JAM2A_DANRE
ID JAM2A_DANRE Reviewed; 307 AA.
AC A0A0R4IGV4;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Junctional adhesion molecule 2A {ECO:0000303|PubMed:22180726};
DE Short=Jam2a {ECO:0000303|PubMed:22180726};
DE AltName: Full=Junctional adhesion molecule B {ECO:0000303|PubMed:22180726};
DE Short=JAM-B {ECO:0000303|PubMed:22180726};
DE Flags: Precursor;
GN Name=jam2a; Synonyms=jamb {ECO:0000303|PubMed:22180726};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22180726; DOI=10.1371/journal.pbio.1001216;
RA Powell G.T., Wright G.J.;
RT "Jamb and jamc are essential for vertebrate myocyte fusion.";
RL PLoS Biol. 9:E1001216-E1001216(2011).
CC -!- FUNCTION: Junctional adhesion protein that mediates heterotypic cell-
CC cell interactions to regulate different cellular processes (By
CC similarity). During myogenesis, it is involved in myocyte fusion
CC through the binding of jam3b on neighboring myocytes (PubMed:22180726).
CC {ECO:0000250|UniProtKB:P57087, ECO:0000269|PubMed:22180726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P57087};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P57087}.
CC Cell junction {ECO:0000250|UniProtKB:P57087}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:Q9JI59}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the somites of the embryo in a wave
CC along the anterior-posterior axis. {ECO:0000269|PubMed:22180726}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown impairs myocyte fusion
CC during myogenesis. {ECO:0000269|PubMed:22180726}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {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; CU571081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0R4IGV4; -.
DR SMR; A0A0R4IGV4; -.
DR Ensembl; ENSDART00000166731; ENSDARP00000132646; ENSDARG00000058996.
DR ZFIN; ZDB-GENE-031204-3; jam2a.
DR GeneTree; ENSGT00940000165208; -.
DR Reactome; R-DRE-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-DRE-216083; Integrin cell surface interactions.
DR PRO; PR:A0A0R4IGV4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000058996; Expressed in mature ovarian follicle and 48 other tissues.
DR ExpressionAtlas; A0A0R4IGV4; baseline and differential.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; ISS:UniProtKB.
DR GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ZFIN.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0048534; P:hematopoietic or lymphoid organ development; IMP:ZFIN.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007520; P:myoblast fusion; IMP:ZFIN.
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; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Tight junction;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..307
FT /note="Junctional adhesion molecule 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_5015344232"
FT TOPO_DOM 19..226
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 19..112
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 126..225
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 278..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 40..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 147..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 307 AA; 34651 MW; 03F8F78E553A91CC CRC64;
MLVCVSLLIL IHSVPVSPVT VSSRNPKVEV HEFSDAELSC EFKTEKDTNP RIEWKRKDKE
KDVSFVYYGE RFVGPFQDRA DIEGATVRLR RVTQADAGEY RCEVSAPSDS ISLGETNVTL
RVLVPPQTPS CDVPSSALTG SQVELRCRDR HSIPPAVYTW YKDNRALPIR HPNATYTVNE
FTGVLIPQSH YNPGTVCQHC MYHPNYHIPN TQLTTTFQTH DLNVAAVVSA VVLVCVILFL
CAFGVCLAHR QGYFSRHRGR SFWIPHCHGV THISSQNLNP SEHTQHSGYS HPPKEPQDFK
HTQSFML
