JAM1_HUMAN
ID JAM1_HUMAN Reviewed; 299 AA.
AC Q9Y624; B7Z941;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Junctional adhesion molecule A;
DE Short=JAM-A;
DE AltName: Full=Junctional adhesion molecule 1;
DE Short=JAM-1;
DE AltName: Full=Platelet F11 receptor;
DE AltName: Full=Platelet adhesion molecule 1;
DE Short=PAM-1;
DE AltName: CD_antigen=CD321;
DE Flags: Precursor;
GN Name=F11R; Synonyms=JAM1, JCAM; ORFNames=UNQ264/PRO301;
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).
RX PubMed=10395639;
RA Ozaki H., Ishii K., Horiuchi H., Arai H., Kawamoto T., Okawa K.,
RA Iwamatsu A., Kita T.;
RT "Combined treatment of TNF-alpha and IFN-gamma causes redistribution of
RT junctional adhesion molecule in human endothelial cells.";
RL J. Immunol. 163:553-557(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=10753840;
RA Sobocka M.B., Sobocki T., Banerjee P., Weiss C., Rushbrook J.I.,
RA Norin A.J., Hartwig J., Salifu M.O., Markell M.S., Babinska A.,
RA Ehrlich Y.H., Kornecki E.;
RT "Cloning of the human platelet F11 receptor: a cell adhesion molecule
RT member of the immunoglobulin superfamily involved in platelet
RT aggregation.";
RL Blood 95:2600-2609(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=11171323; DOI=10.1242/jcs.114.3.539;
RA Naik U.P., Naik M.U., Eckfeld K., Martin-DeLeon P., Spychala J.;
RT "Characterization and chromosomal localization of JAM-1, a platelet
RT receptor for a stimulatory monoclonal antibody.";
RL J. Cell Sci. 114:539-547(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [9]
RP PROTEIN SEQUENCE OF 28-103 AND 123-130, AND GLYCOSYLATION.
RX PubMed=7646439; DOI=10.1042/bj3100155;
RA Naik U.P., Ehrlich Y.H., Kornecki E.;
RT "Mechanisms of platelet activation by a stimulatory antibody: cross-linking
RT of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma
RT RII receptor.";
RL Biochem. J. 310:155-162(1995).
RN [10]
RP PROTEIN SEQUENCE OF 28-42.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [11]
RP PROTEIN SEQUENCE OF 28-39.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH MPDZ.
RX PubMed=11489913; DOI=10.1083/jcb.200103047;
RA Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S.;
RT "Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism
RT for the recruitment of PAR-3 to tight junctions.";
RL J. Cell Biol. 154:491-497(2001).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MAMMALIAN REOVIRUS
RP SIGMA-1 PROTEIN.
RX PubMed=11239401; DOI=10.1016/s0092-8674(01)00231-8;
RA Barton E.S., Forrest J.C., Connolly J.L., Chappell J.D., Liu Y.,
RA Schnell F.J., Nusrat A., Parkos C.A., Dermody T.S.;
RT "Junction adhesion molecule is a receptor for reovirus.";
RL Cell 104:441-451(2001).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=11812992; DOI=10.1038/ni755;
RA Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.;
RT "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in
RT transendothelial migration of leukocytes.";
RL Nat. Immunol. 3:151-158(2002).
RN [15]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=12810109; DOI=10.1016/s1471-4906(03)00117-0;
RA Muller W.A.;
RT "Leukocyte-endothelial-cell interactions in leukocyte transmigration and
RT the inflammatory response.";
RL Trends Immunol. 24:327-334(2003).
RN [16]
RP INTERACTION WITH ITGAL.
RX PubMed=15528364; DOI=10.4049/jimmunol.173.10.6259;
RA Fraemohs L., Koenen R.R., Ostermann G., Heinemann B., Weber C.;
RT "The functional interaction of the beta 2 integrin lymphocyte function-
RT associated antigen-1 with junctional adhesion molecule-A is mediated by the
RT I domain.";
RL J. Immunol. 173:6259-6264(2004).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281; SER-284 AND SER-287, 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 [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP 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 [25]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [26]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ROTAVIRUS STRAIN
RP WA VP4 PROTEIN.
