DUSTY_MACMU
ID DUSTY_MACMU Reviewed; 907 AA.
AC Q20CR4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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:ABD72471.1};
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1] {ECO:0000312|EMBL:ABD72471.1}
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: 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 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}. 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; DQ341264; ABD72471.1; -; mRNA.
DR RefSeq; NP_001035038.1; NM_001039949.1.
DR AlphaFoldDB; Q20CR4; -.
DR SMR; Q20CR4; -.
DR STRING; 9544.ENSMMUP00000013732; -.
DR GeneID; 664732; -.
DR KEGG; mcc:664732; -.
DR CTD; 25778; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_014116_0_0_1; -.
DR InParanoid; Q20CR4; -.
DR OrthoDB; 254886at2759; -.
DR Proteomes; UP000006718; 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; 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; 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; Coiled coil; Cytoplasm; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..907
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000374056"
FT DOMAIN 630..884
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 373..409
FT /evidence="ECO:0000255"
FT ACT_SITE 755
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 636..644
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 907 AA; 103206 MW; F77E50BF58972BF1 CRC64;
MIRELCRGFG RYRRYLGRLR QNLRETQKFF RDIKCSHNHT CPSSPTSGGG AERGPAGDVA
ETGLQAGQLS CISFPPKEEK YLQQIVDCLP CILILGQDCN VKCQLLNLLL GVQVLPTTKL
GSEESCKLRR LRFTYGTQTR VSLALPGQYE LVHTLVAHQG NWETIPEEDL EVQENNEDAA
HVLAELEVTM HHALLQEVDV VVAPCQGLRP TVDVLGDLVN DFLPVITYAL HKDELSERDE
QELQEIRKYF SFPVFFFKVP KLGSEITDSS TRRTESERSL LYRQLIDLGY LSSSHWNCGT
PGQDTKAQSV LVEQSEKLRH LSTFSHQVLQ TRLVDAAKAL NLVHCHCLDI FINQAFDMQR
DLQITPKRLE YTRKKENELY ESLMNIANRK QEEMKDMIVE TLNTMKEELL DDAANMEFKD
VIVPENGEPV GTREIKCCIR QIQELIISRL NQAVANKLIS SVDYLRESFV GTLERCLQSL
EKSQDVSVHI TSNYLKQILN AAYHVEVTFH SGSSVTRMLW EQIKQIIQRI TWVSPPAITL
EWKRKVAQEA IESLSASKLA KSICSQFRTR LNSSHEAFAA SLRQLEAGHS GRLEKTEDLW
LKVRKDHAPR LARLSLESRS LQDVLLHRKP KLGQELGRGQ YGVVYLCDNW GGHFPCALKS
VVPPDEKHWN DLALEFHYMR SLPKHERLVD LHGSVIDYNY GGGSSIAVLL IMERLHRDLY
TGLKAGLTLE TRLQIALDVV EGIRFLHSQG LVHRDIKLKN VLLDKQNRAK ITDLGFCKPE
AMMSGSIVGT PIHMAPELFT GKYDNSVDVY AFGILFWYIC SGSVKLPEAF ERCASKDHLW
NNVRRGARPE RLPVFDEECW QLMEACWDGD PLKRPLLGIV QPMLQGIMDR LCKSNSEQPN
RGLDDST
