STK10_XENLA
ID STK10_XENLA Reviewed; 950 AA.
AC B7ZR30; B7ZR32; Q9YHC9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Serine/threonine-protein kinase 10-A;
DE EC=2.7.11.1;
DE AltName: Full=Polo-like kinase kinase 1;
DE Short=XPlkk1;
GN Name=stk10-a; Synonyms=plkk1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP AND AUTOPHOSPHORYLATION.
RX PubMed=9831560; DOI=10.1126/science.282.5394.1701;
RA Qian Y.W., Erikson E., Maller J.L.;
RT "Purification and cloning of a protein kinase that phosphorylates and
RT activates the polo-like kinase Plx1.";
RL Science 282:1701-1704(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=12207013; DOI=10.1074/jbc.m202172200;
RA Jang Y.-J., Ma S., Terada Y., Erikson R.L.;
RT "Phosphorylation of threonine 210 and the role of serine 137 in the
RT regulation of mammalian polo-like kinase.";
RL J. Biol. Chem. 277:44115-44120(2002).
RN [4]
RP PHOSPHORYLATION AT SER-482; SER-486 AND SER-490, AND MUTAGENESIS OF
RP SER-482; SER-486 AND SER-490.
RX PubMed=15166215; DOI=10.1074/jbc.m403840200;
RA Erikson E., Haystead T.A., Qian Y.W., Maller J.L.;
RT "A feedback loop in the polo-like kinase activation pathway.";
RL J. Biol. Chem. 279:32219-32224(2004).
CC -!- FUNCTION: May act as a polo kinase kinase by mediating phosphorylation
CC of plk1/plx1 and subsequent activation of plk1/plx1 during oocyte
CC maturation. {ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:9831560}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylates. Phosphorylated by plk1/plx1, suggesting the
CC existence of a feedback loop with plk1/plx1. activation of the protein.
CC {ECO:0000269|PubMed:15166215}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- CAUTION: It is unclear whether it acts as an upstream kinase for polo
CC kinase by mediating phosphorylation of plk1/plx1 or whether it is a
CC downstream target of plk1/plx1. {ECO:0000305|PubMed:15166215}.
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DR EMBL; AF100165; AAC95157.1; -; mRNA.
DR EMBL; BC170020; AAI70020.1; -; mRNA.
DR EMBL; BC170022; AAI70022.1; -; mRNA.
DR RefSeq; NP_001079164.1; NM_001085695.1.
DR AlphaFoldDB; B7ZR30; -.
DR SMR; B7ZR30; -.
DR iPTMnet; B7ZR30; -.
DR PRIDE; B7ZR30; -.
DR GeneID; 373731; -.
DR KEGG; xla:373731; -.
DR CTD; 373731; -.
DR Xenbase; XB-GENE-866353; stk10.S.
DR OrthoDB; 851098at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 373731; Expressed in blastula and 17 other tissues.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:2000401; P:regulation of lymphocyte migration; ISS:UniProtKB.
DR CDD; cd06644; STKc_STK10; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR042743; STK10_STKc.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell membrane; Coiled coil; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..950
FT /note="Serine/threonine-protein kinase 10-A"
FT /id="PRO_0000414714"
FT DOMAIN 36..294
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 319..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 634..786
FT /evidence="ECO:0000255"
FT COMPBIAS 361..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 482
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:15166215"
FT MOD_RES 486
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:15166215"
FT MOD_RES 490
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:15166215"
FT MUTAGEN 482
FT /note="S->A: Decreased phosphorylation by plk1/plx1; when
FT associated with A-486 and A-490."
FT /evidence="ECO:0000269|PubMed:15166215"
FT MUTAGEN 486
FT /note="S->A: Decreased phosphorylation by plk1/plx1; when
FT associated with A-482 and A-490."
FT /evidence="ECO:0000269|PubMed:15166215"
FT MUTAGEN 490
FT /note="S->A: Decreased phosphorylation by plk1/plx1; when
FT associated with A-482 and A-486."
FT /evidence="ECO:0000269|PubMed:15166215"
FT CONFLICT 56
FT /note="R -> W (in Ref. 1; AAC95157)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="K -> Q (in Ref. 2; AAI70022)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="R -> K (in Ref. 1; AAC95157)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="K -> N (in Ref. 1; AAC95157)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..402
FT /note="GK -> RN (in Ref. 1; AAC95157)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="M -> I (in Ref. 1; AAC95157)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="H -> Q (in Ref. 2; AAI70022)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="L -> P (in Ref. 1; AAC95157 and 2; AAI70022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 950 AA; 111778 MW; 43E625031D6ED407 CRC64;
MAFANFRRIL RLPNFEKKRL REYEHVRRDV DPNQVWEIIG ELGDGAFGKV YKAKNRETGI
LAAAKVIETK NEEELEDYMV EIEILATCNH HFIVKLLGAF YWEGKLWIMI EFCPGGAVDA
VMLELDRGLK EPEIKTICRQ MLEALAYLHS MKIIHRDLKA GNVLLTLDGD IKLADFGVSA
KNVKTLQRRD SFIGTPYWMA PEVVMCETMK DAPYDYKADI WSLGITLIEM AQIEPPHHEL
NPMRVLLKIA KSEPPTLSSL SKWSPEFHSF LKTALDKNPE TRPSAAQLLE HPFVKKASGN
KPLRDLVAEA KAEVLDEIEE QGEAEEEEDS DMLSPKTKGV SQSTHVEIGK DIEREQVGNG
IKPHSATSPQ KTDSQADNYS QRRNNEVKNC PENGRPDAVN GKPDIIILNP LSSNLEPKRN
STAESYRGEE HSSASSQRQR SAQSAELVPN GSFDSPTRYF TNWSKRDSDS GSNSASESMD
ISMNLSADLS MNKETGFLSH RENRLHKKTL KRTRRFVVDG VEVSITTSKI IGDDEKKDEE
MRFLRRQELR ELRLLQKEEH RHQAQLTSKH SFQLEQMSRR FEQEMNSKRK FYDTELETLE
RHQKQQIVWM EQEHAFRRRD EAKHIKTEQE RDHIKFLEQL KLRKKELKAH VEKLPRQQRR
ETMKVQMDGF AHKKQTEEQQ FVNRQKEDLN LAMRVIVLEN RKEIYNKERE FLNKKQQLLR
DRESVIWELE ERHLQERHQL VKQQLKDQYF LQRHELLRKH EKEQEQMQRY NQRMMEQLRL
RQQQEKVRLP KNQKAEAKTR MTMFKKSLHI SPSGSAAEQR DKIKQFSLQE EKRQKAERLQ
QQQKHEHQLM EMLAECDCNV RDLLQMQNEK CHLLVEHETQ KLKSLDEHHI QLIREWRENI
RPRKKAFEDE LELKKEAQEM FFRLNEEVAG DPFLSNKPTR FYSFSSPEAS