RX PubMed=25481868; DOI=10.1016/j.virol.2014.11.016;
RA Torres-Flores J.M., Silva-Ayala D., Espinoza M.A., Lopez S., Arias C.F.;
RT "The tight junction protein JAM-A functions as coreceptor for rotavirus
RT entry into MA104 cells.";
RL Virology 475:172-178(2015).
RN [27]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
RX PubMed=33970782; DOI=10.1080/19490976.2021.1921928;
RA Marques M.S., Costa A.C., Osorio H., Pinto M.L., Relvas S.,
RA Dinis-Ribeiro M., Carneiro F., Leite M., Figueiredo C.;
RT "Helicobacter pylori PqqE is a new virulence factor that cleaves junctional
RT adhesion molecule A and disrupts gastric epithelial integrity.";
RL Gut Microbes 13:1-21(2021).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 27-233, AND DISULFIDE BONDS.
RX PubMed=12697893; DOI=10.1073/pnas.0937718100;
RA Prota A.E., Campbell J.A., Schelling P., Forrest J.C., Watson M.J.,
RA Peters T.R., Aurrand-Lions M.A., Imhof B.A., Dermody T.S., Stehle T.;
RT "Crystal structure of human junctional adhesion molecule 1: implications
RT for reovirus binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5366-5371(2003).
CC -!- FUNCTION: Seems to play a role in epithelial tight junction formation.
CC Appears early in primordial forms of cell junctions and recruits PARD3
CC (PubMed:11489913). The association of the PARD6-PARD3 complex may
CC prevent the interaction of PARD3 with JAM1, thereby preventing tight
CC junction assembly (By similarity). Plays a role in regulating monocyte
CC transmigration involved in integrity of epithelial barrier (By
CC similarity). Ligand for integrin alpha-L/beta-2 involved in memory T-
CC cell and neutrophil transmigration (PubMed:11812992). Involved in
CC platelet activation (PubMed:10753840). {ECO:0000250|UniProtKB:O88792,
CC ECO:0000269|PubMed:10753840, ECO:0000269|PubMed:11489913,
CC ECO:0000269|PubMed:11812992}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Mammalian
CC reovirus sigma-1. {ECO:0000269|PubMed:11239401}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Human Rotavirus
CC strain Wa. {ECO:0000269|PubMed:25481868}.
CC -!- SUBUNIT: Interacts with the ninth PDZ domain of MPDZ (PubMed:11489913).
CC Interacts with the first PDZ domain of PARD3 (PubMed:11489913). The
CC association between PARD3 and PARD6B probably disrupts this interaction
CC (By similarity). Interacts with ITGAL (via I-domain) (PubMed:15528364).
CC {ECO:0000250|UniProtKB:O88792, ECO:0000269|PubMed:11489913,
CC ECO:0000269|PubMed:15528364}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Mammalian reovirus sigma-
CC 1 capsid protein. {ECO:0000269|PubMed:11239401}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Human Rotavirus strain Wa
CC vp4 capsid protein. {ECO:0000269|PubMed:25481868}.
