DUSTY_XENLA
ID DUSTY_XENLA Reviewed; 916 AA.
AC Q67E01; Q4QR51;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY364232; AAR13047.1; -; mRNA.
DR EMBL; AY429678; AAS55394.1; -; mRNA.
DR EMBL; BC097571; AAH97571.1; -; mRNA.
DR RefSeq; NP_001087088.1; NM_001093619.1.
DR AlphaFoldDB; Q67E01; -.
DR SMR; Q67E01; -.
DR GeneID; 446954; -.
DR KEGG; xla:446954; -.
DR CTD; 446954; -.
DR Xenbase; XB-GENE-971404; dstyk.S.
DR OrthoDB; 254886at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 446954; Expressed in egg cell and 19 other tissues.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; Cytoplasm;
KW Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..916
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233125"
FT DOMAIN 641..895
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 766
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 647..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 605
FT /note="E -> K (in Ref. 2; AAH97571)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="S -> T (in Ref. 2; AAH97571)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="V -> L (in Ref. 2; AAH97571)"
FT /evidence="ECO:0000305"
FT CONFLICT 907..916
FT /note="ETGKALEDST -> KKRKKKKKKKKKK (in Ref. 2; AAH97571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 916 AA; 104164 MW; 5B622AF8C5D57A40 CRC64;
MQRDGTRSAR RMDEGDRRTG SAGRSGSREL GRGFSYYNKY LARLQQNLRD TKRFFRDIKL
TYSGAPGGPD TEFSGAEGEF GQLHSITFPR QEEEYLKLTV RCRPCIFILG QNCSGRGRVA
NGLLGGQLLP ILTHGDIECC KRRRIRFRHG KQTLVSLALP EQYELVHQLV AHQGKWDTIP
EEDLDVPEDE EDPAHRLAEL EVTLPHQLLQ DVDIVVSPCR SSQAVSMTLE DYVDHVQSIV
VYAVSEEMLS KQDEEELTEI KEKYKLPVFF IRTSSTKDRL IGGSEGVRSV LYEQLIELGY
LQRGLCNCGA AGSGSTAPSM LVEQFEKIRQ LSTFSRQVLQ MHLVDAAIVL NMVHSRCLDL
FINKAFDMHR DLQITPKRLE YTRQKENELY ESLMRISDRK QEELKDMIVE TLNSMREQLL
EDAANMQFKD IVIPQNGEPV SAHEVKCCIF QIKELIISRL NQAVVNKLIS SVDYLRESFV
GTMERCLRSL EKSQQESSSH VTSNHLKQIL NAAYHVEVTF NSGSTVTRMV WEQIVQIIQR
ITWVSPPTIT PEWKRRVAQD AIETLSASKL AKSICSQFCK RLKSSHEAFA ASLKQLEVGH
SGRLEKTNDL WLRVRKDHAP RLARLSLESR SLQDVLLHGK PRIGRELGRG QYGVVYLCDS
WGGHFPCALK SVVPPDEKHW NDLALEFHYM RSLPKHERLV DLHGSVIDYS YGGGSSIAVL
LITERLHRDL YVGLKTGLSL ETRLQIALDV VEGIRFLHNQ GVVHRDIKLK NVLLDKKHRA
KITDLGFCKP EAMMSGSIVG TPIHMAPELF SGKYDNSVDV YAFGILFWYI CSGSVKLPEA
FEKCASKDHL WNNVRKGARP ERLTIFDEEC WKLMEACWNG DPSQRPLMGI VQPMLQGIMD
RLCHTQETGK ALEDST
