JAM2_HUMAN
ID JAM2_HUMAN Reviewed; 298 AA.
AC P57087; B2R6T9; B4DGT9; Q6UXG6; Q6YNC1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Junctional adhesion molecule B;
DE Short=JAM-B;
DE AltName: Full=Junctional adhesion molecule 2 {ECO:0000303|PubMed:10945976};
DE Short=JAM-2 {ECO:0000303|PubMed:10945976};
DE AltName: Full=Vascular endothelial junction-associated molecule {ECO:0000303|PubMed:10779521};
DE Short=VE-JAM {ECO:0000303|PubMed:10779521};
DE AltName: CD_antigen=CD322;
DE Flags: Precursor;
GN Name=JAM2 {ECO:0000312|HGNC:HGNC:14686};
GN Synonyms=C21orf43 {ECO:0000312|HGNC:HGNC:14686},
GN VEJAM {ECO:0000303|PubMed:10779521}; ORFNames=UNQ219/PRO245;
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), PROTEIN SEQUENCE OF 29-33,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RC TISSUE=Vascular endothelial cell;
RX PubMed=10779521; DOI=10.1074/jbc.m003189200;
RA Palmeri D., van Zante A., Huang C.-C., Hemmerich S., Rosen S.D.;
RT "Vascular endothelial junction-associated molecule, a novel member of the
RT immunoglobulin superfamily, is localized to intercellular boundaries of
RT endothelial cells.";
RL J. Biol. Chem. 275:19139-19145(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10945976; DOI=10.1074/jbc.m002718200;
RA Cunningham S.A., Arrate M.P., Rodriguez J.M., Bjercke R.J., Vanderslice P.,
RA Morris A.P., Brock T.A.;
RT "A novel protein with homology to the junctional adhesion molecule:
RT Characterization of leukocyte interactions.";
RL J. Biol. Chem. 275:34750-34756(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12036298; DOI=10.1006/geno.2002.6782;
RA Gardiner K., Slavov D., Bechtel L., Davisson M.;
RT "Annotation of human chromosome 21 for relevance to Down syndrome: gene
RT structure and expression analysis.";
RL Genomics 79:833-843(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [8]
RP PROTEIN SEQUENCE OF 29-43.
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
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 [10]
RP FUNCTION.
RX PubMed=12239159; DOI=10.1182/blood-2001-11-0098;
RA Johnson-Leger C.A., Aurrand-Lions M., Beltraminelli N., Fasel N.,
RA Imhof B.A.;
RT "Junctional adhesion molecule-2 (JAM-2) promotes lymphocyte
RT transendothelial migration.";
RL Blood 100:2479-2486(2002).
RN [11]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ASP-82.
RX PubMed=12070135; DOI=10.1074/jbc.c200331200;
RA Cunningham S.A., Rodriguez J.M., Arrate M.P., Tran T.M., Brock T.A.;
RT "JAM2 interacts with alpha4beta1. Facilitation by JAM3.";
RL J. Biol. Chem. 277:27589-27592(2002).
RN [12]
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 [13]
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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
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]
RP INVOLVEMENT IN IBGC8, VARIANTS IBGC8 60-ARG--ILE-298 DEL; HIS-108 AND
RP 229-ARG--ILE-298 DEL, AND CHARACTERIZATION OF VARIANT IBGC8
RP 229-ARG--ILE-298 DEL.
RX PubMed=32142645; DOI=10.1016/j.ajhg.2020.02.007;
RG SYNAPS Study Group;
RA Schottlaender L.V., Abeti R., Jaunmuktane Z., Macmillan C., Chelban V.,
RA O'Callaghan B., McKinley J., Maroofian R., Efthymiou S.,
RA Athanasiou-Fragkouli A., Forbes R., Soutar M.P.M., Livingston J.H.,
RA Kalmar B., Swayne O., Hotton G., Pittman A., Mendes de Oliveira J.R.,
RA de Grandis M., Richard-Loendt A., Launchbury F., Althonayan J.,
RA McDonnell G., Carr A., Khan S., Beetz C., Bisgin A., Tug Bozdogan S.,
RA Begtrup A., Torti E., Greensmith L., Giunti P., Morrison P.J., Brandner S.,
RA Aurrand-Lions M., Houlden H.;
RT "Bi-allelic JAM2 Variants Lead to Early-Onset Recessive Primary Familial
RT Brain Calcification.";
RL Am. J. Hum. Genet. 106:412-421(2020).
