DUSTY_CANLF
ID DUSTY_CANLF Reviewed; 931 AA.
AC Q4VSN4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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; AY641093; AAV40859.1; -; mRNA.
DR RefSeq; NP_001020439.1; NM_001025268.1.
DR AlphaFoldDB; Q4VSN4; -.
DR SMR; Q4VSN4; -.
DR STRING; 9615.ENSCAFP00000014726; -.
DR PaxDb; Q4VSN4; -.
DR GeneID; 478942; -.
DR KEGG; cfa:478942; -.
DR CTD; 25778; -.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; Q4VSN4; -.
DR OrthoDB; 254886at2759; -.
DR Proteomes; UP000002254; 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..931
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000233117"
FT DOMAIN 654..908
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 397..424
FT /evidence="ECO:0000255"
FT ACT_SITE 779
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 660..668
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 931 AA; 105010 MW; 3C413FE8EE1C8725 CRC64;
MEGDAPQRVS ERVSGPGPGG GGGGMIRELC RGFGRHRRYL GQLRQNLRET QKFFRDIKCS
HSHSCPSSPA GGGAAELGPA GDVAEAPLPA GQLSCIAFPP KEEKYLQQIV DCLPCILILG
QDCNVKCQLL NLLLGVQVLP TTRLGSEENC KLRRLRFTYG TQTRVSLALP GQYELVHTLV
AHQGNWDTIP EEDLEVQEDS EDAAHVLAEL EVTMHHALLQ DVDIVVAPCQ GLRPAVDVLG
DLVNDFLPVI TYALHKDELS ERDEQELQEI RKYFSFPIFF FKVPKLGSEI IASSTRRTEN
ERSPLHHQLM DLGYLSSSHC NCGVPGQDTK AQSMLVEQSE KLRHLSTFSH QVLQTHLVDA
AKALNRVHCH CLDIFINQAF DMQRDLQITP KRLEYTRKKE NELYESLMNI ANRKQEEMKD
MICETLNTMK GELLDDAANM EFKDVIVPEN GEAVGTRELK CCIRQIQELI ISRLNQAVAN
KLISSVDYLR ESFVGTLERC LQSLEKSQDV SIHITSNYLK QILNAAYHVE VTFHSGSSVT
RMLWEQIKQI IQRITWVNPP TITLEWKRKV AQEAIDSLSA SKLAKSICSQ FRTRLNSSHE
AFAASLRQLE AGHSGRLENT EDLWLKVRKD HAPRLARLSL ESRSLQDVLL HRKPKLGQEL
GRGQYGVVYL CDNWGGHFPC ALKSVVPPDE KHWNDLALEF HYMRSLPKHE RLVDLHGSVI
DYNYGGGSSI AVLLIMERLH RDLYTGLKAG LTLETRLQIA LDVVEGIRFL HSQGLVHRDI
KLKNVLLDKQ NRAKITDLGF CKPEAMMSGS IVGTPIHMAP ELFTGKYDNS VDVYAFGILF
WYICSGSVKL PEAFERCASK DHLWNNVRRG ARPERLPVFD EECWQLMEAC WDGDPSQRPL
LGIVQPMLQG IMERLCKSNS ERPNTGLDDS T
