JAM3_MOUSE
ID JAM3_MOUSE Reviewed; 310 AA.
AC Q9D8B7; Q8BT59; Q9D1M9; Q9EPK4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Junctional adhesion molecule C;
DE Short=JAM-C;
DE AltName: Full=JAM-2 {ECO:0000303|PubMed:11053409, ECO:0000303|PubMed:11739175};
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11036763; DOI=10.1007/978-3-642-57276-0_12;
RA Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.;
RT "Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular
RT family?";
RL Curr. Top. Microbiol. Immunol. 251:91-98(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11053409; DOI=10.1074/jbc.m005458200;
RA Aurrand-Lions M.A., Duncan L., Ballestrem C., Imhof B.A.;
RT "JAM-2, a novel immunoglobulin superfamily molecule, expressed by
RT endothelial and lymphatic cells.";
RL J. Biol. Chem. 276:2733-2741(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Small intestine, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP PROTEIN SEQUENCE OF 84-91 AND 146-154, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [7]
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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 [9]
RP FUNCTION.
RX PubMed=16297198; DOI=10.1111/j.0022-202x.2005.23912.x;
RA Ludwig R.J., Zollner T.M., Santoso S., Hardt K., Gille J., Baatz H.,
RA Johann P.S., Pfeffer J., Radeke H.H., Schoen M.P., Kaufmann R.,
RA Boehncke W.H., Podda M.;
RT "Junctional adhesion molecules (JAM)-B and -C contribute to leukocyte
RT extravasation to the skin and mediate cutaneous inflammation.";
RL J. Invest. Dermatol. 125:969-976(2005).
RN [10]
RP FUNCTION IN ANGIOGENESIS.
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF GLU-66.
RX PubMed=16093349; DOI=10.1091/mbc.e05-04-0310;
RA Lamagna C., Meda P., Mandicourt G., Brown J., Gilbert R.J., Jones E.Y.,
RA Kiefer F., Ruga P., Imhof B.A., Aurrand-Lions M.;
RT "Dual interaction of JAM-C with JAM-B and alpha(M)beta2 integrin: function
RT in junctional complexes and leukocyte adhesion.";
RL Mol. Biol. Cell 16:4992-5003(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION IN ANGIOGENESIS (SOLUBLE FORM OF JAM-C).
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 [15]
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 [16] {ECO:0007744|PDB:5GMI}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 292-310 IN COMPLEX WITH GORASP2,
RP INTERACTION WITH GORASP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=28617811; DOI=10.1371/journal.pgen.1006803;
RA Cartier-Michaud A., Bailly A.L., Betzi S., Shi X., Lissitzky J.C.,
RA Zarubica A., Serge A., Roche P., Lugari A., Hamon V., Bardin F.,
RA Derviaux C., Lembo F., Audebert S., Marchetto S., Durand B., Borg J.P.,
RA Shi N., Morelli X., Aurrand-Lions M.;
RT "Genetic, structural, and chemical insights into the dual function of
RT GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization
RT during spermatogenesis.";
RL PLoS Genet. 13:e1006803-e1006803(2017).
CC -!- FUNCTION: Junctional adhesion protein that mediates heterotypic cell-
CC cell interactions with its cognate receptor JAM2 to regulate different
CC cellular processes (PubMed:15372036, PubMed:16093349). 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:24357068). Plays a central role in
CC leukocytes extravasation by facilitating transmigration through the
CC endothelium (PubMed:16297198). Plays a role in spermatogenesis where
CC JAM2 and JAM3, which are respectively expressed by Sertoli and germ
CC cells, mediate an interaction between both cell types and play an
CC essential role in the anchorage of germ cells onto Sertoli cells and
CC the assembly of cell polarity complexes during spermatid
CC differentiation (PubMed:15372036, PubMed:15994945). Also functions as a
CC counter-receptor for ITGAM, mediating leukocyte-platelet interactions
CC and is involved in the regulation of transepithelial migration of
CC polymorphonuclear neutrophils (PMN) (PubMed:16093349). Plays a role in
CC angiogenesis (PubMed:15994945). Plays a role in the regulation of cell
CC migration (By similarity). During myogenesis, it is involved in myocyte
CC fusion (By similarity). {ECO:0000250|UniProtKB:A3KPA0,
CC ECO:0000250|UniProtKB:Q9BX67, ECO:0000269|PubMed:15372036,
CC ECO:0000269|PubMed:15994945, ECO:0000269|PubMed:16093349,
CC ECO:0000269|PubMed:16297198, ECO:0000269|PubMed:24357068}.
