ID   SGK1B_XENLA             Reviewed;         434 AA.
AC   Q6GLY8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Serine/threonine-protein kinase Sgk1-B;
DE            EC=2.7.11.1;
DE   AltName: Full=Serum/glucocorticoid-regulated kinase 1-B;
GN   Name=sgk1-b; Synonyms=sgk-b;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein kinase that may play an important role in cellular
CC       stress response. Plays an important role in activating certain
CC       potassium, sodium, and chloride channels, suggesting an involvement in
CC       the regulation of processes such as cell survival, neuronal
CC       excitability and renal sodium excretion (By similarity). {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; BC074305; AAH74305.1; -; mRNA.
DR   RefSeq; NP_001086189.1; NM_001092720.1.
DR   AlphaFoldDB; Q6GLY8; -.
DR   SMR; Q6GLY8; -.
DR   DNASU; 444618; -.
DR   GeneID; 444618; -.
DR   KEGG; xla:444618; -.
DR   CTD; 444618; -.
DR   Xenbase; XB-GENE-6254615; sgk1.S.
DR   OMA; HICITDF; -.
DR   OrthoDB; 614710at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 444618; Expressed in camera-type eye and 19 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
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   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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; Cytoplasm; Endoplasmic reticulum; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Stress response; Transferase.
FT   CHAIN           1..434
FT                   /note="Serine/threonine-protein kinase Sgk1-B"
FT                   /id="PRO_0000380134"
FT   DOMAIN          101..358
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          359..434
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          68..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        225
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         107..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   434 AA;  49100 MW;  7842E9103A32395B CRC64;
     MTVKTETAAG ASTLTYSKMR GMVALLIAFM KQRRMGLNEF IQKIATNSSY SCKPSEVQSI
     LNISPPQESE LLNENSSPPP SHSQQINLGP SSNPHAKPSD FQFLKIIGKG SFGKVLLARH
     KADEKFYAVK VLQKKAILKK KEEKHIMSER NVLLKNVKHP FLVGLHFSIQ TTSRLYFILD
     YINGGELFYH LQRERCFLEP RARFYAAEIA SALGYLHSLN IVYRDLKPEN ILLDSQGHIV
     LTDFGLCKEN IEPNGITSTF CGTPEYLAPE VLHKQPYDRT VDWWCLGAVL YEMLYGLPPF
     YSRNTAEMYD NILNKPLQLK PNITNSARNL LEGLLQKDRT KRTGAKTDFM EIKNHIFFSP
     IDWDDLINKK ITPPFNPNVS GPSDLQHFDP EFTDEPVPNS IGQSPDSILI TASIKEAAEA
     FMGFSYAPPM DSYL