DUSTY_TETNG
ID DUSTY_TETNG Reviewed; 922 AA.
AC Q4VSN3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
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:AAV40860.1};
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 Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1] {ECO:0000312|EMBL:AAV40860.1}
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}.
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DR EMBL; AY641094; AAV40860.1; -; mRNA.
DR AlphaFoldDB; Q4VSN3; -.
DR SMR; Q4VSN3; -.
DR STRING; 99883.ENSTNIP00000004768; -.
DR Ensembl; ENSTNIT00000002065; ENSTNIP00000000837; ENSTNIG00000014651.
DR GeneTree; ENSGT00840000129948; -.
DR InParanoid; Q4VSN3; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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; Cytoplasm;
KW Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..922
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000374058"
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:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 651..659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 922 AA; 103531 MW; 63A04B6409935998 CRC64;
MEGHGAQRSS PLARDLTRAF TSYNKHTVLL KKNLKETHAF FREMRQNYSN TCASSTLSSD
SSSQETGQFS CISFPSHEEE FLRNTVGAAP YILVLGQDCA ARYQLLNCLL GDRLLPLGPE
AGQACHGGQG NVCKRRKLCF THGRQTRLSL ALPGQYELVH QLAANCGRWE TVPREDLEIL
DECEDPAHRQ AELEITLHHP LLQEAKVMVV PCPSVQPIEE ALEDCTRSVI PIILYAVNRD
SLSSEQVADL RKVKEILSFP VCYVRLPDAS AASAELGQRC EKDKSKLQKQ LLSRGLLGSL
SGNCSCGAPA QTAAPGAKPQ SVVGENFEKL HRILVPFTRQ VLQNQQVEAA SLLNGLHCRC
LDLFINQAFD MQRDLQITPR RLEYTREKEG ELFTSLMTIA NRKQEEMKDM IVETLGSMKE
QLLEDAANLE FTDIIVTTNG DPVTSKEIKS CIQQIQDLIV VRLNQAVANK LISSVDYLRE
SFVGTLERCL SSLEKSHIES SVHNITSNHL KQLLNAAYHV EVTFHSGSSV TRLFWEQIKQ
IIHRITFVNP PAITPEWKRK VAQDAIESLS AAKLARSICS QFRTRLYSSH EAFAASLRQL
EERHTGRLER TEDLWLRVRK DHAPRLARLS LESRSLRDVV LHGKPKLGRE LGRGQYGVVY
LCDSWGGHNP CALKSVVPPD DKHWNDLALE FHYTRTLPKH ERLVDLHGSV IDHTYAGGSS
IAVLLIMERL HRDLYTGLKA GLSLQERLQI ALDVVEGIRF LHSQGLLHRD IKLKNVLLDK
QNRAKITDLG FCKPEAMMSG SIVGTPIHMA PELFTGKYDN SVDVYAFGIL FWYLCAGSVK
LPEAFEKCSS KDQLWNNVRK GARPERLPCF DEECWQLMEA CWNGDPSQRP LLGIVEPSLE
SITVRMCNCG SEQKSSSLED SC
