JAM3_HUMAN
ID JAM3_HUMAN Reviewed; 310 AA.
AC Q9BX67; B3KWG9; Q8WWL8; Q96FL1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Junctional adhesion molecule C;
DE Short=JAM-C;
DE AltName: Full=JAM-2;
DE AltName: Full=Junctional adhesion molecule 3;
DE Short=JAM-3;
DE Contains:
DE RecName: Full=Soluble form of JAM-C {ECO:0000303|PubMed:20592283};
DE Short=sJAM-C {ECO:0000303|PubMed:20592283};
DE Flags: Precursor;
GN Name=JAM3; ORFNames=UNQ859/PRO1868;
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, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11590146; DOI=10.1074/jbc.m105972200;
RA Arrate M.P., Rodriguez J.M., Tran T.M., Brock T.A., Cunningham S.A.;
RT "Cloning of human junctional adhesion molecule 3 (JAM3) and its
RT identification as the JAM2 counter-receptor.";
RL J. Biol. Chem. 276:45826-45832(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11739175; DOI=10.1182/blood.v98.13.3699;
RA Aurrand-Lions M.A., Johnson-Leger C., Wong C., Du Pasquier L., Imhof B.A.;
RT "Heterogeneity of endothelial junctions is reflected by differential
RT expression and specific subcellular localization of the three JAM family
RT members.";
RL Blood 98:3699-3707(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH ITGAM.
RX PubMed=12208882; DOI=10.1084/jem.20020267;
RA Santoso S., Sachs U.J.H., Kroll H., Linder M., Ruf A., Preissner K.T.,
RA Chavakis T.;
RT "The junctional adhesion molecule 3 (JAM-3) on human platelets is a
RT counterreceptor for the leukocyte integrin Mac-1.";
RL J. Exp. Med. 196:679-691(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11944976; DOI=10.1006/geno.2002.6742;
RA Phillips H.M., Renforth G.L., Spalluto C., Hearn T., Curtis A.R.J.,
RA Craven L., Havarani B., Clement-Jones M., English C., Stumper O.,
RA Salmon T., Hutchinson S., Jackson M.S., Wilson D.I.;
RT "Narrowing the critical region within 11q24-qter for hypoplastic left heart
RT and identification of a candidate gene, JAM3, expressed during
RT cardiogenesis.";
RL Genomics 79:475-478(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thalamus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Uterus;
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 [10]
RP PROTEIN SEQUENCE OF 32-46.
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 FUNCTION.
RX PubMed=11823489; DOI=10.4049/jimmunol.168.4.1618;
RA Liang T.W., Chiu H.H., Gurney A., Sidle A., Tumas D.B., Schow P.,
RA Foster J., Klassen T., Dennis K., DeMarco R.A., Pham T., Frantz G.,
RA Fong S.;
RT "Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts
RT with T, NK, and dendritic cells through JAM 3.";
RL J. Immunol. 168:1618-1626(2002).
RN [12]
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 [13]
RP FUNCTION IN NEUTROPHIL TRANSEPITHELIAL MIGRATION, INTERACTION WITH ITGAM,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15194813; DOI=10.1091/mbc.e04-04-0317;
RA Zen K., Babbin B.A., Liu Y., Whelan J.B., Nusrat A., Parkos C.A.;
RT "JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated
RT neutrophil transepithelial migration.";
RL Mol. Biol. Cell 15:3926-3937(2004).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=15372036; DOI=10.1038/nature02877;
RA Gliki G., Ebnet K., Aurrand-Lions M., Imhof B.A., Adams R.H.;
RT "Spermatid differentiation requires the assembly of a cell polarity complex
RT downstream of junctional adhesion molecule-C.";
RL Nature 431:320-324(2004).
RN [15]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15994945; DOI=10.1158/0008-5472.can-04-4012;
RA Lamagna C., Hodivala-Dilke K.M., Imhof B.A., Aurrand-Lions M.;
RT "Antibody against junctional adhesion molecule-C inhibits angiogenesis and
RT tumor growth.";
RL Cancer Res. 65:5703-5710(2005).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [17]
RP INVOLVEMENT IN HDBSCC.