CC -!- INTERACTION:
CC Q9Y624; Q9NP70: AMBN; NbExp=3; IntAct=EBI-742600, EBI-11893530;
CC Q9Y624; P49069: CAMLG; NbExp=3; IntAct=EBI-742600, EBI-1748958;
CC Q9Y624; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-742600, EBI-10266796;
CC Q9Y624; Q92615: LARP4B; NbExp=3; IntAct=EBI-742600, EBI-1052558;
CC Q9Y624; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-742600, EBI-10317612;
CC Q9Y624; P50281: MMP14; NbExp=3; IntAct=EBI-742600, EBI-992788;
CC Q9Y624; Q9BV20: MRI1; NbExp=3; IntAct=EBI-742600, EBI-747381;
CC Q9Y624; Q96S97: MYADM; NbExp=3; IntAct=EBI-742600, EBI-13301517;
CC Q9Y624; Q8TEW0: PARD3; NbExp=2; IntAct=EBI-742600, EBI-81968;
CC Q9Y624; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-742600, EBI-12092917;
CC Q9Y624; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-742600, EBI-712367;
CC Q9Y624; O43765: SGTA; NbExp=11; IntAct=EBI-742600, EBI-347996;
CC Q9Y624; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-742600, EBI-8644112;
CC Q9Y624; P78382: SLC35A1; NbExp=3; IntAct=EBI-742600, EBI-12870360;
CC Q9Y624; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-742600, EBI-10244848;
CC Q9Y624; P0DN84: STRIT1; NbExp=3; IntAct=EBI-742600, EBI-12200293;
CC Q9Y624; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-742600, EBI-8644968;
CC Q9Y624; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-742600, EBI-348587;
CC Q9Y624; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-742600, EBI-2548832;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:11171323}. Cell membrane
CC {ECO:0000269|PubMed:11171323}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11171323}. Note=Localized at tight junctions of
CC both epithelial and endothelial cells. {ECO:0000269|PubMed:11171323}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y624-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y624-2; Sequence=VSP_056218;
CC -!- TISSUE SPECIFICITY: Expressed in endothelium, epithelium and leukocytes
CC (at protein level). {ECO:0000269|PubMed:11812992}.
CC -!- DOMAIN: The Ig-like V-type 2 domain is necessary and sufficient for
CC interaction with integrin alpha-L/beta-2.
CC {ECO:0000269|PubMed:11812992}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:7646439}.
CC -!- PTM: (Microbial infection) Cleaved by H.pylori virulence factor PqqE.
CC Cleavage leads to altered tight junction functions.
CC {ECO:0000269|PubMed:33970782}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AF111713; AAD42050.1; -; mRNA.
DR EMBL; AF207907; AAF22829.1; -; mRNA.
DR EMBL; AF172398; AAD48877.1; -; mRNA.
DR EMBL; AL136649; CAB66584.1; -; mRNA.
DR EMBL; AY358896; AAQ89255.1; -; mRNA.
DR EMBL; AK304412; BAH14177.1; -; mRNA.
DR EMBL; AL591806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001533; AAH01533.1; -; mRNA.
DR CCDS; CCDS1213.1; -. [Q9Y624-1]
DR CCDS; CCDS86026.1; -. [Q9Y624-2]
DR PIR; A59406; S56749.
DR RefSeq; NP_001335020.1; NM_001348091.1. [Q9Y624-2]
DR RefSeq; NP_058642.1; NM_016946.5. [Q9Y624-1]
DR PDB; 1NBQ; X-ray; 2.90 A; A/B=27-233.
DR PDB; 3EOY; X-ray; 3.40 A; G/H/I/J/K/L=28-129.
DR PDB; 3TSZ; X-ray; 2.50 A; B=288-299.
DR PDB; 4ODB; X-ray; 3.20 A; D/E/F=28-129.
DR PDBsum; 1NBQ; -.
DR PDBsum; 3EOY; -.
DR PDBsum; 3TSZ; -.
DR PDBsum; 4ODB; -.
DR AlphaFoldDB; Q9Y624; -.
DR SMR; Q9Y624; -.
DR BioGRID; 119153; 78.
DR CORUM; Q9Y624; -.
DR IntAct; Q9Y624; 33.
DR MINT; Q9Y624; -.
DR STRING; 9606.ENSP00000357005; -.
DR GlyConnect; 1427; 12 N-Linked glycans (1 site).
DR GlyGen; Q9Y624; 2 sites, 13 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y624; -.
DR MetOSite; Q9Y624; -.
DR PhosphoSitePlus; Q9Y624; -.
DR SwissPalm; Q9Y624; -.
DR BioMuta; F11R; -.
DR DMDM; 10720061; -.
DR EPD; Q9Y624; -.
DR jPOST; Q9Y624; -.
DR MassIVE; Q9Y624; -.
DR MaxQB; Q9Y624; -.
DR PaxDb; Q9Y624; -.
DR PeptideAtlas; Q9Y624; -.
DR PRIDE; Q9Y624; -.
DR ProteomicsDB; 7002; -.
