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Database: UniProt
Entry: Q9W629_DANRE
LinkDB: Q9W629_DANRE
Original site: Q9W629_DANRE 
ID   Q9W629_DANRE            Unreviewed;       530 AA.
AC   Q9W629;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   08-MAY-2019, entry version 163.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   Name=bmpr1ba {ECO:0000313|Ensembl:ENSDARP00000140548,
GN   ECO:0000313|ZFIN:ZDB-GENE-991208-8};
GN   Synonyms=bmpr-IB {ECO:0000313|EMBL:BAA76408.1}, bmpr1b
GN   {ECO:0000313|EMBL:AAH81625.1, ECO:0000313|ZFIN:ZDB-GENE-991208-8};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:BAA76408.1};
RN   [1] {ECO:0000313|EMBL:BAA76408.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|EMBL:BAA76408.1};
RA   Nikaido M., Tada M., Ueno N.;
RT   "Restricted expression of the receptor serine/threonine kinase, BMPR-
RT   IB, in zebrafish.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAH81625.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:AAH81625.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000140548, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000140548,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   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.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|Ensembl:ENSDARP00000140548}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000140548};
RG   Ensembl;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
CC         phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
CC         COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|SAAS:SAAS01128400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-threonine + ATP = [receptor-
CC         protein]-O-phospho-L-threonine + ADP + H(+);
CC         Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-
CC         COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30; Evidence={ECO:0000256|RuleBase:RU361271,
CC         ECO:0000256|SAAS:SAAS01128404};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU361271};
CC       Single-pass type I membrane protein
CC       {ECO:0000256|RuleBase:RU361271}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00595019}.
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DR   EMBL; CABZ01039094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01039095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01039096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01039097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01039098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01061830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01069883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01069884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU856184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; LO017812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC081625; AAH81625.1; -; mRNA.
DR   EMBL; AB020758; BAA76408.1; -; mRNA.
DR   RefSeq; NP_571532.1; NM_131457.2.
DR   STRING; 7955.ENSDARP00000016669; -.
DR   Ensembl; ENSDART00000168820; ENSDARP00000140548; ENSDARG00000104100.
DR   GeneID; 30742; -.
DR   KEGG; dre:30742; -.
DR   CTD; 30742; -.
DR   ZFIN; ZDB-GENE-991208-8; bmpr1ba.
DR   eggNOG; KOG2052; Eukaryota.
DR   eggNOG; ENOG410XQT0; LUCA.
DR   GeneTree; ENSGT00940000155919; -.
DR   HOGENOM; HOG000230587; -.
DR   KO; K13578; -.
DR   OrthoDB; 776697at2759; -.
DR   Reactome; R-DRE-201451; Signaling by BMP.
DR   Proteomes; UP000000437; Chromosome 5.
DR   Bgee; ENSDARG00000104100; Expressed in 40 organ(s), highest expression level in somite.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR   GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central.
DR   GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IGI:ZFIN.
DR   GO; GO:0048263; P:determination of dorsal identity; IMP:ZFIN.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:ZFIN.
DR   GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR003605; GS_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Kinase {ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138139};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138203};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:BAA76408.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138186}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138220};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00488859}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    530       Serine/threonine-protein kinase receptor.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5015100983.
FT   TRANSMEM    154    176       Helical. {ECO:0000256|RuleBase:RU361271}.
FT   DOMAIN      202    231       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      232    522       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   530 AA;  60190 MW;  8FB5410C0BE1E277 CRC64;
     MDLYRSCLRW LCVLLIGLLG LVEENLANVL DSMLLRNSGK VEERRETGSD APALPQRFLW
     CYCYHHCPED STNNTCRTDG YCFTMVEEEG GAAVVTSGCL GLVGSEFQCR DTGNSKQRRA
     LECCTDQDYC NRDLHPTLPP LRTPSYVVGD IHHIALLISV SVCSFILTFI IIFCYFRYKR
     HELAPRYSLG LHPDESFIPA GESLRDLIEQ SQSSGSGSGL PLLVQRTIAK QIQMVTQIGK
     GRYGEVWMGR WRGEKVAVKV FFTTEEASWF RETEIYQTVL MRHDNILGFI AADIKGTGSW
     TQLYLITDYH ENGSLYDYLK CTTLDSRAML KLAYSSVSGL CHLHTEIFGT QGKPAIAHRD
     LKSKNILVKR NGACCIADLG LAVKFISDTN EVDIPLNTRV GTKRFMAPEV LDETLNRNHF
     QSYIMADMYS FGLILWEISR RCVTGGIVEE YQLPYHDHVP NDPSYEDMRE VVCIKRIRPS
     FPNRWSSDEC LRQMGKLMTE CWAHNPASRL TALRVKKTLA KMSESQDIKV
//
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