDBsum; 7VXZ; -.
DR PDBsum; 7VYK; -.
DR PDBsum; 7VYL; -.
DR PDBsum; 7VYM; -.
DR PDBsum; 7W14; -.
DR AlphaFoldDB; P78310; -.
DR BMRB; P78310; -.
DR SMR; P78310; -.
DR BioGRID; 107905; 354.
DR IntAct; P78310; 21.
DR MINT; P78310; -.
DR STRING; 9606.ENSP00000284878; -.
DR TCDB; 8.A.23.1.14; the basigin (basigin) family.
DR UniLectin; P78310; -.
DR GlyConnect; 1159; 1 N-Linked glycan (1 site).
DR GlyGen; P78310; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P78310; -.
DR PhosphoSitePlus; P78310; -.
DR SwissPalm; P78310; -.
DR BioMuta; CXADR; -.
DR DMDM; 6685351; -.
DR EPD; P78310; -.
DR jPOST; P78310; -.
DR MassIVE; P78310; -.
DR MaxQB; P78310; -.
DR PaxDb; P78310; -.
DR PeptideAtlas; P78310; -.
DR PRIDE; P78310; -.
DR ProteomicsDB; 12784; -.
DR ProteomicsDB; 57548; -. [P78310-1]
DR ProteomicsDB; 57549; -. [P78310-2]
DR ProteomicsDB; 57550; -. [P78310-3]
DR ProteomicsDB; 57551; -. [P78310-4]
DR ProteomicsDB; 57552; -. [P78310-5]
DR ProteomicsDB; 6303; -.
DR Antibodypedia; 1120; 486 antibodies from 39 providers.
DR DNASU; 1525; -.
DR Ensembl; ENST00000284878.12; ENSP00000284878.7; ENSG00000154639.19. [P78310-1]
DR Ensembl; ENST00000356275.10; ENSP00000348620.6; ENSG00000154639.19. [P78310-3]
DR Ensembl; ENST00000400165.5; ENSP00000383029.1; ENSG00000154639.19. [P78310-4]
DR Ensembl; ENST00000400166.5; ENSP00000383030.1; ENSG00000154639.19. [P78310-5]
DR Ensembl; ENST00000400169.1; ENSP00000383033.1; ENSG00000154639.19. [P78310-6]
DR GeneID; 1525; -.
DR KEGG; hsa:1525; -.
DR MANE-Select; ENST00000284878.12; ENSP00000284878.7; NM_001338.5; NP_001329.1.
DR UCSC; uc002ykh.3; human. [P78310-1]
DR CTD; 1525; -.
DR DisGeNET; 1525; -.
DR GeneCards; CXADR; -.
DR HGNC; HGNC:2559; CXADR.
DR HPA; ENSG00000154639; Low tissue specificity.
DR MIM; 602621; gene.
DR neXtProt; NX_P78310; -.
DR OpenTargets; ENSG00000154639; -.
DR PharmGKB; PA27055; -.
DR VEuPathDB; HostDB:ENSG00000154639; -.
DR eggNOG; ENOG502QSG0; Eukaryota.
DR GeneTree; ENSGT00940000154829; -.
DR HOGENOM; CLU_040549_0_0_1; -.
DR InParanoid; P78310; -.
DR OMA; CQFTLAP; -.
DR OrthoDB; 896005at2759; -.
DR PhylomeDB; P78310; -.
DR TreeFam; TF330875; -.
DR PathwayCommons; P78310; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P78310; -.
DR BioGRID-ORCS; 1525; 39 hits in 1053 CRISPR screens.
DR ChiTaRS; CXADR; human.
DR EvolutionaryTrace; P78310; -.
DR GeneWiki; Coxsackie_virus_and_adenovirus_receptor; -.
DR GenomeRNAi; 1525; -.
DR Pharos; P78310; Tbio.
DR PRO; PR:P78310; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P78310; protein.