RN [17]
RP VARIANT IBGC8 CYS-168, CHARACTERIZATION OF VARIANT IBGC8 CYS-168,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31851307; DOI=10.1093/brain/awz392;
RA Cen Z., Chen Y., Chen S., Wang H., Yang D., Zhang H., Wu H., Wang L.,
RA Tang S., Ye J., Shen J., Wang H., Fu F., Chen X., Xie F., Liu P., Xu X.,
RA Cao J., Cai P., Pan Q., Li J., Yang W., Shan P.F., Li Y., Liu J.Y.,
RA Zhang B., Luo W.;
RT "Biallelic loss-of-function mutations in JAM2 cause primary familial brain
RT calcification.";
RL Brain 143:491-502(2020).
CC -!- FUNCTION: Junctional adhesion protein that mediates heterotypic cell-
CC cell interactions with its cognate receptor JAM3 to regulate different
CC cellular processes (PubMed:11590146, PubMed:11823489, PubMed:24357068).
CC Plays a role in homing and mobilization of hematopoietic stem and
CC progenitor cells within the bone marrow (PubMed:24357068). At the
CC surface of bone marrow stromal cells, it contributes to the retention
CC of the hematopoietic stem and progenitor cells expressing JAM3
CC (PubMed:11590146, PubMed:24357068). Plays a central role in leukocytes
CC extravasation by facilitating not only transmigration but also
CC tethering and rolling of leukocytes along the endothelium
CC (PubMed:12239159). Tethering and rolling of leukocytes are dependent on
CC the binding by JAM2 of the integrin alpha-4/beta-1 (PubMed:12070135).
CC Plays a role in spermatogenesis where JAM2 and JAM3, which are
CC respectively expressed by Sertoli and germ cells, mediate an
CC interaction between both cell types and play an essential role in the
CC anchorage of germ cells onto Sertoli cells and the assembly of cell
CC polarity complexes during spermatid differentiation (By similarity).
CC Also functions as an inhibitory somatodendritic cue that prevents the
CC myelination of non-axonal parts of neurons (By similarity). During
CC myogenesis, it is involved in myocyte fusion (By similarity). May also
CC play a role in angiogenesis (By similarity).
CC {ECO:0000250|UniProtKB:A0A0R4IGV4, ECO:0000250|UniProtKB:Q9JI59,
CC ECO:0000269|PubMed:11590146, ECO:0000269|PubMed:11823489,
CC ECO:0000269|PubMed:12070135, ECO:0000269|PubMed:12239159,
CC ECO:0000269|PubMed:24357068}.
CC -!- INTERACTION:
CC P57087; Q9BX67: JAM3; NbExp=2; IntAct=EBI-3918416, EBI-4314733;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10779521,
CC ECO:0000269|PubMed:11590146, ECO:0000269|PubMed:31851307}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:10779521,
CC ECO:0000269|PubMed:11590146}. Cell junction
CC {ECO:0000269|PubMed:10779521, ECO:0000269|PubMed:10945976}. Cell
CC junction, tight junction {ECO:0000250|UniProtKB:Q9JI59}. Note=Localized
CC at tight junctions of both epithelial and endothelial cells (By
CC similarity). Specifically localized within the somatodendritic
CC compartment of neurons and excluded from the axon (By similarity).
CC {ECO:0000250|UniProtKB:Q9JI59}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P57087-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57087-2; Sequence=VSP_045153;
CC Name=3;
CC IsoId=P57087-3; Sequence=VSP_047352;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta, lung, foreskin
CC and lymph node (PubMed:10779521, PubMed:10945976). Prominently
CC expressed on high endothelial venules and also present on the
CC endothelia of other vessels (at protein level) (PubMed:10779521,
CC PubMed:10945976). Also expressed in the brain in the caudate nuclei
CC (PubMed:31851307). {ECO:0000269|PubMed:10779521,
CC ECO:0000269|PubMed:10945976, ECO:0000269|PubMed:31851307}.
