DUSTY_PIMPR
ID DUSTY_PIMPR Reviewed; 903 AA.
AC A2CI34;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Dual serine/threonine and tyrosine protein kinase {ECO:0000303|PubMed:17123648};
DE EC=2.7.12.1 {ECO:0000250|UniProtKB:P16879};
DE AltName: Full=Dusty protein kinase {ECO:0000303|PubMed:17123648, ECO:0000312|EMBL:ABD77593.1};
DE Short=Dusty PK {ECO:0000303|PubMed:17123648};
DE AltName: Full=Receptor-interacting serine/threonine-protein kinase 5 {ECO:0000250|UniProtKB:Q6XUX3};
GN Name=dstyk {ECO:0000250|UniProtKB:Q6XUX3};
GN Synonyms=ripk5 {ECO:0000250|UniProtKB:Q6XUX3};
OS Pimephales promelas (Fathead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Leuciscidae; Pogonichthyinae; Pimephales.
OX NCBI_TaxID=90988;
RN [1] {ECO:0000312|EMBL:ABD77593.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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 May play a role in the embryonic development.
CC {ECO:0000250|UniProtKB:Q4VSN1, 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 Evidence={ECO:0000250|UniProtKB:P16879};
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; Evidence={ECO:0000250|UniProtKB:P16879};
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 Evidence={ECO:0000250|UniProtKB:P16879};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ419945; ABD77593.1; -; mRNA.
DR AlphaFoldDB; A2CI34; -.
DR SMR; A2CI34; -.
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:0048568; P:embryonic organ development; ISS:UniProtKB.
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;
KW Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..903
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000374057"
FT DOMAIN 627..881
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 382..414
FT /evidence="ECO:0000255"
FT ACT_SITE 752
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 633..641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 903 AA; 101593 MW; 82D50FDA42F415C6 CRC64;
MENPQKAGPL LRDLTRAFSH YNKHNLLLKK NLKETIAFFR EIRQNHSNTC STSGPELDSG
QLRCISFPRH DEDHLQKVVG CAPYILILGQ DCSARYQLLN CMLGERLLPL GSDAGGACGV
EGGACRRRKL CFTHGRQTRL SLALPGQYEL VHQLAAHCGR WDTVPREDLE IQECEDPAQR
LAELEITLHH ALLQEAKIMV LPCRNVQPVE EALEDCRRGI LPIILYAVSK ATLSADQLSE
LQKVRETLPY PVCFVRIPTE PAPDPPGQRS ALFAQLVSQE LIGGAAGNCA CGAPAQTPGK
MQGILGEDLE RLHRVLVPFA RQVLQSQQVE ATTLLNAVHC RCLDLFINQA FDMQRDLQIT
PRRLEYTREK EGELYSSLMA IANRKQEEMK EMIVETLESM KEQLLEDAAN LEFTDIIMTS
NSEPMSSKDI KVCISQIQDL IVIRLNQAVA NKLTSSVDYL RESFVGTLER CLCSLEKSTG
EPCAHNVTSN HLKQILNAAY HVEVTFHSGS SVTRLFWEQI KQIIHRISWV NPPSVTSEWK
RKVAQDAIES LSAAKLAKSI CSQFRTRLNS SHEAFASSLR QLEEGHTGRL ERTEDLWLRV
RKDHAPRLAR LSLESRSLRD ILLHGKPKLG RELGRGQYGV VYLCDNWAGR HPCALKSVVP
PDDKHWNDLA LEFHYTRSLP KHERLVNLHG SVIDHSYGGG SSIAVLLIME RLHRDLYTGL
KAGLVLKERL QIALDVVEGI RFLHGQGLLH RDIKLKNVLL DKQNRAKITD LGFCKPEAMM
SGSIVGTPIH MAPELFTGKY DNSVDVYAFG ILFWYLCTGS VKLPEAFERC SSKDQLWTNV
KKGSRPERLA SFDEECWQLM EACWNGDPSQ RPLLGIVQPS LQSIMDRLCN DSDQKSGNLE
DSN
