DUSTY_XENTR
ID DUSTY_XENTR Reviewed; 918 AA.
AC Q67E00;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
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).
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}.
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; AY364233; AAR13048.1; -; mRNA.
DR EMBL; AY429679; AAS55395.1; -; mRNA.
DR RefSeq; NP_001007477.1; NM_001007476.1.
DR AlphaFoldDB; Q67E00; -.
DR SMR; Q67E00; -.
DR STRING; 8364.ENSXETP00000031184; -.
DR PaxDb; Q67E00; -.
DR PRIDE; Q67E00; -.
DR GeneID; 493205; -.
DR KEGG; xtr:493205; -.
DR CTD; 25778; -.
DR Xenbase; XB-GENE-971397; dstyk.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; Q67E00; -.
DR OrthoDB; 254886at2759; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; 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:0048568; P:embryonic organ development; ISS:UniProtKB.
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; 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..918
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233126"
FT DOMAIN 643..897
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 768
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 649..657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 918 AA; 104337 MW; 30F28DAA8D9889F9 CRC64;
MQKDGTRSSR RMEEGDRRNG STGSSGSVSR ELGRGFSYYN KYLARLQQNL RDTKRFFRDI
KHTYSGAPGG PDTDIKGAEG DLGQLHSITF PRQEEEYLKL TVRCRPCIFI LGQSCSSRGR
VANSLLGDQL LPILTHCGSE CCKRRRIRFR YGKQTLVSLA LPEQYELVHE LVAHQGKWDT
IPEEDLDVPE DEEDPAHRLA ELEVTLPHQL LQDVDIVVSP CRSSQAVSMT LEDYVDHVQS
IVVYAVCEER LSQQDEEELT EIKEKYKLPV FFIRTSSTRD RLIGGSEGVR SALYEQLMEL
GFLKRGLCNC GAAGSGSTAP SMLVEQFEKL RQVSTFSRQV LQMHLVDAAI VLNMVHSRCL
DLFINKAFDM HRDLQITPKR LEYTRQKENE LYESLMRISD RKQEELKDMI VETLNSMREQ
LLEDAANMQF KDIAIPQNGE PVSVQEVKCC IFQIKELIIS RLNQAVVNKL ISSVDYLRES
FVGTLERCLR SLEKSQQESS SHVTSNHLKQ ILNAAYHVEV TFNSGSTVTR MVWEQIVQII
QRITWVSPPT ITPEWKRRVA QDAIESLSAS KLAKSICSQF CKRLKSSHEA FAASLKQLEV
GHSGRLEKTN DLWLRVRKDH APRLARLSLE SRSLQDVLLH GKPRIGRELG RGQYGVVYLC
DSWGGHFPCA LKSVVPPDEK HWNDLALEFH YMRSLPKHER LVDLHGSVID YSYGGGSSIA
VLLITERLHR DLYVGLKTGL SLETRLQIAL DVVEGIRFLH NQGLVHRDIK LKNVLLDKKH
RAKITDLGFC KPEAMMSGSI VGTPIHMAPE LFSGKYDNSV DVYAFGILFW YICSGSVKLP
EAFEKCASKD HLWNNVRKGA RPERLAIFDE ECWKLMEACW NGDPSQRPLM GIVQPMLQGI
MDRLCRAQET GKALEDST
