JAM2_MOUSE
ID JAM2_MOUSE Reviewed; 298 AA.
AC Q9JI59; A6X955; Q8C5K9; Q8CE95;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Junctional adhesion molecule B;
DE Short=JAM-B;
DE AltName: Full=Junctional adhesion molecule 2 {ECO:0000303|PubMed:11036763};
DE Short=JAM-2 {ECO:0000303|PubMed:11036763};
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|MGI:MGI:1933820};
GN Synonyms=Vejam {ECO:0000303|PubMed:10779521};
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], AND PROTEIN SEQUENCE OF 29-33.
RC STRAIN=C57BL/6J;
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], AND SUBCELLULAR LOCATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Medulla oblongata, and Skin;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [10]
RP FUNCTION.
RX PubMed=19740376; DOI=10.1111/j.1365-2567.2009.03100.x;
RA Ludwig R.J., Hardt K., Hatting M., Bistrian R., Diehl S., Radeke H.H.,
RA Podda M., Schoen M.P., Kaufmann R., Henschler R., Pfeilschifter J.M.,
RA Santoso S., Boehncke W.H.;
RT "Junctional adhesion molecule (JAM)-B supports lymphocyte rolling and
RT adhesion through interaction with alpha4beta1 integrin.";
RL Immunology 128:196-205(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [12]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21868569; DOI=10.1182/blood-2010-12-323972;
RA Arcangeli M.L., Frontera V., Bardin F., Obrados E., Adams S., Chabannon C.,
RA Schiff C., Mancini S.J., Adams R.H., Aurrand-Lions M.;
RT "JAM-B regulates maintenance of hematopoietic stem cells in the bone
RT marrow.";
RL Blood 118:4609-4619(2011).
RN [13]
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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND UBIQUITINATION.
RX PubMed=25817991; DOI=10.1016/j.bbagrm.2015.03.005;
RA Zhang X., Lui W.Y.;
RT "Transforming growth factor-beta3 regulates cell junction restructuring via
RT MAPK-mediated mRNA destabilization and Smad-dependent protein degradation
RT of junctional adhesion molecule B (JAM-B).";
RL Biochim. Biophys. Acta 1849:601-611(2015).
RN [15]
RP FUNCTION.
RX PubMed=25911611; DOI=10.1096/fj.15-270223;
RA Meguenani M., Miljkovic-Licina M., Fagiani E., Ropraz P., Hammel P.,
RA Aurrand-Lions M., Adams R.H., Christofori G., Imhof B.A.,
RA Garrido-Urbani S.;
RT "Junctional adhesion molecule B interferes with angiogenic VEGF/VEGFR2
RT signaling.";
RL FASEB J. 29:3411-3425(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27499083; DOI=10.1016/j.neuron.2016.07.021;
RA Redmond S.A., Mei F., Eshed-Eisenbach Y., Osso L.A., Leshkowitz D.,
RA Shen Y.A., Kay J.N., Aurrand-Lions M., Lyons D.A., Peles E., Chan J.R.;
RT "Somatodendritic Expression of JAM2 Inhibits Oligodendrocyte Myelination.";
RL Neuron 91:824-836(2016).
RN [17]
RP DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Junctional adhesion protein that mediates heterotypic cell-
CC cell interactions with its cognate receptor JAM3 to regulate different
CC cellular processes (PubMed:16093349, PubMed:21868569, PubMed:24357068).
CC Plays a role in homing and mobilization of hematopoietic stem and
CC progenitor cells within the bone marrow (PubMed:21868569,
CC PubMed:24357068). 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:21868569, PubMed:24357068). Plays a
CC central role in leukocytes extravasation by facilitating not only
CC transmigration but also tethering and rolling of leukocytes along the
CC endothelium (PubMed:16297198, PubMed:19740376). Tethering and rolling
CC of leukocytes are dependent on the binding by JAM2 of the integrin
CC alpha-4/beta-1 (PubMed:19740376). 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 (Probable). Also functions as an inhibitory
CC somatodendritic cue that prevents the myelination of non-axonal parts
CC of neurons (PubMed:27499083). During myogenesis, it is involved in
CC myocyte fusion (By similarity). May also play a role in angiogenesis
CC (PubMed:25911611). {ECO:0000250|UniProtKB:A0A0R4IGV4,
CC ECO:0000269|PubMed:16093349, ECO:0000269|PubMed:16297198,
CC ECO:0000269|PubMed:19740376, ECO:0000269|PubMed:21868569,
CC ECO:0000269|PubMed:24357068, ECO:0000269|PubMed:25911611,
CC ECO:0000269|PubMed:27499083, ECO:0000305|PubMed:15372036,
CC ECO:0000305|PubMed:25817991}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11036763,
CC ECO:0000269|PubMed:25817991}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P57087}. Cell junction
CC {ECO:0000269|PubMed:16093349, ECO:0000269|PubMed:25817991}. Cell
CC junction, tight junction {ECO:0000269|PubMed:11036763,
CC ECO:0000269|PubMed:15372036}. Note=Localized at tight junctions of both
CC epithelial, endothelial cells and Sertoli cells (PubMed:11036763).
CC Specifically localized within the somatodendritic compartment of
CC neurons and excluded from the axon (PubMed:27499083).
CC {ECO:0000269|PubMed:11036763, ECO:0000269|PubMed:27499083}.
CC -!- TISSUE SPECIFICITY: Expressed by bone marrow stromal cells (at protein
CC level) (PubMed:21868569). Expressed in skin (at protein level)
CC (PubMed:16297198). Expressed in testis by Sertoli cells (at protein
CC level) (PubMed:15372036, PubMed:25817991). Expressed by dorsal root
CC ganglion and spinal cord neurons (PubMed:27499083).
