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Database: UniProt
Entry: M3YK12_MUSPF
LinkDB: M3YK12_MUSPF
Original site: M3YK12_MUSPF 
ID   M3YK12_MUSPF            Unreviewed;       932 AA.
AC   M3YK12;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Dual serine/threonine and tyrosine protein kinase {ECO:0000256|ARBA:ARBA00040421};
DE            EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
DE   AltName: Full=Dusty protein kinase {ECO:0000256|ARBA:ARBA00042638};
DE   AltName: Full=Receptor-interacting serine/threonine-protein kinase 5 {ECO:0000256|ARBA:ARBA00041268};
GN   Name=DSTYK {ECO:0000313|Ensembl:ENSMPUP00000011669.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011669.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000011669.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000972};
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:0000256|ARBA:ARBA00001076};
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:0000256|ARBA:ARBA00001687};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004221}. Basolateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004187}. Cell junction
CC       {ECO:0000256|ARBA:ARBA00004282}. Lateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004124}.
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DR   EMBL; AEYP01041258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01041259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01041260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01041261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01041262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01041263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3YK12; -.
DR   STRING; 9669.ENSMPUP00000011669; -.
DR   Ensembl; ENSMPUT00000011861.1; ENSMPUP00000011669.1; ENSMPUG00000011763.1.
DR   eggNOG; KOG0192; Eukaryota.
DR   GeneTree; ENSGT00840000129948; -.
DR   HOGENOM; CLU_014116_0_0_1; -.
DR   InParanoid; M3YK12; -.
DR   OMA; KSCIHLI; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd13975; PKc_Dusty; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR46392; DUAL SERINE/THREONINE AND TYROSINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR46392:SF1; DUAL SERINE_THREONINE AND TYROSINE PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          655..909
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          398..444
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         684
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   932 AA;  105685 MW;  7915806D1784EF2F CRC64;
     MEGDGVPWGS EPVSGPGPGG GGMIRELCRG FGRYRRYLGR LRQNLRETQK FFRDIKCSHS
     HSCPSYPSGY CGSKIGPVVC FLLPRPPLPR AGQLSCIAFP PKEEKYLQQV VDCLPCILIL
     GQDCNVKCQL LNLLLGVHVL PTTRPAREES CRLRRLRFTY GTQTRVGLAL PGQYELVHTL
     VAHQGNWETI PEEDLEVQED GEDTAPVLAE LEVTMHHALL QDVDIVVAPC QGLRPAVDVL
     GDLVNDFLPV ITYALHKDEL SERDEQELQE IRKYFSFPVF FFKVPKLGSE IIASPTRRLE
     NERSALHHQL VDLGYLSSSH WNCGTSGQDT KAQSMLVEQS EKLRHLSTFS HQVLQTRLVD
     TAKALNRVHC HCLDIFINQA FDMQRDLQIT PKRLEYTRKK ENELYESLMN IANRKQEEMK
     DMIVETLNAM KEELLEDAAN MEFKDVIVPE NGEAVGTREI KCCIRQIQEL IISRLNQAVA
     NKLISSVDYL RESFVGTLER CLQSLEKSQD VSVHITSNYL KQILNAAYHV EVTFHSGSSV
     TRMLWEQIKQ IIQRLTWVSP PAITLEWKRK VAQEAIESLS ASKLAKSICS QFRTRLNSSH
     EAFAASLRQL EAGHSGRLEK TEDLWLKVRK DHAPRLARLS LESRSLQDVL LHRKPKLGQE
     LGRGQYGVVY LCDNWGGHFP CALKSVVPPD EKHWNDLALE FHYMRSLPKH ERLVDLHGSV
     IDYSYGGGSS IAVLLIMERL HRDLYTGLKA GLTLETRLQI ALDVVEGVRF LHSQGLVHRD
     IKLKNVLLDK QNRAKITDLG FCKPEAMMSG SIVGTPIHMA PELFTGKYDN SVDVYAFGIL
     FWYICSGSVK LPEAFERCAS KDHLWNNVRR GARPERLPVF DEECWQLMEA CWDGDPSQRP
     LLGIVQPMLQ GIMDRLCKSS SERPSRGLDD ST
//
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