RX PubMed=21109224; DOI=10.1016/j.ajhg.2010.10.026;
RA Mochida G.H., Ganesh V.S., Felie J.M., Gleason D., Hill R.S., Clapham K.R.,
RA Rakiec D., Tan W.H., Akawi N., Al-Saffar M., Partlow J.N., Tinschert S.,
RA Barkovich A.J., Ali B., Al-Gazali L., Walsh C.A.;
RT "A homozygous mutation in the tight-junction protein JAM3 causes
RT hemorrhagic destruction of the brain, subependymal calcification, and
RT congenital cataracts.";
RL Am. J. Hum. Genet. 87:882-889(2010).
RN [18]
RP FUNCTION IN ANGIOGENESIS (SOLUBLE FORM OF JAM-C), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION (SOLUBLE FORM OF JAM-C), AND PROTEOLYTIC CLEAVAGE BY
RP ADAM10 AND ADAM17.
RX PubMed=20592283; DOI=10.4049/jimmunol.1000556;
RA Rabquer B.J., Amin M.A., Teegala N., Shaheen M.K., Tsou P.S., Ruth J.H.,
RA Lesch C.A., Imhof B.A., Koch A.E.;
RT "Junctional adhesion molecule-C is a soluble mediator of angiogenesis.";
RL J. Immunol. 185:1777-1785(2010).
RN [19]
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 [20]
RP FUNCTION.
RX PubMed=24357068; DOI=10.1002/stem.1624;
RA Arcangeli M.L., Bardin F., Frontera V., Bidaut G., Obrados E., Adams R.H.,
RA Chabannon C., Aurrand-Lions M.;
RT "Function of Jam-B/Jam-C interaction in homing and mobilization of human
RT and mouse hematopoietic stem and progenitor cells.";
RL Stem Cells 32:1043-1054(2014).
RN [21]
RP FUNCTION, PALMITOYLATION AT CYS-264 AND CYS-265, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-264 AND CYS-265.
RX PubMed=28196865; DOI=10.1074/jbc.m116.730523;
RA Aramsangtienchai P., Spiegelman N.A., Cao J., Lin H.;
RT "S-Palmitoylation of Junctional Adhesion Molecule C Regulates Its Tight
RT Junction Localization and Cell Migration.";
RL J. Biol. Chem. 292:5325-5334(2017).
RN [22]
RP VARIANTS HDBSCC LYS-116 AND TYR-219, CHARACTERIZATION OF VARIANT HDBSCC
RP TYR-219, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23255084; DOI=10.1002/humu.22263;
RA Akawi N.A., Canpolat F.E., White S.M., Quilis-Esquerra J.,
RA Morales Sanchez M., Gamundi M.J., Mochida G.H., Walsh C.A., Ali B.R.,
RA Al-Gazali L.;
RT "Delineation of the clinical, molecular and cellular aspects of novel JAM3
RT mutations underlying the autosomal recessive hemorrhagic destruction of the
RT brain, subependymal calcification, and congenital cataracts.";
RL Hum. Mutat. 34:498-505(2013).
CC -!- FUNCTION: Junctional adhesion protein that mediates heterotypic cell-
CC cell interactions with its cognate receptor JAM2 to regulate different
CC cellular processes (PubMed:11590146, PubMed:11823489). Plays a role in
CC homing and mobilization of hematopoietic stem and progenitor cells
CC within the bone marrow. At the surface of bone marrow stromal cells, it
CC contributes to the retention of the hematopoietic stem and progenitor
CC cells expressing JAM3 (PubMed:11590146, PubMed:24357068). Plays a
CC central role in leukocytes extravasation by facilitating transmigration
CC through the endothelium (By similarity). Plays a role in
CC spermatogenesis where JAM2 and JAM3, which are respectively expressed
CC by Sertoli and germ cells, mediate an interaction between both cell
CC types and play an essential role in the anchorage of germ cells onto
CC Sertoli cells and the assembly of cell polarity complexes during
CC spermatid differentiation (By similarity). Also functions as a counter-
CC receptor for ITGAM, mediating leukocyte-platelet interactions and is
CC involved in the regulation of transepithelial migration of
CC polymorphonuclear neutrophils (PMN) (PubMed:12208882, PubMed:15194813).
CC Plays a role in angiogenesis (PubMed:23255084). Plays a role in the
CC regulation of cell migration (Probable). During myogenesis, it is
CC involved in myocyte fusion (By similarity).
