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Database: UniProt
Entry: W5PBE3_SHEEP
LinkDB: W5PBE3_SHEEP
Original site: W5PBE3_SHEEP 
ID   W5PBE3_SHEEP            Unreviewed;       685 AA.
AC   W5PBE3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Serine/threonine-protein kinase PLK {ECO:0000256|RuleBase:RU361162};
DE            EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
DE   AltName: Full=Polo-like kinase {ECO:0000256|RuleBase:RU361162};
GN   Name=PLK2 {ECO:0000313|Ensembl:ENSOARP00000007754.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000007754.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000007754.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000007754.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000007754.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR   EMBL; AMGL01034623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004017013.1; XM_004016964.3.
DR   AlphaFoldDB; W5PBE3; -.
DR   SMR; W5PBE3; -.
DR   STRING; 9940.ENSOARP00000007754; -.
DR   PaxDb; 9940-ENSOARP00000007754; -.
DR   Ensembl; ENSOART00000007869.1; ENSOARP00000007754.1; ENSOARG00000007234.1.
DR   GeneID; 101110619; -.
DR   KEGG; oas:101110619; -.
DR   CTD; 10769; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   HOGENOM; CLU_000288_46_1_1; -.
DR   OMA; QRRRTIC; -.
DR   OrthoDB; 5471704at2759; -.
DR   Proteomes; UP000002356; Chromosome 16.
DR   Bgee; ENSOARG00000007234; Expressed in uterus and 52 other cell types or tissues.
DR   GO; GO:0005814; C:centriole; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043008; F:ATP-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0007052; P:mitotic spindle organization; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; IEA:Ensembl.
DR   GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0046599; P:regulation of centriole replication; IEA:Ensembl.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   CDD; cd14188; STKc_PLK2; 1.
DR   Gene3D; 3.30.1120.30; POLO box domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR042825; PLK2_STKc.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF44; SERINE_THREONINE-PROTEIN KINASE PLK2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU361162};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT   DOMAIN          82..334
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          510..573
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          606..677
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          24..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   685 AA;  78265 MW;  AF363B127D015A74 CRC64;
     MELLRTITYQ PAASTKMCEQ ALGKACGGDS KKKRPQPSPE EPQPPQTPAQ VQPAVPHHHH
     HHSHSGAEIS RIIIDPTTGK RYCRGKVLGK GGFAKCYEMT DLTNNKVYAA KIIPHSRVAK
     PHQREKIDKE IELHRILHHK HVVQFYHYFE DKENIYILLE YCSRRSMAHI LKARKVLTEP
     EVRYYLRQIV SGLKYLHEQE ILHRDLKLGN FFINEAMELK VGDFGLAARL EPLEHRRRTI
     CGTPNYLSPE VLNKQGHGCE SDIWALGCVM YTMLLGRPPF ETTNLKETYR CIREARYTMP
     SSLLAPAKHL IASMLSKNPE DRPSLDDIIR HDFFLQGFTP DRLSSSCCHT VPDFHLSSPA
     KNFFKKAAAA LFGGKKDKAR YIDTHNKVSK EDEEIYKLRH DLKKTSITQQ PSKHRTDEEL
     QPPTTTVARS GTPAVENKQQ IGDAIRMIVR GTLGSCSSSS ECLEDSTMGS VADTVARVLR
     GCLENMPEAD CIPKEQLSTS FQWVTKWVDY SNKYGFGYQL SDHTVGVLFN NGAHMSLLPD
     KKTVHYYAEL GQCSVFPATD APEQFISQVT VLKYFSHYME ENLMDGGDLP SVTDVRRPRL
     YLLQWLKSDK ALMMLFNDGT FQVNFYHDHT KIIICSQNEE YLLTYINEDR ISTTFRLTTL
     LMSGCSLELK NRMEYALNML LQRCN
//
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