DR Bgee; ENSG00000154639; Expressed in nipple and 199 other tissues.
DR Genevisible; P78310; HS.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA: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; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI: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; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA: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; ISS:BHF-UCL.
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:0045216; P:cell-cell junction organization; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP: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; IDA:UniProtKB.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:0098904; P:regulation of AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0070633; P:transepithelial transport; IMP:UniProtKB.
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;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Receptor; 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"
FT /id="PRO_0000014739"
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..134
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..228
FT /note="Ig-like C2-type 2"
FT REGION 269..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..365
FT /note="PDZ-binding"
FT COMPBIAS 269..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..330
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:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97792"
FT LIPID 259
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12021372"
FT LIPID 260
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12021372"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..120
FT /evidence="ECO:0000269|PubMed:10567268,
FT ECO:0000269|PubMed:11080637, ECO:0000269|PubMed:14967025"
FT DISULFID 162..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:14967025"
FT VAR_SEQ 71..89
FT /note="IILYSGDKIYDDYYPDLKG -> GRCATSKEPYVHCQKLHRQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14978041"
FT /id="VSP_014819"
FT VAR_SEQ 90..365
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14978041"
FT /id="VSP_014820"
FT VAR_SEQ 139
FT /note="V -> GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVK
FT TLNALLRVRLSHLLR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14978041"
FT /id="VSP_014821"
FT VAR_SEQ 140..365
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14978041"
FT /id="VSP_014822"
FT VAR_SEQ 191..232
FT /note="EMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPP -> A (in
FT isoform 7)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_047729"
FT VAR_SEQ 191
FT /note="E -> GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVK
FT TLNALLRVRLSHLLR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14978041"
FT /id="VSP_014823"
FT VAR_SEQ 192..365
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14978041"
FT /id="VSP_014824"
FT VAR_SEQ 340..365
FT /note="VAAPNLSRMGAIPVMIPAQSKDGSIV -> FKYPYKTDGITVV (in
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_047357"
FT VAR_SEQ 340..345
FT /note="VAAPNL -> FKYPY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_014825"
FT VAR_SEQ 346..365
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_014826"
FT VARIANT 323
FT /note="S -> R (in dbSNP:rs34727960)"
FT /id="VAR_049871"
FT MUTAGEN 70..72
FT /note="VII->AID: Abolishes binding to adenovirus type 5."
FT /evidence="ECO:0000269|PubMed:10666333"
FT MUTAGEN 259..260
FT /note="CC->AA: Loss of palmitoylation and altered
FT localization."
FT /evidence="ECO:0000269|PubMed:12021372"
FT MUTAGEN 318
FT /note="Y->A: Affects basolateral localization in airway
FT epithelial cells."
FT /evidence="ECO:0000269|PubMed:11316797"
FT MUTAGEN 345..348
FT /note="LSRM->AAAA: Affects basolateral localization in
FT airway epithelial cells."
FT /evidence="ECO:0000269|PubMed:11316797"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1RSF"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1EAJ"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1EAJ"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1EAJ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 127..138
FT /evidence="ECO:0007829|PDB:1EAJ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2NPL"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:2NPL"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2NPL"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:2NPL"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:2NPL"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2NPL"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:2NPL"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:2NPL"
FT CONFLICT P78310-2:343
FT /note="P -> A (in Ref. 14; AAD31772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 40030 MW; AB01C6346CB7FE64 CRC64;
MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS
PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS GDASINVTNL QLSDIGTYQC
KVKKAPGVAN KKIHLVVLVK PSGARCYVDG SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD
SQKMPTSWLA EMTSSVISVK NASSEYSGTY SCTVRNRVGS DQCLLRLNVV PPSNKAGLIA
GAIIGTLLAL ALIGLIIFCC RKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
SLGSMSPSNM EGYSKTQYNQ VPSEDFERTP QSPTLPPAKV AAPNLSRMGA IPVMIPAQSK
DGSIV