CC {ECO:0000250|UniProtKB:A3KPA0, ECO:0000250|UniProtKB:Q9D8B7,
CC ECO:0000269|PubMed:11590146, ECO:0000269|PubMed:11823489,
CC ECO:0000269|PubMed:12208882, ECO:0000269|PubMed:15194813,
CC ECO:0000269|PubMed:23255084, ECO:0000269|PubMed:24357068,
CC ECO:0000305|PubMed:28196865}.
CC -!- FUNCTION: [Soluble form of JAM-C]: Promotes chemotaxis of vascular
CC endothelial cells and stimulates angiogenesis.
CC {ECO:0000269|PubMed:20592283}.
CC -!- SUBUNIT: Interacts with ITGAM (PubMed:12208882, PubMed:15194813).
CC Interacts with GORASP2 (By similarity). {ECO:0000250|UniProtKB:Q9D8B7,
CC ECO:0000269|PubMed:11590146, ECO:0000269|PubMed:12208882,
CC ECO:0000269|PubMed:15194813}.
CC -!- INTERACTION:
CC Q9BX67; P57087: JAM2; NbExp=2; IntAct=EBI-4314733, EBI-3918416;
CC Q9BX67; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-4314733, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11590146,
CC ECO:0000269|PubMed:12208882, ECO:0000269|PubMed:15994945,
CC ECO:0000269|PubMed:23255084, ECO:0000269|PubMed:28196865}; Single-pass
CC type I membrane protein {ECO:0000305|PubMed:11590146}. Cell junction
CC {ECO:0000269|PubMed:15994945}. Cell junction, desmosome
CC {ECO:0000269|PubMed:15194813}. Cell junction, tight junction
CC {ECO:0000269|PubMed:28196865}. Note=Detected in the acrosome region in
CC developing spermatids (By similarity). In epithelial cells, it is
CC expressed at desmosomes but not at tight junctions (PubMed:15194813).
CC Localizes at the cell surface of endothelial cells; treatment of
CC endothelial cells with vascular endothelial growth factor stimulates
CC recruitment of JAM3 to cell-cell contacts (PubMed:15994945).
CC {ECO:0000250|UniProtKB:Q9D8B7}.
CC -!- SUBCELLULAR LOCATION: [Soluble form of JAM-C]: Secreted
CC {ECO:0000269|PubMed:20592283}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BX67-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BX67-2; Sequence=VSP_042561;
CC -!- TISSUE SPECIFICITY: Detected on round and elongated spermatids (at
CC protein level) (PubMed:15372036). Highest expression in placenta, brain
CC and kidney. Significant expression is detected on platelets. Expressed
CC in intestinal mucosa cells. Expressed in the vascular endothelium.
CC Found in serum (at protein level). Also detected in the synovial fluid
CC of patients with rheumatoid arthritis, psoriatic arthritis or
CC ostearthritis (at protein level). {ECO:0000269|PubMed:11590146,
CC ECO:0000269|PubMed:11944976, ECO:0000269|PubMed:12208882,
CC ECO:0000269|PubMed:15194813, ECO:0000269|PubMed:15372036,
CC ECO:0000269|PubMed:15994945, ECO:0000269|PubMed:20592283}.
CC -!- DOMAIN: The Ig-like V-type domain mediates interaction with JAM2.
CC {ECO:0000250|UniProtKB:Q9D8B7}.
CC -!- PTM: Proteolytically cleaved from endothelial cells surface into a
CC soluble form by ADAM10 and ADAM17; the release of soluble JAM3 is
CC increased by pro-inflammatory factors. {ECO:0000269|PubMed:20592283}.
CC -!- PTM: S-palmitoylated by ZDHHC7. S-palmitoylation promotes expression at
CC tight junctions. {ECO:0000269|PubMed:28196865}.
CC -!- DISEASE: Hemorrhagic destruction of the brain with subependymal
CC calcification and cataracts (HDBSCC) [MIM:613730]: A syndrome
CC characterized by congenital cataracts and severe brain abnormalities
CC apparently resulting from hemorrhagic destruction of the brain
CC parenchyma, including the cerebral white matter and basal ganglia.