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 (By similarity). Interacts with GORASP2
CC (PubMed:28617811). {ECO:0000250|UniProtKB:Q9BX67,
CC ECO:0000269|PubMed:28617811}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11053409,
CC ECO:0000269|PubMed:11739175, ECO:0000269|PubMed:16093349}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:Q9BX67}. Cell junction
CC {ECO:0000269|PubMed:11053409, ECO:0000269|PubMed:16093349}. Cell
CC junction, desmosome {ECO:0000250|UniProtKB:Q9BX67}. Cell junction,
CC tight junction {ECO:0000269|PubMed:11053409,
CC ECO:0000269|PubMed:11739175}. Note=Detected in the acrosome region in
CC developing spermatids (PubMed:28617811). In epithelial cells, it is
CC expressed at desmosomes but not at tight junctions (By similarity).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BX67, ECO:0000269|PubMed:28617811}.
CC -!- SUBCELLULAR LOCATION: [Soluble form of JAM-C]: Secreted
CC {ECO:0000250|UniProtKB:Q9BX67}.
CC -!- TISSUE SPECIFICITY: Colocalizes with Jam2 near the lumen of
CC seminiferous tubulues. Detected at junctional plaques that correspond
CC to cell-cell contacts between spermatids and Sertoli cells
CC (PubMed:15372036, PubMed:28617811). Detected on endothelial cells, in
CC brain vessels and kidney glomeruli (at protein level) (PubMed:11053409,
CC PubMed:11739175). Detected in heart, lung, liver, kidney, testis,
CC thymus, lymph node and Peyer patch (PubMed:11053409, PubMed:11739175).
CC Endothelial cells (PubMed:11739175). {ECO:0000269|PubMed:11053409,
CC ECO:0000269|PubMed:11739175, ECO:0000269|PubMed:15372036,
CC ECO:0000269|PubMed:28617811}.
CC -!- DEVELOPMENTAL STAGE: Detected in diploid pre-meiotic spermatocytes,
CC haploid spermatids and elongated spermatids (PubMed:28617811,
CC PubMed:15372036). Restricted to junctional plaques in the heads of
CC elongated spermatids (at protein level) (PubMed:15372036).
CC {ECO:0000269|PubMed:15372036, ECO:0000269|PubMed:28617811}.
CC -!- DOMAIN: The Ig-like V-type domain mediates interaction with JAM2.
CC {ECO:0000269|PubMed:16093349}.
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:0000250|UniProtKB:Q9BX67}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11053409}.
CC -!- PTM: S-palmitoylated by ZDHHC7. S-palmitoylation promotes expression at
CC tight junctions. {ECO:0000250|UniProtKB:Q9BX67}.
CC -!- DISRUPTION PHENOTYPE: Important mortality during the postnatal period;
CC about 40% of the mutant mice survive. Mutant males are infertile; they
CC have strongly reduced testis size and fail to produce mature sperm
CC cells. Developing spermatids fail to become polarized, and do not form
CC acrosomes. {ECO:0000269|PubMed:15372036}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AJ300304; CAC20704.1; -; mRNA.
DR EMBL; AK008187; BAB25519.1; -; mRNA.
DR EMBL; AK003326; BAB22715.1; -; mRNA.
DR EMBL; AK013156; BAB28683.1; -; mRNA.
DR EMBL; AK017692; BAC25526.1; -; mRNA.
DR EMBL; AK032833; BAC28049.1; -; mRNA.
DR EMBL; BC024357; AAH24357.1; -; mRNA.
DR CCDS; CCDS22939.1; -.
DR RefSeq; NP_075766.1; NM_023277.4.
DR PDB; 5GMI; X-ray; 2.71 A; C/D=292-310.
DR PDBsum; 5GMI; -.
DR AlphaFoldDB; Q9D8B7; -.
DR SMR; Q9D8B7; -.
DR BioGRID; 219990; 1.
DR CORUM; Q9D8B7; -.
DR DIP; DIP-42154N; -.
DR IntAct; Q9D8B7; 1.
DR MINT; Q9D8B7; -.
DR STRING; 10090.ENSMUSP00000034472; -.
DR GlyConnect; 2448; 4 N-Linked glycans (1 site).
DR GlyGen; Q9D8B7; 2 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q9D8B7; -.
