STK10_XENTR
ID STK10_XENTR Reviewed; 951 AA.
AC Q0IHQ8; F7A3L3;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Serine/threonine-protein kinase 10;
DE EC=2.7.11.1;
GN Name=stk10;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AAMC01112142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01112143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01112144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01112145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC123019; AAI23020.1; -; mRNA.
DR RefSeq; NP_001072623.1; NM_001079155.1.
DR AlphaFoldDB; Q0IHQ8; -.
DR SMR; Q0IHQ8; -.
DR PaxDb; Q0IHQ8; -.
DR DNASU; 780079; -.
DR Ensembl; ENSXETT00000031556; ENSXETP00000031556; ENSXETG00000014423.
DR GeneID; 780079; -.
DR KEGG; xtr:780079; -.
DR CTD; 6793; -.
DR Xenbase; XB-GENE-494456; stk10.
DR eggNOG; KOG0579; Eukaryota.
DR InParanoid; Q0IHQ8; -.
DR OrthoDB; 851098at2759; -.
DR Reactome; R-XTR-6798695; Neutrophil degranulation.
DR Reactome; R-XTR-9013026; RHOB GTPase cycle.
DR Reactome; R-XTR-9013106; RHOC GTPase cycle.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014423; Expressed in liver and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 2: Evidence at transcript 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..951
FT /note="Serine/threonine-protein kinase 10"
FT /id="PRO_0000414715"
FT DOMAIN 36..294
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 319..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 583..723
FT /evidence="ECO:0000255"
FT COILED 898..928
FT /evidence="ECO:0000255"
FT COMPBIAS 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..479
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 483
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250"
FT MOD_RES 487
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250"
FT MOD_RES 491
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 951 AA; 111828 MW; BB08720CABE2960D CRC64;
MAFANFRRIL RLPNFEKKRL REYEHVRRDL DPNQVWEIIG ELGDGAFGKV YKAKNKETGI
LAAAKVIETK NEEELEDYMV EIEILATCNH HFIVKLLGSY YWEGKLWIMI EFCPGGAVDA
IMLELDRGLK EPEIRTICRQ MLEGLTYLHS MKMIHRDLKA GNVLLTLDGD IKLADFGVSA
KNVKTLQRRD SFIGTPYWMA PEVVMCETMK DAPYDYKADI WSLGITLIEM AQIEPPHHEL
NPMRVLLKIA KSEPPTLSSP SKWSPEFHNF LKTALDKNPE TRPSAAQLLE HPFVKKVSGN
KPLRDLVAEA KAEVLDEIEE NGEVEEEEAS DTPSSNKSVS QSALGEKDKH TGKEHVGNGI
KAEPQNTDSQ ADIHSQKRNH EGKNYPEHNR HDAVNGKPDI IILNPVSSNH EPKRNSAAES
YRNEEHGSAV SSNQRPKSSQ SDRQSVELVP NGSFDSPTRY FTGWSKRDSD SGSNSASESM
DISMNLSADL SINKETGSLS LRESRLHKKT LKRTRRFVVD GVEVSITTSK IIGDDEKKDE
EMRFLRRQEL RELRLLQKEE HRNQAQLTSK HSFQMEQMLR RFEQEMNSKR KFYDSELEAL
ERHQKQQIER MEQEHALRRR DEARRIRTEQ ERDHVKFLEQ LKLRKKELKA QVEKLPRQQR
RDAMKVQMDD FAQKKHIEEQ QFLNKQKEDL TLALRVIVLE NRKEIYNKER EFLNKKQQLL
RDREAVIWDL EERHLQERHQ LVKQQLKDQY FLQRHELLRK HEKEQEQMQR YNQRMMEQLK
LRQQQERARL PKNQKAEAKT RMTMFKKSLH ISPSGSAAEQ REKIKQFSLQ EEKRQKAERL
QQQQKHEHQL LEMQAECDCN VRDLLQMQNE KCHLLVEHET QKLKTLDEHH IQMIREWREN
LRPRKKALED ELEHKKEEQE MFFRMNEEVA GHPFPSNKPA KFYSFSSPEA S