CC Patients manifest profound developmental delay, and other neurologic
CC features included seizures, spasticity, and hyperreflexia. The clinical
CC course is very severe resulting in death in infancy. Brain imaging
CC shows multifocal intraparenchymal hemorrhage with associated
CC liquefaction and massive cystic degeneration, and calcification in the
CC subependymal region and in brain tissue. {ECO:0000269|PubMed:21109224,
CC ECO:0000269|PubMed:23255084}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC94776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF356518; AAK27221.1; -; mRNA.
DR EMBL; AJ344431; CAC69845.1; -; mRNA.
DR EMBL; AF448478; AAM20925.1; -; mRNA.
DR EMBL; AJ416101; CAC94776.1; ALT_INIT; mRNA.
DR EMBL; AK074769; BAC11195.1; -; mRNA.
DR EMBL; AK075309; BAC11538.1; -; mRNA.
DR EMBL; AK125071; BAG54131.1; -; mRNA.
DR EMBL; AY358335; AAQ88701.1; -; mRNA.
DR EMBL; AP000911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67820.1; -; Genomic_DNA.
DR EMBL; BC010690; AAH10690.1; -; mRNA.
DR EMBL; BC012147; AAH12147.1; -; mRNA.
DR CCDS; CCDS55799.1; -. [Q9BX67-2]
DR CCDS; CCDS8494.2; -. [Q9BX67-1]
DR RefSeq; NP_001192258.1; NM_001205329.1. [Q9BX67-2]
DR RefSeq; NP_116190.3; NM_032801.4. [Q9BX67-1]
DR AlphaFoldDB; Q9BX67; -.
DR SMR; Q9BX67; -.
DR BioGRID; 123734; 28.
DR IntAct; Q9BX67; 8.
DR MINT; Q9BX67; -.
DR STRING; 9606.ENSP00000299106; -.
DR GlyConnect; 672; 2 N-Linked glycans (1 site).
DR GlyGen; Q9BX67; 2 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q9BX67; -.
DR PhosphoSitePlus; Q9BX67; -.
DR SwissPalm; Q9BX67; -.
DR BioMuta; JAM3; -.
DR DMDM; 51701611; -.
DR EPD; Q9BX67; -.
DR jPOST; Q9BX67; -.
DR MassIVE; Q9BX67; -.
DR MaxQB; Q9BX67; -.
DR PeptideAtlas; Q9BX67; -.
DR PRIDE; Q9BX67; -.
DR ProteomicsDB; 79366; -. [Q9BX67-1]
DR ProteomicsDB; 79367; -. [Q9BX67-2]
DR ABCD; Q9BX67; 4 sequenced antibodies.
DR Antibodypedia; 1117; 432 antibodies from 35 providers.
DR DNASU; 83700; -.
DR Ensembl; ENST00000299106.9; ENSP00000299106.4; ENSG00000166086.13. [Q9BX67-1]
DR Ensembl; ENST00000441717.3; ENSP00000395742.3; ENSG00000166086.13. [Q9BX67-2]
DR GeneID; 83700; -.
DR KEGG; hsa:83700; -.
DR MANE-Select; ENST00000299106.9; ENSP00000299106.4; NM_032801.5; NP_116190.3.
DR UCSC; uc001qhb.4; human. [Q9BX67-1]
DR CTD; 83700; -.
DR DisGeNET; 83700; -.
DR GeneCards; JAM3; -.
DR HGNC; HGNC:15532; JAM3.
DR HPA; ENSG00000166086; Low tissue specificity.
DR MalaCards; JAM3; -.
DR MIM; 606871; gene.
DR MIM; 613730; phenotype.
DR neXtProt; NX_Q9BX67; -.
DR OpenTargets; ENSG00000166086; -.
DR Orphanet; 306547; Porencephaly-microcephaly-bilateral congenital cataract syndrome.
DR PharmGKB; PA29993; -.
DR VEuPathDB; HostDB:ENSG00000166086; -.
DR eggNOG; ENOG502QTVP; Eukaryota.
DR GeneTree; ENSGT00940000156937; -.
DR HOGENOM; CLU_067351_2_0_1; -.
DR InParanoid; Q9BX67; -.
DR OMA; PRPYYSW; -.
DR OrthoDB; 906664at2759; -.
DR PhylomeDB; Q9BX67; -.
