DUSTY_BOVIN
ID DUSTY_BOVIN Reviewed; 928 AA.
AC Q4TVR5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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; DQ054504; AAY46409.1; -; mRNA.
DR RefSeq; NP_001019995.1; NM_001024824.1.
DR AlphaFoldDB; Q4TVR5; -.
DR SMR; Q4TVR5; -.
DR STRING; 9913.ENSBTAP00000022108; -.
DR PaxDb; Q4TVR5; -.
DR PRIDE; Q4TVR5; -.
DR Ensembl; ENSBTAT00000022108; ENSBTAP00000022108; ENSBTAG00000016618.
DR GeneID; 534684; -.
DR KEGG; bta:534684; -.
DR CTD; 25778; -.
DR VEuPathDB; HostDB:ENSBTAG00000016618; -.
DR VGNC; VGNC:28227; DSTYK.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00840000129948; -.
DR HOGENOM; CLU_014116_0_0_1; -.
DR InParanoid; Q4TVR5; -.
DR OMA; KSCIHLI; -.
DR OrthoDB; 254886at2759; -.
DR TreeFam; TF331821; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000016618; Expressed in spermatid and 105 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..928
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233116"
FT DOMAIN 651..905
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 REGION 55..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..430
FT /evidence="ECO:0000255"
FT ACT_SITE 776
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 657..665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 928 AA; 104804 MW; 21AE8DAF0D53DFE8 CRC64;
MEGDGVPWGS EPESGPGPGG GGVIRELCRG FGRYRRYLGR LRQNLRDTQK FFRDLRGSQP
RGCPSSPAEG GEAGRGPAGD VAATGLPAGQ LSCISFPPKE EKRLQQMVDC LPCILILGQD
CSVKCQLLNL LLGVQVLPTN KLGGENCKLR RLRFTYGTQT RVSLALPDRY ELVHTLAAHQ
GTWETVPEED LEAREDSEDA ARVLAELEVT MRHALLQEVD IVVAPCQGLR PTVDVLSDLV
NDFLPVITYA LHKDELSERD EQELQEIRKY FSFPIFFFKV PKLGSEIIDS STERMESERS
PLHRQLTDLG YLSSSLCNCG APGQDTKAQS MLVEQSEKLR HLNTFSHQVL QTRLVDAAKA
LNLVHCRCLD IFINQAFDMQ RDLQITPKRL EYTRKKENEL YESLMNIANR KQEEMKDMIV
ETLNTMKEEL LDDAANMEFK DVIVPENGEP VGTREIKCCI RQIQELIISR LNQAVANKLI
SSVDYLRESF VGTLERCLQS LEKSQDVSVH ITSNYLKQIL NAAYHVEVTF HSGSSVTRML
WEQIKQIIQR ITWVSPPAIT LEWKRKVAQE AIESLSASKL AKSICSQFRT RLNSSHEAFA
ASLRQLEAGH SGRLEKTEDL WLKVRKDHAP RLARLSLESR SLQDVLLHRK PKLGQELGRG
QYGVVYLCDS WGGHFPCALK SVVPPDEKHW NDLALEFHYM RSLPKHERLV DLHGSVIDYS
YGGGSSIAVL LIMERLHRDL YTGLKAGLAL ETRLQIALDV VEGIRFLHSQ GLVHRDVKLK
NVLLDKQNRA KITDLGFCKP EAMMSGSIVG TPIHMAPELF TGKYDNSVDV YAFGILFWYI
CSGSVKLPEA FERCASKDHL WNNVRRGARP ERLPVFDEEC WQLMEACWDG DPSQRPLLGI
VQPMLQGIMD RLCKSHSERP NRGLDDST