CC -!- DOMAIN: The Ig-like V-type domain is necessary and sufficient to
CC mediate interaction with JAM3 and integrin alpha-4/beta-1.
CC {ECO:0000269|PubMed:12070135}.
CC -!- DISEASE: Basal ganglia calcification, idiopathic, 8, autosomal
CC recessive (IBGC8) [MIM:618824]: A form of basal ganglia calcification,
CC a genetically heterogeneous condition characterized by symmetric
CC calcification in the basal ganglia and other brain regions. Affected
CC individuals can either be asymptomatic or show a wide spectrum of
CC neuropsychiatric symptoms, including parkinsonism, dystonia, tremor,
CC ataxia, dementia, psychosis, seizures, and chronic headache. Serum
CC levels of calcium, phosphate, alkaline phosphatase and parathyroid
CC hormone are normal. The neuropathological hallmark of the disease is
CC vascular and pericapillary calcification, mainly of calcium phosphate,
CC in the affected brain areas. {ECO:0000269|PubMed:31851307,
CC ECO:0000269|PubMed:32142645}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AF255910; AAF81223.1; -; mRNA.
DR EMBL; AY016009; AAG49022.1; -; mRNA.
DR EMBL; AY077698; AAL82538.1; -; mRNA.
DR EMBL; AY358361; AAQ88727.1; -; mRNA.
DR EMBL; AK294769; BAG57900.1; -; mRNA.
DR EMBL; AK312708; BAG35586.1; -; mRNA.
DR EMBL; AP000223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017779; AAH17779.1; -; mRNA.
DR CCDS; CCDS42911.1; -. [P57087-1]
DR CCDS; CCDS58787.1; -. [P57087-3]
DR CCDS; CCDS58788.1; -. [P57087-2]
DR RefSeq; NP_001257336.1; NM_001270407.1. [P57087-2]
DR RefSeq; NP_001257337.1; NM_001270408.1. [P57087-3]
DR RefSeq; NP_067042.1; NM_021219.3. [P57087-1]
DR AlphaFoldDB; P57087; -.
DR SMR; P57087; -.
DR BioGRID; 121824; 12.
DR CORUM; P57087; -.
DR IntAct; P57087; 8.
DR MINT; P57087; -.
DR STRING; 9606.ENSP00000383376; -.
DR GlyGen; P57087; 3 sites.
DR iPTMnet; P57087; -.
DR PhosphoSitePlus; P57087; -.
DR SwissPalm; P57087; -.
DR BioMuta; JAM2; -.
DR DMDM; 10720348; -.
DR EPD; P57087; -.
DR jPOST; P57087; -.
DR MassIVE; P57087; -.
DR MaxQB; P57087; -.
DR PaxDb; P57087; -.
DR PeptideAtlas; P57087; -.
DR PRIDE; P57087; -.
DR ProteomicsDB; 4159; -.
DR ProteomicsDB; 56996; -. [P57087-1]
DR Antibodypedia; 4909; 476 antibodies from 38 providers.
DR DNASU; 58494; -.
DR Ensembl; ENST00000312957.9; ENSP00000318416.6; ENSG00000154721.15. [P57087-2]
DR Ensembl; ENST00000400532.5; ENSP00000383376.1; ENSG00000154721.15. [P57087-3]
DR Ensembl; ENST00000480456.6; ENSP00000420419.1; ENSG00000154721.15. [P57087-1]
DR GeneID; 58494; -.
DR KEGG; hsa:58494; -.
DR MANE-Select; ENST00000480456.6; ENSP00000420419.1; NM_021219.4; NP_067042.1.
DR UCSC; uc002ylp.3; human. [P57087-1]
DR CTD; 58494; -.
DR DisGeNET; 58494; -.
DR GeneCards; JAM2; -.
DR HGNC; HGNC:14686; JAM2.
DR HPA; ENSG00000154721; Tissue enhanced (placenta).
DR MalaCards; JAM2; -.
DR MIM; 606870; gene.
DR MIM; 618824; phenotype.