DR TreeFam; TF331459; -.
DR PathwayCommons; Q9BX67; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR SignaLink; Q9BX67; -.
DR BioGRID-ORCS; 83700; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; JAM3; human.
DR GeneWiki; JAM3; -.
DR GenomeRNAi; 83700; -.
DR Pharos; Q9BX67; Tbio.
DR PRO; PR:Q9BX67; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BX67; protein.
DR Bgee; ENSG00000166086; Expressed in corpus callosum and 207 other tissues.
DR ExpressionAtlas; Q9BX67; baseline and differential.
DR Genevisible; Q9BX67; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL.
DR GO; GO:0030057; C:desmosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IDA:ARUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:ARUK-UCL.
DR GO; GO:0033010; C:paranodal junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:UniProtKB.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IDA:ARUK-UCL.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:Ensembl.
DR GO; GO:0034333; P:adherens junction assembly; IMP:ARUK-UCL.
DR GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR GO; GO:0045176; P:apical protein localization; IMP:ARUK-UCL.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ARUK-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0097530; P:granulocyte migration; IMP:ARUK-UCL.
DR GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; IMP:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IDA:ARUK-UCL.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IMP:ARUK-UCL.
DR GO; GO:0033624; P:negative regulation of integrin activation; IMP:ARUK-UCL.
DR GO; GO:0001780; P:neutrophil homeostasis; IEA:Ensembl.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:ARUK-UCL.
DR GO; GO:1905710; P:positive regulation of membrane permeability; IMP:ARUK-UCL.
DR GO; GO:1902414; P:protein localization to cell junction; IMP:ARUK-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:ARUK-UCL.
DR GO; GO:0090138; P:regulation of actin cytoskeleton organization by cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
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; IPR042974; JAM-C.
DR PANTHER; PTHR44598; PTHR44598; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell adhesion; Cell junction;
KW Cell membrane; Differentiation; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Secreted; Signal; Spermatogenesis;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 32..310
FT /note="Junctional adhesion molecule C"
FT /id="PRO_0000015071"
FT CHAIN 32..?
FT /note="Soluble form of JAM-C"
FT /id="PRO_0000445336"
FT TOPO_DOM 32..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..127
FT /note="Ig-like V-type"
FT DOMAIN 139..236
FT /note="Ig-like C2-type"
FT LIPID 264
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:28196865"
FT LIPID 265
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:28196865"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 53..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 85..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042561"
FT VARIANT 116
FT /note="E -> K (in HDBSCC; normal location at the cell
FT membrane; dbSNP:rs397515439)"
FT /evidence="ECO:0000269|PubMed:23255084"
FT /id="VAR_069529"
FT VARIANT 219
FT /note="C -> Y (in HDBSCC; the mutant is retained in the
FT endoplasmic reticulum; dbSNP:rs397515438)"
FT /evidence="ECO:0000269|PubMed:23255084"
FT /id="VAR_069530"
FT MUTAGEN 264
FT /note="C->S: Decreased palmitoylation. Abolishes
FT palmitoylation; when associated with S-265."
FT /evidence="ECO:0000269|PubMed:28196865"
FT MUTAGEN 265
FT /note="C->S: Decreased palmitoylation. Abolishes
FT palmitoylation; when associated with S-264."
FT /evidence="ECO:0000269|PubMed:28196865"
FT CONFLICT 136
FT /note="Q -> R (in Ref. 9; AAH10690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 35020 MW; CE39ADF33EA1DAB9 CRC64;
MALRRPPRLR LCARLPDFFL LLLFRGCLIG AVNLKSSNRT PVVQEFESVE LSCIITDSQT
SDPRIEWKKI QDEQTTYVFF DNKIQGDLAG RAEILGKTSL KIWNVTRRDS ALYRCEVVAR
NDRKEIDEIV IELTVQVKPV TPVCRVPKAV PVGKMATLHC QESEGHPRPH YSWYRNDVPL
PTDSRANPRF RNSSFHLNSE TGTLVFTAVH KDDSGQYYCI ASNDAGSARC EEQEMEVYDL
NIGGIIGGVL VVLAVLALIT LGICCAYRRG YFINNKQDGE SYKNPGKPDG VNYIRTDEEG
DFRHKSSFVI
