ID   STK10_DANRE             Reviewed;         974 AA.
AC   Q7SY52;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Serine/threonine-protein kinase 10;
DE            EC=2.7.11.1;
GN   Name=stk10; ORFNames=zgc:63495;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a polo kinase kinase by mediating phosphorylation
CC       of plk1. {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. {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; BC055124; AAH55124.1; -; mRNA.
DR   RefSeq; NP_957427.1; NM_201133.1.
DR   AlphaFoldDB; Q7SY52; -.
DR   SMR; Q7SY52; -.
DR   STRING; 7955.ENSDARP00000103060; -.
DR   PaxDb; Q7SY52; -.
DR   PRIDE; Q7SY52; -.
DR   GeneID; 394108; -.
DR   KEGG; dre:394108; -.
DR   CTD; 6793; -.
DR   ZFIN; ZDB-GENE-040426-1136; stk10.
DR   eggNOG; KOG0579; Eukaryota.
DR   InParanoid; Q7SY52; -.
DR   OrthoDB; 851098at2759; -.
DR   PhylomeDB; Q7SY52; -.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR   Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR   PRO; PR:Q7SY52; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..974
FT                   /note="Serine/threonine-protein kinase 10"
FT                   /id="PRO_0000414713"
FT   DOMAIN          37..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          320..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          605..729
FT                   /evidence="ECO:0000255"
FT   COILED          870..950
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        339..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         43..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   974 AA;  113687 MW;  370DB9A41360D89C CRC64;
     MAFSKFGKMF RLPTIEIKKK TKQYNHLQRD VNPNDMWEII GELGDGAFGK VYKAQNKETG
     VLAAAKVIET KSEEELEDYM VEIDILASCN HQYIVKLLDA FFFDNKLSIM IEFCPGGAVD
     AIMLELDRGL QEPQIRVICK QMLEALQYLH SMKIIHRDLK AGNILLTLDG DIKLADFGVS
     AKNTKTLQRR DSFIGTPYWM APEVVMCETM KDAPYDYKAD IWSLGITLIE LAQIEPPHHE
     LNPMRVLLKI AKSEPPGLDQ PSKWSMDFND FLKKALDRHP ETRPTAAQLL EHPFVSSVNT
     NRPLRELVAE AKAEVMEEIE DNHEDGEDED PADLTPVQAP TKDPSQTSAT SLNGDHPHGT
     CYAETSMEIE EEPSTLESTK TPLKEQEDNL SDKFQVEDHD KPESEASGKA SSSDSGIEDG
     KSTPTSEEDT KTVEASEPEL PVQRTPTPAE EPEYPSETME KYLEKPKEPE KEDHCEETQP
     VLKRIQLKDP NGRMSVVSNR SSFAGDDAES LVSHTNGRLS NRYSDVASDS MDISLNLSGD
     LSVNKEMGTI SLRDSKKTLK RTRRFLVDGV EVSVTTSKII TDDEKKDEEM RFLRRQELRD
     LRLLQKEQHR SLTVLNMKLK EQREQMHRRF DQEMNAKKKY YYTELEALEK HQKQTIERME
     TEHSNSLREE GKRIRVEQEK AYQKFLDQMK QKKKEVKQEV EKMPRNQRKD TMKMKMNNYQ
     QMRSDEEQKF IADQKEYLDV TLKSIISKNK HEISETERQC LLKKQNLVRE REATLWDMEE
     KNLHERHQLH KQQLKDQYFL QRHQLLKKHE KEQEQMLHYN LRMVELLKAR QQQERNRLPK
     IQRNEAKTRM VMFKKSLKIN SSGSAAEDRE KVKQFSRMEE KRQKAERLHQ QQKHENQMRE
     MLSQCDGNTR ELQQLQNEKC HLLIENETQR LKSLDEQHNQ QLKEWREHLK PRKKVLEDEL
     TLRKRAGAFL QDDG