Entry euk:Q5M7Y2_DANRE

ID   Q5M7Y2_DANRE            Unreviewed;       604 AA.
AC   Q5M7Y2;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   10-MAY-2017, entry version 117.
DE   SubName: Full=A-Raf proto-oncogene, serine/threonine kinase {ECO:0000313|Ensembl:ENSDARP00000118701};
DE   SubName: Full=Zgc:92074 protein {ECO:0000313|EMBL:AAH88382.1};
GN   Name=araf {ECO:0000313|Ensembl:ENSDARP00000118701,
GN   ECO:0000313|ZFIN:ZDB-GENE-050102-2};
GN   Synonyms=zgc:92074 {ECO:0000313|EMBL:AAH88382.1};
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:AAH88382.1};
RN   [1] {ECO:0000313|EMBL:AAH88382.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:AAH88382.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000118701}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118701};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000118701, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118701,
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: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|SAAS:SAAS00786134}.
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DR   EMBL; CU041374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC088382; AAH88382.1; -; mRNA.
DR   RefSeq; XP_005171875.1; XM_005171818.3.
DR   UniGene; Dr.77625; -.
DR   STRING; 7955.ENSDARP00000118602; -.
DR   Ensembl; ENSDART00000140081; ENSDARP00000118701; ENSDARG00000054533.
DR   GeneID; 403063; -.
DR   CTD; 369; -.
DR   ZFIN; ZDB-GENE-050102-2; araf.
DR   eggNOG; KOG0193; Eukaryota.
DR   eggNOG; ENOG410Y4UP; LUCA.
DR   GeneTree; ENSGT00760000118807; -.
DR   HOVERGEN; HBG001886; -.
DR   Reactome; R-DRE-5673000; RAF activation.
DR   Reactome; R-DRE-5675221; Negative regulation of MAPK pathway.
DR   Proteomes; UP000000437; Chromosome 5.
DR   Bgee; ENSDARG00000054533; -.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005057; F:signal transducer activity, downstream of receptor; IEA:InterPro.
DR   GO; GO:0046332; F:SMAD binding; IDA:ZFIN.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:1900108; P:negative regulation of nodal signaling pathway; IDA:ZFIN.
DR   GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:ZFIN.
DR   CDD; cd00029; C1; 1.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR003116; RBD_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF02196; RBD; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00455; RBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00783584};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Kinase {ECO:0000256|SAAS:SAAS00784476};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00515414};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00783584};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q5M7Y2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00784476};
KW   Transferase {ECO:0000256|SAAS:SAAS00784476};
KW   Zinc {ECO:0000256|SAAS:SAAS00515409}.
FT   DOMAIN       23     95       RBD (Ras-binding).
FT                                {ECO:0000259|PROSITE:PS50898}.
FT   DOMAIN      102    148       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      308    572       Protein kinase.
FT                                {ECO:0000259|PROSITE:PS50011}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       103    149       ipfam:C1_1 [T]
FT   MYHIT        23     95       iprf:RBD [T]
FT   MYHIT       314    334       ipat:PROTEIN_KINASE_ATP [T]
FT   MYHIT       103    148       ipat:ZF_DAG_PE_1 [T]
FT   MYHIT       308    572       ismart:S_TKc [T]
FT   MYHIT        23     95       ismart:RBD [T]
FT   MYHIT       103    148       ismart:C1 [T]
FT   MYHIT       102    148       iprf:ZF_DAG_PE_2 [T]
FT   MYHIT       423    435       ipat:PROTEIN_KINASE_ST [T]
FT   MYHIT       309    562       ipfam:Pkinase_Tyr [T]
FT   MYHIT        24     93       ipfam:RBD [T]
FT   MYHIT       308    572       iprf:PROTEIN_KINASE_DOM [T]
SQ   SEQUENCE   604 AA;  68240 MW;  D38FFC7A2B39BD20 CRC64;
     MSNTSSCSSS GETSPDDTPR GGGTIRVYLP NKQRTVVNVR PGQTVYDSLD KALKVRGLSQ
     DCCAVFRLLE GRKRLTEWDT DITPLVGEEL LVEVLDDVPL TMHNFVRKTF FKLAYCDFCH
     KFLFNGFRCQ TCGYKFHQHC SSKVPTVCVD MDTMTKRCVN NTEDCPAILI YPATNSISQS
     DLPLTSDSPG GELPSSPSNF CLFIRGEDGQ SLQRHRSTST PNVHMVSTLE PGAAGLLEEP
     FKISTVGYES SPKPSTSPPH LGSPGRKPPK SPSEPKERKQ SSSDDKKKVH RGGYRDSSYY
     WEVHPREVSM LKRIGAGSFG TVFKGKWHGD VAIKILKVTE PTPEQLQAFK NEMQVLRKTR
     HVNILLFMGF MTRPNFAIIT QWCEGSSLYR HLHVTETKFD TMRRIDVARQ TAQGMDYLHA
     KNIIHRDLKS NNIFLHEGWT VKIGDFGLAT VKSRWSGSQQ VEQPSGSILW MAPEVIRMQD
     TNPYTFQSDV YGYGVVLYEL MSGTLPYSNI NNRDQIIFMV GRGYLSPDLS KLYSNCPKSM
     KRLIIDCLKF KRDERPLFPQ ILVSIEQVQE LLPKIERSAS EPSLHRAVHA EDLNPLLLHT
     TRFL
//