DUSTY_TAKRU
ID DUSTY_TAKRU Reviewed; 921 AA.
AC Q4VSN2; Q6XUW9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4VSN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4VSN2-2; Sequence=VSP_018041, VSP_018042;
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; AY208854; AAP42422.1; -; mRNA.
DR EMBL; AY429680; AAS55396.1; -; mRNA.
DR EMBL; AY641095; AAV40861.1; -; mRNA.
DR RefSeq; NP_001027827.1; NM_001032655.1. [Q4VSN2-2]
DR RefSeq; XP_011612104.1; XM_011613802.1.
DR AlphaFoldDB; Q4VSN2; -.
DR SMR; Q4VSN2; -.
DR STRING; 31033.ENSTRUP00000023514; -.
DR GeneID; 445996; -.
DR KEGG; tru:445996; -.
DR CTD; 25778; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_014116_0_0_1; -.
DR InParanoid; Q4VSN2; -.
DR OrthoDB; 254886at2759; -.
DR Proteomes; UP000005226; 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: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 Alternative splicing; 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..921
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233124"
FT DOMAIN 645..899
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 770
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 651..659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 513..540
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17123648"
FT /id="VSP_018041"
FT VAR_SEQ 817..861
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17123648"
FT /id="VSP_018042"
SQ SEQUENCE 921 AA; 103845 MW; F3E559F57BB5485A CRC64;
MEGHGPQKSS PLARDLTRAF NGYHKQTVLL KKNLKETHAF FREMRQNYSN TCASSTLSSD
SASLETSQFS CISFPSHEEE FLRNTVGAAP YILVLGQDCA ARYQLLNCLL GERLLPLGPQ
AGHACHGGQG STCKRRKLCF THGKQTRLSL ALPGQYELVH QLVANCGRWD TVPREDLEIL
DECEDPAHRQ AELEITLHHP MLQEAKVMVV PCPSVQPIEE AIEDCTRSAI PIVLYAVNQD
SLSSEQVADL WKVKEILSFP ICFVRLPNLS EDSSEPGQRF EKDKSKLQKQ LLSHGLLTCP
MGNCSCGAPT QMPTPGAKPQ SVLGENFERL HRILVPFTRQ VLQNQQVEAA SLLNGLHCRC
LDLFINQAFD MQRDLQITPR RLEYTREKEG ELFTSLMAIA NRKQEEMKDM IVETLGSMKE
QLLEDAANLE FTDIIVTTNG DPVTSKEIKS CIHQIQDLIV VRLNQAVANK LISSVDYLRE
SFVGTLERCL DSLEKSHIES SVHNITSNHL KQLLNAAYHV EVTFHSGSSV TRLFWEQIKQ
IIHRITFVNP PAITPEWKRK VAQDAIESLS AAKLARSICS QFRTRLNSSH EAFAASLRQL
EERHTGRLER TEDLWLRVRK DHAPRLARLS LESRSLRDVL LHGKPKLGRE LGRGQYGVVY
LCDNWGGHYP CALKSVVPPD DKHWNDLALE FHYTRTLPKH ERLVDLHGSV IDHTYAGGSS
IAVLLIMERL HRDLYTGLKA GLSLQERLQI ALDVVEGIRF LHNQGLLHRD IKLKNVLLDK
QNRAKITDLG FCKPEAMMSG SIVGTPIHMA PELFTGKYDN SVDVYAFGIL FWYLCAGSVK
LPEAFEKCSS KDQLWNNVKK GARPERLPCF DEECWQLMEA CWNGDPSQRP LLGIVEPSLQ
SMMVRLCCGS EQKSSSLEDS S
