DUSTY_CHICK
ID DUSTY_CHICK Reviewed; 930 AA.
AC Q6XUX0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Dual serine/threonine and tyrosine protein kinase;
DE EC=2.7.12.1;
DE AltName: Full=Dusty protein kinase;
DE Short=Dusty PK;
DE AltName: Full=Receptor-interacting serine/threonine-protein kinase 5;
GN Name=DSTYK; Synonyms=RIPK5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=17123648; DOI=10.1016/j.bbaexp.2006.10.004;
RA Peng J., Dong W., Chen Y., Mo R., Cheng J.-F., Hui C.-C., Mohandas N.,
RA Huang C.-H.;
RT "Dusty protein kinases: primary structure, gene evolution, tissue specific
RT expression and unique features of the catalytic domain.";
RL Biochim. Biophys. Acta 1759:562-572(2006).
CC -!- FUNCTION: May act as a positive regulator of ERK phosphorylation
CC downstream of fibroblast growth factor-receptor activation. May induce
CC both caspase-dependent apoptosis and caspase-independent cell death.
CC {ECO:0000250|UniProtKB:Q6XUX3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XUX1}. Cell
CC membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q6XUX1}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q6XUX1}. Cell junction
CC {ECO:0000250|UniProtKB:Q6XUX1}.
CC -!- TISSUE SPECIFICITY: Widely expressed with the highest expression in
CC brain and ovary. {ECO:0000269|PubMed:17123648}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY208853; AAP42421.1; -; mRNA.
DR EMBL; AY429677; AAS55393.1; -; mRNA.
DR RefSeq; NP_989837.1; NM_204506.2.
DR AlphaFoldDB; Q6XUX0; -.
DR SMR; Q6XUX0; -.
DR STRING; 9031.ENSGALP00000034586; -.
DR PaxDb; Q6XUX0; -.
DR GeneID; 395171; -.
DR KEGG; gga:395171; -.
DR CTD; 25778; -.
DR VEuPathDB; HostDB:geneid_395171; -.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; Q6XUX0; -.
DR OrthoDB; 254886at2759; -.
DR PhylomeDB; Q6XUX0; -.
DR PRO; PR:Q6XUX0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell junction; Cell membrane; Coiled coil; Cytoplasm; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..930
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233122"
FT DOMAIN 653..907
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 383..428
FT /evidence="ECO:0000255"
FT ACT_SITE 778
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 659..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 930 AA; 105410 MW; 6FCF8B8073AFFB74 CRC64;
MEGEGAPSWR GGPGGLIREL CRSFGHYNRH LARLQHNLRE TKKFFRDVKY SQGNLFASGA
AIGEGSPSGA GGGGTRDGGQ NFISFPRHEE EHLQQTVSWH PCLLILGQNC NAKCQLLNIL
LGEKLLPTTK ISSEENCKRR RIRFTHGTQT RVSLALPEQY ELVHMMAAHR GHWDTIPEED
LEIRGDSEDP AHRIAELEVV LPYSLLKEVD VVVAPCRGFQ SAEATLEEYM NQVLLIVIFA
ISEAELSSSD ENELREIKEK FSLPIFFFKV PESGVELISP KKTDNEKSSL YCQLMDLEYL
STNHCSCGAP SPDAVAQSML VEQLEKLRLL STFSRQVLQK HLVEAATSLN EVHCRCLNIF
INQAFDMQRD LQITPKRLEY TRRKENELYE SLMNIANRKQ EEMKDMIIET LSNMKEELLE
DAANMEFKDI IIPENGEPVS SKDIKCCIKQ IQELIISRLN QAVANKLISS VDYLRESFVG
TLERCLKSLE ESWEVSVHPA RSLEKSKDVS VHITSNYLKQ ILNAAYHVEV TFHSGSTVTR
MLWEQIKQII QRITWVSPPA ITSDWKRKVA QDAIESLSAS KLAKSICSQF RTRLNSSHEA
FAASLRQLED GHSGRLEKTE DLWLKVRKDH APRLARLSLE SRSLQDVLLH GKPKLGRELG
RGQYGVVYLC DSWGGHFPCA LKSVVPPDEK HWNDLALEFH YMRSLQSHER LVDLHGSVID
YGYGGGSSIA VLLIMERLHR DLYTGLKAGL ELETRLQIAL DVVEGIRYLH SQGLVHRDIK
LKNVLLDKKN RAKITDLGFC KPEAMMSGSI VGTPIHMAPE LFTGKYDNSV DVYAFGILFW
YICSGHVKLP EAFERCASKD HLWNNVRRGV RPERLPVFDE ECWQLMEACW DGDSSQRPLL
GIVQPMLQGI MDRLCKSSSE HPNKGLDDST
