JAM3B_DANRE
ID JAM3B_DANRE Reviewed; 302 AA.
AC A3KPA0;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Junctional adhesion molecule 3B {ECO:0000303|PubMed:22180726};
DE Short=Jam3b {ECO:0000303|PubMed:22180726};
DE AltName: Full=Junctional adhesion molecule C;
DE Short=JAM-C;
DE Flags: Precursor;
GN Name=jam3b; Synonyms=jamc {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 MRNA].
RX PubMed=18296487; DOI=10.1101/gr.7187808;
RA Bushell K.M., Soellner C., Schuster-Boeckler B., Bateman A., Wright G.J.;
RT "Large-scale screening for novel low-affinity extracellular protein
RT interactions.";
RL Genome Res. 18:622-630(2008).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 jam2a on neighboring myocytes (PubMed:22180726).
CC {ECO:0000250|UniProtKB:P57087, ECO:0000269|PubMed:22180726}.
CC -!- INTERACTION:
CC A3KPA0; A4JYM3: jam2a; NbExp=5; IntAct=EBI-1579361, EBI-1579304;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BX67};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX67}.
CC Cell junction {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, desmosome
CC {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9BX67}.
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}.
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DR EMBL; CU458938; CAM73199.1; -; mRNA.
DR EMBL; BX470244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR383673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC134233; AAI34234.1; -; mRNA.
DR RefSeq; NP_001076332.2; NM_001082863.3.
DR AlphaFoldDB; A3KPA0; -.
DR SMR; A3KPA0; -.
DR DIP; DIP-40322N; -.
DR IntAct; A3KPA0; 1.
DR STRING; 7955.ENSDARP00000082979; -.
DR GeneID; 569217; -.
DR KEGG; dre:569217; -.
DR CTD; 569217; -.
DR ZFIN; ZDB-GENE-030131-441; jam3b.
DR OrthoDB; 906664at2759; -.
DR PhylomeDB; A3KPA0; -.
DR Reactome; R-DRE-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-DRE-216083; Integrin cell surface interactions.
DR PRO; PR:A3KPA0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P: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; 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 SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..302
FT /note="Junctional adhesion molecule 3B"
FT /evidence="ECO:0000255"
FT /id="PRO_5015086358"
FT TOPO_DOM 24..235
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 27..124
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 131..228
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 45..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 302 AA; 33937 MW; 62DCDA86C2BAFD85 CRC64;
MALTPLACVL LLLSMQCYIS TLAVLLKSTN SKPWVNEFES IELSCMIESI TTTKPRIEWK
KIKNGDPSYV YFDNQISGDL ERRAKIREPA TLVILNATRS DSADYRCEVT APNDQKSFDE
ILISLTVRVK PVVPRCSVPK SIPVGKPAEL HCLEDEGYPK SQYQWFRNKE EIPLDPKSSP
KFFNSTYTLD GEMGTLKFSA VRKEDAGEYY CRAKNEAGIS ECGPQMMEVY DINIAGIILG
VVVVVMVLLC ITVGIFCAYK RGYFTSQKQT GNNYKPPAKG DGVDYVRTED EGDFRHKSSF
VI