CC {ECO:0000269|PubMed:15372036, ECO:0000269|PubMed:16297198,
CC ECO:0000269|PubMed:21868569, ECO:0000269|PubMed:25817991,
CC ECO:0000269|PubMed:27499083}.
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:0000250|UniProtKB:P57087}.
CC -!- PTM: The expression in Sertoli cells is regulated by TGFB3 through
CC ubiquitin-mediated proteasomal degradation.
CC {ECO:0000269|PubMed:25817991}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Jam2 do not display overt
CC morphological, vascular or immunologic phenotype (PubMed:21868569).
CC However, aberrant myelination of dorsal horn interneuron cell bodies is
CC observed (PubMed:27499083, PubMed:21868569). They develop age-dependent
CC significant walking and gait abnormalities compared to controls.
CC Neuropathologic brain analysis show age-dependent progressive prominent
CC vacuolization in the midbrain, thalamus, and cerebral and cerebellar
CC cortices. These changes are associated with reactive astrogliosis,
CC microglial activation, and a reduced neuronal density. Similar findings
CC are observed in spinal cord sections. There is no evidence of
CC mineralization or calcification in the brain or spinal cord of mutant
CC mice (PubMed:32142645). {ECO:0000269|PubMed:21868569,
CC ECO:0000269|PubMed:27499083, ECO:0000269|PubMed:32142645}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AF255911; AAF81224.1; -; mRNA.
DR EMBL; AJ291757; CAC20699.1; -; mRNA.
DR EMBL; AK010616; BAB27064.1; -; mRNA.
DR EMBL; AK013914; BAB29053.1; -; mRNA.
DR EMBL; AK028757; BAC26102.1; -; mRNA.
DR EMBL; AK078128; BAC37139.1; -; mRNA.
DR EMBL; AC164162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT027693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028778; AAH28778.1; -; mRNA.
DR CCDS; CCDS37381.1; -.
DR RefSeq; NP_076333.3; NM_023844.5.
DR PDB; 5GMJ; X-ray; 2.99 A; C/D=280-298.
DR PDBsum; 5GMJ; -.
DR AlphaFoldDB; Q9JI59; -.
DR SMR; Q9JI59; -.
DR DIP; DIP-61078N; -.
DR IntAct; Q9JI59; 1.
DR STRING; 10090.ENSMUSP00000109833; -.
DR GlyConnect; 2447; 1 N-Linked glycan (1 site).
DR GlyGen; Q9JI59; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9JI59; -.
DR PhosphoSitePlus; Q9JI59; -.
DR SwissPalm; Q9JI59; -.
DR MaxQB; Q9JI59; -.
DR PaxDb; Q9JI59; -.
DR PeptideAtlas; Q9JI59; -.
DR PRIDE; Q9JI59; -.
DR ProteomicsDB; 269358; -.
DR Antibodypedia; 4909; 476 antibodies from 38 providers.
DR DNASU; 67374; -.
DR Ensembl; ENSMUST00000114195; ENSMUSP00000109833; ENSMUSG00000053062.
DR GeneID; 67374; -.
DR KEGG; mmu:67374; -.
DR UCSC; uc007ztg.2; mouse.
DR CTD; 58494; -.
DR MGI; MGI:1933820; Jam2.
DR VEuPathDB; HostDB:ENSMUSG00000053062; -.
DR eggNOG; ENOG502QZ6E; Eukaryota.
DR GeneTree; ENSGT00940000160634; -.
DR HOGENOM; CLU_067351_0_0_1; -.
DR InParanoid; Q9JI59; -.
DR OMA; ILLMQCL; -.
DR OrthoDB; 1034087at2759; -.
DR PhylomeDB; Q9JI59; -.
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; 67374; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9JI59; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JI59; protein.
DR Bgee; ENSMUSG00000053062; Expressed in interventricular septum and 219 other tissues.
DR ExpressionAtlas; Q9JI59; baseline and differential.
DR Genevisible; Q9JI59; MM.
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; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; ISS:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:0070160; C:tight junction; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS: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; ISO:MGI.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IGI:MGI.
DR GO; GO:0031642; P:negative regulation of myelination; IMP:UniProtKB.
DR GO; GO:2000403; P:positive regulation of lymphocyte migration; IMP:ARUK-UCL.
DR GO; GO:0007286; P:spermatid development; IDA: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 SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:10779521"
FT CHAIN 29..298
FT /note="Junctional adhesion molecule B"
FT /id="PRO_0000015070"
FT TOPO_DOM 29..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..128
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 135..238
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 156..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 133
FT /note="V -> M (in Ref. 3; BAC26102)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="T -> H (in Ref. 3; BAC37139)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="G -> R (in Ref. 3; BAC37139)"
FT /evidence="ECO:0000305"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:5GMJ"
SQ SEQUENCE 298 AA; 33047 MW; 1124E0F07E6CF751 CRC64;
MARSPQGLLM LLLLHYLIVA LDYHKANGFS ASKDHRQEVT VIEFQEAILA CKTPKKTTSS
RLEWKKVGQG VSLVYYQQAL QGDFKDRAEM IDFNIRIKNV TRSDAGEYRC EVSAPTEQGQ
NLQEDKVMLE VLVAPAVPAC EVPTSVMTGS VVELRCQDKE GNPAPEYIWF KDGTSLLGNP
KGGTHNNSSY TMNTKSGILQ FNMISKMDSG EYYCEARNSV GHRRCPGKRM QVDVLNISGI
IATVVVVAFV ISVCGLGTCY AQRKGYFSKE TSFQKGSPAS KVTTMSENDF KHTKSFII
