DUSTY_RAT
ID DUSTY_RAT Reviewed; 927 AA.
AC Q6XUX2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; 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: Acts as a positive regulator of ERK phosphorylation
CC downstream of fibroblast growth factor-receptor activation. Involved in
CC the regulation of both caspase-dependent apoptosis and caspase-
CC independent cell death. In the skin, it plays a predominant role in
CC suppressing caspase-dependent apoptosis in response to UV stress in a
CC range of dermal cell types. {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}. Note=Detected in basolateral and apical
CC membranes of all tubular epithelia. Detected at apical cell-cell
CC junctions. Colocalized with FGF receptors to the cell membrane.
CC {ECO:0000250|UniProtKB:Q6XUX1}.
CC -!- TISSUE SPECIFICITY: Expressed in many regions of the adult brain.
CC {ECO:0000269|PubMed:17123648}.
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; AY208851; AAP42419.1; -; mRNA.
DR EMBL; AY429675; AAS55391.1; -; mRNA.
DR RefSeq; NP_955750.1; NM_199463.2.
DR AlphaFoldDB; Q6XUX2; -.
DR SMR; Q6XUX2; -.
DR BioGRID; 257980; 1.
DR STRING; 10116.ENSRNOP00000004810; -.
DR jPOST; Q6XUX2; -.
DR PaxDb; Q6XUX2; -.
DR PRIDE; Q6XUX2; -.
DR GeneID; 304791; -.
DR KEGG; rno:304791; -.
DR UCSC; RGD:735051; rat.
DR CTD; 25778; -.
DR RGD; 735051; Dstyk.
DR VEuPathDB; HostDB:ENSRNOG00000021298; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_014116_0_0_1; -.
DR InParanoid; Q6XUX2; -.
DR OMA; KSCIHLI; -.
DR OrthoDB; 254886at2759; -.
DR PhylomeDB; Q6XUX2; -.
DR TreeFam; TF331821; -.
DR PRO; PR:Q6XUX2; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000021298; Expressed in cerebellum and 18 other tissues.
DR Genevisible; Q6XUX2; RN.
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; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; 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; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..927
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233121"
FT DOMAIN 650..904
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..429
FT /evidence="ECO:0000255"
FT ACT_SITE 775
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 656..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 927 AA; 104898 MW; 88C938259D04472C CRC64;
MEADGQSWSG ESVSGPGPGG GGMIRELCRG FGRYRRYLGR LRQNLRETQK FFRDIKCSHS
HSCPSSPAGG GAAELGPAGD VAAAPLPAGQ LSCISFPPME EKYLQQIVDH LPCILILGQD
CNAKCQLLNL LLAVRVLPTL KLDSDESCKL RRLRFTYGTR TQVSLALPGQ YELVHTLASH
QDNWETIPEE DLEVQEDSED TARVLADLEV TMHHALLQEV DIVVAPCHSH RPAVDVLSDL
ANDFLPVITY ALHKDELSER DEQELQEIRK YFSFPVFFFK VPTLEIIRSS SGRADSERSP
LSGQLMDLGY LSSSHRNCMA SDQDCRAQSM LVEQSEKLRQ LSTFSHQLLQ TRLVDAAKAL
NAVHSHCLDI FINQAFDMQR DLQITPKRLE YTRKKENELY ESLMNIANRK QEEMKDMIVE
TLNTMKEELL DDAANMEFKD VIVPENGETV GTREIKSCIR QIQELIISRL NQAVANKLIS
SVDYLRESFV GTLERCLQSL EKSQDVSVHI TSNYLKQILN AAYHVEVTFH SGSSVTRMLW
EQIKQIIQRI TWVNPPTITL EWKRKVAQEA IDSLSASKLA KSICSQFRTR LNSSHEAFAA
SLRQLEAGHS GRLEKTEDLW LKVRKDHAPR LARLSLESRS LQDVLLHRKP KLGQELGRGQ
YGVVYLCDNW GGHFPCALKS VVPPDEKHWN DLALEFHYMR SLPKHERLVD LHGSVIDYNY
GGGSSVAVLL IMERLHRDLY TGLKAGLSLE TRLQIALDVV EGIRFLHSQG LVHRDIKLKN
VLLDKQNRAK ITDLGFCKPE AMMSGSIVGT PIHMAPELFT GKYDNSVDVY AFGILFWYIC
SGSIKLPEAF ERCASKDHLW NNVRRGTRPE RLPVFDEECW QLMEACWDGD PSKRPLLGIV
QPILRSIMDR LCKCDSERPS RGLDDST