DR neXtProt; NX_P57087; -.
DR OpenTargets; ENSG00000154721; -.
DR Orphanet; 1980; Bilateral striopallidodentate calcinosis.
DR PharmGKB; PA29992; -.
DR VEuPathDB; HostDB:ENSG00000154721; -.
DR eggNOG; ENOG502QZ6E; Eukaryota.
DR GeneTree; ENSGT00940000160634; -.
DR HOGENOM; CLU_067351_1_0_1; -.
DR InParanoid; P57087; -.
DR OMA; GVYYAQK; -.
DR OrthoDB; 1034087at2759; -.
DR PhylomeDB; P57087; -.
DR TreeFam; TF331459; -.
DR PathwayCommons; P57087; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR SignaLink; P57087; -.
DR BioGRID-ORCS; 58494; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; JAM2; human.
DR GeneWiki; JAM2; -.
DR GenomeRNAi; 58494; -.
DR Pharos; P57087; Tbio.
DR PRO; PR:P57087; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P57087; protein.
DR Bgee; ENSG00000154721; Expressed in ventricular zone and 196 other tissues.
DR ExpressionAtlas; P57087; baseline and differential.
DR Genevisible; P57087; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:UniProtKB.
DR GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0045123; P:cellular extravasation; IDA:UniProtKB.
DR GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; IMP:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IDA:ARUK-UCL.
DR GO; GO:0071593; P:lymphocyte aggregation; IDA:ARUK-UCL.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; ISS:UniProtKB.
DR GO; GO:2000403; P:positive regulation of lymphocyte migration; IDA:ARUK-UCL.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR042625; JAM2.
DR PANTHER; PTHR44663; PTHR44663; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:10779521,
FT ECO:0000269|PubMed:15340161"
FT CHAIN 29..298
FT /note="Junctional adhesion molecule B"
FT /id="PRO_0000015069"
FT TOPO_DOM 29..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..127
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 134..238
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 44..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045153"
FT VAR_SEQ 289..298
FT /note="DFKHTKSFII -> VQWLTPVIPALWKAAAGGSRGQEF (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_047352"
FT VARIANT 60..298
FT /note="Missing (in IBGC8)"
FT /evidence="ECO:0000269|PubMed:32142645"
FT /id="VAR_083943"
FT VARIANT 108
FT /note="R -> H (in IBGC8; dbSNP:rs1383641309)"
FT /evidence="ECO:0000269|PubMed:32142645"
FT /id="VAR_083944"
FT VARIANT 168
FT /note="W -> C (in IBGC8; loss of localization to the plasma
FT membrane; mainly retained in the cytoplasm;
FT dbSNP:rs1230941179)"
FT /evidence="ECO:0000269|PubMed:31851307"
FT /id="VAR_083945"
FT VARIANT 229..298
FT /note="Missing (in IBGC8; loss of protein expression)"
FT /evidence="ECO:0000269|PubMed:32142645"
FT /id="VAR_083946"
FT VARIANT 286
FT /note="S -> R (in dbSNP:rs9976382)"
FT /id="VAR_049973"
FT MUTAGEN 82
FT /note="D->A: No effect on binding of JAM3 or integrin."
FT /evidence="ECO:0000269|PubMed:12070135"
FT CONFLICT 270
FT /note="E -> G (in Ref. 3; AAL82538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33207 MW; CA78E518E22DCAEE CRC64;
MARRSRHRLL LLLLRYLVVA LGYHKAYGFS APKDQQVVTA VEYQEAILAC KTPKKTVSSR
LEWKKLGRSV SFVYYQQTLQ GDFKNRAEMI DFNIRIKNVT RSDAGKYRCE VSAPSEQGQN
LEEDTVTLEV LVAPAVPSCE VPSSALSGTV VELRCQDKEG NPAPEYTWFK DGIRLLENPR
LGSQSTNSSY TMNTKTGTLQ FNTVSKLDTG EYSCEARNSV GYRRCPGKRM QVDDLNISGI
IAAVVVVALV ISVCGLGVCY AQRKGYFSKE TSFQKSNSSS KATTMSENDF KHTKSFII
