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 27-MAR-2024, entry version 189. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 34. DR IntAct; Q9BX67; 11. DR MINT; Q9BX67; -. DR STRING; 9606.ENSP00000299106; -. DR GlyConnect; 672; 2 N-Linked glycans (1 site). DR GlyCosmos; Q9BX67; 2 sites, 4 glycans. 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 PaxDb; 9606-ENSP00000299106; -. DR PeptideAtlas; Q9BX67; -. DR ProteomicsDB; 79366; -. [Q9BX67-1] DR ProteomicsDB; 79367; -. [Q9BX67-2] DR Pumba; Q9BX67; -. DR ABCD; Q9BX67; 4 sequenced antibodies. DR Antibodypedia; 1117; 467 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 AGR; HGNC:15532; -. 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; ELSCIIM; -. DR OrthoDB; 3019723at2759; -. 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 1154 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 209 other cell types or tissues. DR ExpressionAtlas; Q9BX67; baseline and differential. 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:0005902; C:microvillus; IDA:ARUK-UCL. DR GO; GO:0033010; C:paranodal junction; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. 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:1905710; P:positive regulation of membrane permeability; IMP:ARUK-UCL. DR GO; GO:2000439; P:positive regulation of monocyte extravasation; 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 CDD; cd20946; IgV_1_JAM1-like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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; JUNCTIONAL ADHESION MOLECULE C; 1. DR PANTHER; PTHR44598:SF2; JUNCTIONAL ADHESION MOLECULE C; 1. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; Q9BX67; HS. 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 //