DUSTY_PANTR
ID DUSTY_PANTR Reviewed; 930 AA.
AC Q4VSN5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, 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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [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 -!- 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY641092; AAV40858.1; -; mRNA.
DR RefSeq; NP_001029338.1; NM_001034166.1.
DR AlphaFoldDB; Q4VSN5; -.
DR SMR; Q4VSN5; -.
DR STRING; 9598.ENSPTRP00000003173; -.
DR PaxDb; Q4VSN5; -.
DR Ensembl; ENSPTRT00000003448; ENSPTRP00000003173; ENSPTRG00000001895.
DR GeneID; 457666; -.
DR KEGG; ptr:457666; -.
DR CTD; 25778; -.
DR VGNC; VGNC:6785; DSTYK.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00840000129948; -.
DR HOGENOM; CLU_014116_0_0_1; -.
DR InParanoid; Q4VSN5; -.
DR OMA; KSCIHLI; -.
DR OrthoDB; 254886at2759; -.
DR TreeFam; TF331821; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001895; Expressed in bone marrow and 21 other tissues.
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..930
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233120"
FT DOMAIN 653..907
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..216
FT /evidence="ECO:0000255"
FT COILED 396..432
FT /evidence="ECO:0000255"
FT ACT_SITE 778
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 659..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 930 AA; 105305 MW; 347812961CF5F68A CRC64;
MEGDGVPWGS EPVSGPGPGG GGGMIRELCR GFGRYRRYLG RLRQNLRETQ KFFRDIKCSH
NHTCLSSLTG GGGAERGPAG DVAETGLQAG QLSCISFPPK EEKYLQQIVD CLPCILILGQ
DCNVKCQLLN LLLGVQVLPT TKLGSEESCK LRRLRFTYGT QTRVSLALPG QYELVHTLVA
HQGNWETIPE EDLEVQENNE DAAHVLAELE VTMHHALLQE VDVVVAPCQG LRPTVDVLGD
LVNDFLPVIT YALHKDELSE RDEQELQEIR KYFSFPVFFF KVPKLGSEII DSSTKRMESE
RSLLYRQLID LGYLSSSHWN CGAPGQDTKA QSMLVEQSEK LRHLSTFSHQ VLQTRLVDAA
KALNLVHCHC LDIFINQAFD MQRDLQITPK RLEYTRKKEN ELYESLMNIA NRKQEEMKDM
IVETLNTMKE ELLDDATNME FKDVIVPENG EPVGTREIKC CIRQIQELII SRLNQAVANK
LISSVDYLRE SFVGTLERCL QSLEKSQDVS VHITSNYLKQ ILNAAYHVEV TFHSGSSVTR
MLWEQIKQII QRITWVSPPA ITLEWKRKVA QEAIESLSAS KLAKSICSQF RTRLNSSHEA
FAASLRQLEA GHSGRLEKTE DLWLRVRKDH APRLARLSLE SRSLQDVLLH RKPKLGQELG
RGQYGVVYLC DNWGGHFPCA LKSVVPPDEK HWNDLALEFH YMRSLPKHER LVDLHGSVID
YNYGGGSSIA VLLIMERLHR DLYTGLKAGL TLETRLQIAL DVVEGIRFLH SQGLVHRDIK
LKNVLLDKQN RAKITDLGFC KPEAMMSGSI VGTPIHMAPE LFTGKYDNSV DVYAFGILFW
YICSGSVKLP EAFERCASKD HLWNNVRRGA RPERLPVFDE ECWQLMEACW DGDPLKRPLL
GIVQPMLQGI MDRLCKSNSE QPNRGLDDST
