ID B0V233_DANRE Unreviewed; 306 AA.
AC B0V233; A0A8M1NH75;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Junctional adhesion molecule 2 precursor {ECO:0000313|RefSeq:NP_001121766.1};
DE SubName: Full=Junctional adhesion molecule 2b {ECO:0000313|Ensembl:ENSDARP00000102441};
GN Name=jam2b {ECO:0000313|Ensembl:ENSDARP00000102441,
GN ECO:0000313|RefSeq:NP_001121766.1,
GN ECO:0000313|ZFIN:ZDB-GENE-080229-3};
GN Synonyms=im:7155552 {ECO:0000313|RefSeq:NP_001121766.1}, sc:d0813
GN {ECO:0000313|RefSeq:NP_001121766.1}, si:ch211-160b11.5
GN {ECO:0000313|RefSeq:NP_001121766.1};
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 {ECO:0000313|Ensembl:ENSDARP00000102441};
RN [1] {ECO:0000313|RefSeq:NP_001121766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121766.1};
RX PubMed=22609279;
RA Niu X., Gao C., Jan Lo L., Luo Y., Meng C., Hong J., Hong W., Peng J.;
RT "Sec13 safeguards the integrity of the endoplasmic reticulum and
RT organogenesis of the digestive system in zebrafish.";
RL Dev. Biol. 367:197-207(2012).
RN [2] {ECO:0000313|RefSeq:NP_001121766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121766.1};
RX PubMed=22815827;
RA Powell G.T., Wright G.J.;
RT "Genomic organisation, embryonic expression and biochemical interactions of
RT the zebrafish junctional adhesion molecule family of receptors.";
RL PLoS ONE 7:e40810-e40810(2012).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000102441, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000102441};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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 [4] {ECO:0000313|Ensembl:ENSDARP00000102441}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000102441};
RG Ensembl;
RL Submitted (AUG-2013) to UniProtKB.
RN [5] {ECO:0000313|RefSeq:NP_001121766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121766.1};
RX PubMed=25119047;
RA Kobayashi I., Kobayashi-Sun J., Kim A.D., Pouget C., Fujita N., Suda T.,
RA Traver D.;
RT "Jam1a-Jam2a interactions regulate haematopoietic stem cell fate through
RT Notch signalling.";
RL Nature 512:319-323(2014).
RN [6] {ECO:0000313|RefSeq:NP_001121766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121766.1};
RX PubMed=26370768;
RA Matsui H., Dorigo A., Buchberger A., Hocking J.C., Distel M., Koster R.W.;
RT "Zebrafish jam-b2 Gal4-enhancer trap line recapitulates endogenous jam-b2
RT expression in extraocular muscles.";
RL Dev. Dyn. 244:1574-1580(2015).
RN [7] {ECO:0000313|RefSeq:NP_001121766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121766.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [8] {ECO:0000313|RefSeq:NP_001121766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121766.1};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [9] {ECO:0000313|RefSeq:NP_001121766.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121766.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; CR936415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001121766.1; NM_001128294.1.
DR STRING; 7955.ENSDARP00000102441; -.
DR PaxDb; 7955-ENSDARP00000102441; -.
DR Ensembl; ENSDART00000111437; ENSDARP00000102441; ENSDARG00000079071.
DR Ensembl; ENSDART00000111437.5; ENSDARP00000102441.3; ENSDARG00000079071.5.
DR GeneID; 100005301; -.
DR KEGG; dre:100005301; -.
DR AGR; ZFIN:ZDB-GENE-080229-3; -.
DR CTD; 100005301; -.
DR ZFIN; ZDB-GENE-080229-3; jam2b.
DR eggNOG; ENOG502QY6U; Eukaryota.
DR OMA; HNPRIEW; -.
DR OrthoDB; 3027035at2759; -.
DR PhylomeDB; B0V233; -.
DR TreeFam; TF331459; -.
DR Proteomes; UP000000437; Alternate scaffold 9.
DR Proteomes; UP000000437; Chromosome 9.
DR Bgee; ENSDARG00000079071; Expressed in pectoral fin and 23 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IBA:GO_Central.
DR GO; GO:0070160; C:tight junction; IBA:GO_Central.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IBA:GO_Central.
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; IPR042625; JAM2.
DR PANTHER; PTHR44663:SF1; JUNCTIONAL ADHESION MOLECULE 2 PRECURSOR; 1.
DR PANTHER; PTHR44663; JUNCTIONAL ADHESION MOLECULE B; 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.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001121766.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..306
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001121766.1"
FT /id="PRO_5035034957"
FT TRANSMEM 241..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..131
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 138..233
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 306 AA; 34194 MW; 75027DD36EAEBF0C CRC64;
MLLQQPYITK MKTKQLLTSA LLLLIYIPSS DPVTVTTSKA KMDVHENTNA VLSCEFRTEK
ETNPRVEWKK RGKDVSYVYF EGDFTGSYKG RASIDGATLT LRGVTQKDSG VYHCEVTARQ
DKIKLGEVSV TLSVLVPPHA PTCEVPEAVM RGFSAELHCK DKLSVPAATY SWYKDNKPLN
TANPHDVHYT LDTKTGSLKF KSVSKSDEGQ YRCEASNGVG APKSCAGHHM KITEFELNMT
MIIAIEVGAF LLLVSCCVSI CLCCRRGCCH CCRRQSKEEI KQSKTKTSYN QPTDPRRYKH
TQSFVL
//