DR PhosphoSitePlus; Q9D8B7; -.
DR SwissPalm; Q9D8B7; -.
DR MaxQB; Q9D8B7; -.
DR PaxDb; Q9D8B7; -.
DR PeptideAtlas; Q9D8B7; -.
DR PRIDE; Q9D8B7; -.
DR ProteomicsDB; 269359; -.
DR Antibodypedia; 1117; 432 antibodies from 35 providers.
DR DNASU; 83964; -.
DR Ensembl; ENSMUST00000034472; ENSMUSP00000034472; ENSMUSG00000031990.
DR GeneID; 83964; -.
DR KEGG; mmu:83964; -.
DR UCSC; uc009oqj.2; mouse.
DR CTD; 83700; -.
DR MGI; MGI:1933825; Jam3.
DR VEuPathDB; HostDB:ENSMUSG00000031990; -.
DR eggNOG; ENOG502QTVP; Eukaryota.
DR GeneTree; ENSGT00940000156937; -.
DR HOGENOM; CLU_067351_2_0_1; -.
DR InParanoid; Q9D8B7; -.
DR OMA; PRPYYSW; -.
DR OrthoDB; 906664at2759; -.
DR PhylomeDB; Q9D8B7; -.
DR TreeFam; TF331459; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR BioGRID-ORCS; 83964; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Jam3; mouse.
DR PRO; PR:Q9D8B7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D8B7; protein.
DR Bgee; ENSMUSG00000031990; Expressed in ectoplacental cone and 250 other tissues.
DR Genevisible; Q9D8B7; MM.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0030057; C:desmosome; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0033010; C:paranodal junction; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; ISS:UniProtKB.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:MGI.
DR GO; GO:0070160; C:tight junction; ISO:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005178; F:integrin binding; IPI:MGI.
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; IMP:MGI.
DR GO; GO:0034333; P:adherens junction assembly; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR GO; GO:0045176; P:apical protein localization; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IDA:MGI.
DR GO; GO:0097530; P:granulocyte migration; ISO:MGI.
DR GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; IMP:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IMP:MGI.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:0033624; P:negative regulation of integrin activation; ISO:MGI.
DR GO; GO:0001780; P:neutrophil homeostasis; IMP:MGI.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:MGI.
DR GO; GO:1905710; P:positive regulation of membrane permeability; ISO:MGI.
DR GO; GO:1902414; P:protein localization to cell junction; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
DR GO; GO:0090138; P:regulation of actin cytoskeleton organization by cell-cell adhesion; IMP:MGI.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
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 3D-structure; Angiogenesis; Cell adhesion; Cell junction; Cell membrane;
KW Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal; Spermatogenesis; Tight junction;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..310
FT /note="Junctional adhesion molecule C"
FT /id="PRO_0000015072"
FT CHAIN 31..?
FT /note="Soluble form of JAM-C"
FT /id="PRO_0000445337"
FT TOPO_DOM 30..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:0000250|UniProtKB:Q9BX67"
FT LIPID 265
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX67"
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:19656770"
FT DISULFID 53..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 66
FT /note="E->R: Decreased binding to JAM2."
FT /evidence="ECO:0000269|PubMed:16093349"
FT CONFLICT 44
FT /note="H -> Q (in Ref. 3; BAB25519)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="S -> N (in Ref. 3; BAB25519)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="R -> K (in Ref. 3; BAB22715)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..307
FT /note="SS -> IA (in Ref. 3; BAB22715)"
FT /evidence="ECO:0000305"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5GMI"
SQ SEQUENCE 310 AA; 34838 MW; 4B92BCB51D0A4B0A CRC64;
MALSRRLRLR LYARLPDFFL LLLFRGCMIE AVNLKSSNRN PVVHEFESVE LSCIITDSQT
SDPRIEWKKI QDGQTTYVYF DNKIQGDLAG RTDVFGKTSL RIWNVTRSDS AIYRCEVVAL
NDRKEVDEIT IELIVQVKPV TPVCRIPAAV PVGKTATLQC QESEGYPRPH YSWYRNDVPL
PTDSRANPRF QNSSFHVNSE TGTLVFNAVH KDDSGQYYCI ASNDAGAARC EGQDMEVYDL
NIAGIIGGVL VVLIVLAVIT MGICCAYRRG CFISSKQDGE SYKSPGKHDG VNYIRTSEEG
DFRHKSSFVI
