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Database: UniProt
Entry: Q8JFB0_DANRE
LinkDB: Q8JFB0_DANRE
Original site: Q8JFB0_DANRE 
ID   Q8JFB0_DANRE            Unreviewed;       499 AA.
AC   Q8JFB0;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   31-JUL-2019, entry version 148.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   Name=acvrl1 {ECO:0000313|EMBL:AAM53074.1,
GN   ECO:0000313|Ensembl:ENSDARP00000043461,
GN   ECO:0000313|ZFIN:ZDB-GENE-021003-1};
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:AAM53074.1};
RN   [1] {ECO:0000313|EMBL:AAM53074.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12050147;
RA   Roman B.L., Pham V.N., Lawson N.D., Kulik M., Childs S., Lekven A.C.,
RA   Garrity D.M., Moon R.T., Fishman M.C., Lechleider R.J.,
RA   Weinstein B.M.;
RT   "Disruption of acvrl1 increases endothelial cell number in zebrafish
RT   cranial vessels.";
RL   Development 129:3009-3019(2002).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000043461}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000043461};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000043461, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000043461,
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).
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|SAAS:SAAS01128404};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; CR387931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF435024; AAM53074.1; -; mRNA.
DR   EMBL; AF435025; AAM53075.1; -; mRNA.
DR   RefSeq; NP_705929.1; NM_153643.1.
DR   RefSeq; XP_009295081.1; XM_009296806.2.
DR   Ensembl; ENSDART00000043462; ENSDARP00000043461; ENSDARG00000018179.
DR   GeneID; 266753; -.
DR   KEGG; dre:266753; -.
DR   CTD; 94; -.
DR   ZFIN; ZDB-GENE-021003-1; acvrl1.
DR   eggNOG; KOG2052; Eukaryota.
DR   eggNOG; ENOG410XQT0; LUCA.
DR   GeneTree; ENSGT00940000166145; -.
DR   OrthoDB; 776697at2759; -.
DR   TreeFam; TF314724; -.
DR   Proteomes; UP000000437; Chromosome 23.
DR   Bgee; ENSDARG00000018179; Expressed in 29 organ(s), highest expression level in pharyngeal gill.
DR   ExpressionAtlas; Q8JFB0; baseline.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
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:0048185; F:activin binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0098821; F:BMP receptor activity; IBA:GO_Central.
DR   GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
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:0032924; P:activin receptor signaling pathway; IEA:GOC.
DR   GO; GO:0060840; P:artery development; IMP:ZFIN.
DR   GO; GO:0048844; P:artery morphogenesis; IMP:ZFIN.
DR   GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:ZFIN.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IMP:ZFIN.
DR   GO; GO:0048264; P:determination of ventral identity; IDA:ZFIN.
DR   GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR   GO; GO:0034405; P:response to fluid shear stress; IMP:ZFIN.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0001944; P:vasculature development; IMP:ZFIN.
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; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
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:RU000304,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139, ECO:0000313|EMBL:AAM53074.1};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:AAM53074.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00138186}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00138220,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00488859,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    499       Receptor protein serine/threonine kinase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5015099172.
FT   TRANSMEM    114    139       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      164    193       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      194    491       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   499 AA;  56448 MW;  CDE0A8B2632F5A58 CRC64;
     MKASVMLAVL FVLVYSGSYA TTADHLMETS TLKNDESSLQ CSCENTNLCE NNSCWGRICF
     YTSVHERVVR GCFQTAEQCY VPAIPGVYTK CCYTHHCNAN LTMPEKPVEK PIRVILLVGV
     PLLVLLVIAM AACGLVLWLR TRRQYCHPVE HDTSMLKVPS GGDPTYGDIF DEFCTSGSGT
     GLPYLVQRTM ARQISLVECV GKGRYGEVWR GTWMGESVAV KIFSSRDEQS WFRETEIYNT
     VQLRHENILG FIASDMTSKN SSTQLWLVTH FHELGSLYDF LQYSTLDPEG CLRMCLSIAS
     GLVHLHTEIL STQGKPAIAH RDLKSRNILV KRNGQCCIAD LGLAVIHSQS TDYLDVGTNP
     RVGTKRYMAP EVLDETIRVD VFESYKQTDI WALGLVLWEI TRRTIVNGIV EEYRPPFFDM
     VPSDPSFEEM KKVVCVDQHR PSLHNRLHSH PILSAIAKIM KECWFQSPSA RLTALRVRKS
     LSKLDQDHDY DIDKLKLDL
//
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