DR ProteomicsDB; 86590; -. [Q9Y624-1]
DR Antibodypedia; 3317; 633 antibodies from 44 providers.
DR DNASU; 50848; -.
DR Ensembl; ENST00000368026.11; ENSP00000357005.5; ENSG00000158769.18. [Q9Y624-1]
DR Ensembl; ENST00000537746.1; ENSP00000440812.1; ENSG00000158769.18. [Q9Y624-2]
DR GeneID; 50848; -.
DR KEGG; hsa:50848; -.
DR MANE-Select; ENST00000368026.11; ENSP00000357005.5; NM_016946.6; NP_058642.1.
DR UCSC; uc009wtt.4; human. [Q9Y624-1]
DR CTD; 50848; -.
DR DisGeNET; 50848; -.
DR GeneCards; F11R; -.
DR HGNC; HGNC:14685; F11R.
DR HPA; ENSG00000158769; Low tissue specificity.
DR MIM; 605721; gene.
DR neXtProt; NX_Q9Y624; -.
DR OpenTargets; ENSG00000158769; -.
DR PharmGKB; PA29991; -.
DR VEuPathDB; HostDB:ENSG00000158769; -.
DR eggNOG; ENOG502QWVN; Eukaryota.
DR GeneTree; ENSGT00940000159186; -.
DR HOGENOM; CLU_067351_0_0_1; -.
DR InParanoid; Q9Y624; -.
DR OMA; YSRGYFE; -.
DR PhylomeDB; Q9Y624; -.
DR TreeFam; TF343984; -.
DR PathwayCommons; Q9Y624; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-HSA-420029; Tight junction interactions.
DR SignaLink; Q9Y624; -.
DR SIGNOR; Q9Y624; -.
DR BioGRID-ORCS; 50848; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; F11R; human.
DR EvolutionaryTrace; Q9Y624; -.
DR GeneWiki; F11_receptor; -.
DR GenomeRNAi; 50848; -.
DR Pharos; Q9Y624; Tbio.
DR PRO; PR:Q9Y624; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y624; protein.
DR Bgee; ENSG00000158769; Expressed in olfactory segment of nasal mucosa and 134 other tissues.
DR ExpressionAtlas; Q9Y624; baseline and differential.
DR Genevisible; Q9Y624; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; TAS:Reactome.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR GO; GO:0070160; C:tight junction; IMP:ARUK-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IPI:ARUK-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ARUK-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:ARUK-UCL.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0050892; P:intestinal absorption; IMP:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:ARUK-UCL.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0035683; P:memory T cell extravasation; IDA:ARUK-UCL.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:ARUK-UCL.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IMP:ARUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:ARUK-UCL.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:ARUK-UCL.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; IMP:ARUK-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:ARUK-UCL.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:ARUK-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IDA:ARUK-UCL.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:ARUK-UCL.
DR GO; GO:0090559; P:regulation of membrane permeability; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042456; F11R.
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; PTHR45113; PTHR45113; 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 junction; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:7646439,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 28..299
FT /note="Junctional adhesion molecule A"
FT /id="PRO_0000015066"
FT TOPO_DOM 28..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..125
FT /note="Ig-like V-type 1"
FT DOMAIN 135..228
FT /note="Ig-like V-type 2"
FT SITE 285..286
FT /note="(Microbial infection) Cleavage; by H.pylori PqqE"
FT /evidence="ECO:0000269|PubMed:33970782"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 50..109
FT /evidence="ECO:0000269|PubMed:12697893"
FT DISULFID 153..212
FT /evidence="ECO:0000269|PubMed:12697893"
FT VAR_SEQ 81..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056218"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4ODB"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3EOY"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1NBQ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4ODB"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1NBQ"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1NBQ"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1NBQ"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1NBQ"
SQ SEQUENCE 299 AA; 32583 MW; D95DE2FEA23D2851 CRC64;
MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC AYSGFSSPRV
EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT REDTGTYTCM VSEEGGNSYG
EVKVKLIVLV PPSKPTVNIP SSATIGNRAV LTCSEQDGSP PSEYTWFKDG IVMPTNPKST
RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV
AAVLVTLILL GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLV
