ID   ST17A_RABIT             Reviewed;         397 AA.
AC   Q9GM70;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Serine/threonine-protein kinase 17A;
DE            EC=2.7.11.1;
DE   AltName: Full=DAP kinase-related apoptosis-inducing protein kinase 1;
DE            Short=rDRAK1;
GN   Name=STK17A; Synonyms=DRAK1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Osteoclast;
RX   PubMed=11279167; DOI=10.1074/jbc.m101023200;
RA   Kojima H., Nemoto A., Uemura T., Honma R., Ogura M., Liu Y.-K.;
RT   "rDRAK1, a novel kinase related to apoptosis, is strongly expressed in
RT   active osteoclasts and induces apoptosis.";
RL   J. Biol. Chem. 276:19238-19243(2001).
CC   -!- FUNCTION: Acts as a positive regulator of apoptosis. May also act as a
CC       regulator of cellular reactive oxygen species.
CC       {ECO:0000269|PubMed:11279167}.
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   -!- ACTIVITY REGULATION: Inhibited by thiazolidinedione-type compounds:
CC       inhibited by furan- and pyridone- thiazolidinediones. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11279167}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in bone marrow. Lower levels in
CC       brain, heart, lung, liver and kidney. {ECO:0000269|PubMed:11279167}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. DAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; AB042195; BAB16111.1; -; mRNA.
DR   RefSeq; NP_001075475.1; NM_001082006.1.
DR   AlphaFoldDB; Q9GM70; -.
DR   SMR; Q9GM70; -.
DR   GeneID; 100008622; -.
DR   KEGG; ocu:100008622; -.
DR   CTD; 9263; -.
DR   InParanoid; Q9GM70; -.
DR   BRENDA; 2.7.11.1; 1749.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR   CDD; cd14197; STKc_DRAK1; 1.
DR   InterPro; IPR042704; DRAK1_STKc.
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   Pfam; PF00069; Pkinase; 1.
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   Apoptosis; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..397
FT                   /note="Serine/threonine-protein kinase 17A"
FT                   /id="PRO_0000086705"
FT   DOMAIN          44..304
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         50..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UEE5"
SQ   SEQUENCE   397 AA;  44463 MW;  589041E107F50097 CRC64;
     MIPLEKPGSG GSPSAAASGS GPGGLLTEIR TAIRTEPFQD CYSLSPGREL GRGKFAVVRK
     CIQKDSGKEF AAKFMRKRRK GQDCRMEIIH EIAVLELAQD NPWVINLHEV YETSSEMILV
     LEYAAGGEIS DQCVADRDEA FNEKDVQRLM RQILEGVHFL HTHDVVHLDL KPQNILLTSE
     SPLGDIKIVD FGLSRIVKNS EELREIMGTP EYVAPEILSY DPISMATDMW SIGVLTYVML
     TGISPFLGDN KQETFLNISQ MNLSYSEEEF DTVSESAVDF IKKLLVKKPE DRATAEECLK
     HPWLTQSSIQ DPVLRVKEAL EEANALQKGD SVPEISSATE KPGTEESIVT EELIVVTSYT
     LGQCRQSEKE KMEQKAISKR FKFEEPLLQE IPGEFIY