SGK1A_XENLA
ID SGK1A_XENLA Reviewed; 434 AA.
AC Q6GPN6; O93524;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Serine/threonine-protein kinase Sgk1-A;
DE EC=2.7.11.1;
DE AltName: Full=Serum/glucocorticoid-regulated kinase 1-A;
GN Name=sgk1-a; Synonyms=sgk-a;
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], FUNCTION, AND INDUCTION.
RC TISSUE=Kidney distal tubule;
RX PubMed=10051674; DOI=10.1073/pnas.96.5.2514;
RA Chen S.-Y., Bhargava A., Mastroberardino L., Meijer O.C., Wang J., Buse P.,
RA Firestone G.L., Verrey F., Pearce D.;
RT "Epithelial sodium channel regulated by aldosterone-induced protein sgk.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2514-2519(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 (By similarity). Plays an important role in activating
CC certain potassium, sodium, and chloride channels, suggesting an
CC involvement in the regulation of processes such as cell survival,
CC neuronal excitability, and renal sodium excretion. {ECO:0000250,
CC ECO:0000269|PubMed:10051674}.
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 -!- INDUCTION: Up-regulated by aldosterone and glucocorticoids.
CC {ECO:0000269|PubMed:10051674}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF057138; AAC62398.1; -; mRNA.
DR EMBL; BC073077; AAH73077.1; -; mRNA.
DR RefSeq; NP_001083809.1; NM_001090340.1.
DR AlphaFoldDB; Q6GPN6; -.
DR SMR; Q6GPN6; -.
DR BioGRID; 100455; 1.
DR DNASU; 399130; -.
DR GeneID; 399130; -.
DR KEGG; xla:399130; -.
DR CTD; 399130; -.
DR Xenbase; XB-GENE-1003523; sgk1.L.
DR OrthoDB; 614710at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 399130; Expressed in camera-type eye and 18 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-A"
FT /id="PRO_0000380133"
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 66..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..94
FT /note="Polar residues"
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"
FT CONFLICT 122
FT /note="A -> S (in Ref. 1; AAC62398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 49114 MW; 1A62C43C621A0F6B CRC64;
MTVKTETAAG ASTLTYSKMR GMVALLIAFM KQRRMGLNDF IQKIATNSSY ACKPSEVQSI
LNISPPQEPE LLNENSSPPP SPSQQINLGP SSNPHAKPSD FQFLKIIGKG SFGKVLLARH
QADEKFYAVK VLQKKAILKK KEEKHIMSER NVLLKNVKHP FLVGLHFSFQ TTSRLYFILD
YINGGELFYH LQRERCFLEP RARFYAAEIA SALGYLHSLN IVYRDLKPEN ILLDSQGHIV
LTDFGLCKEN IEPNGTTSTF CGTPEYLAPE VLHKQPYDRT VDWWCLGAVL YEMLYGLPPF
YSRNTAEMYD NILNKPLQLK PNITNSARNL LEGLLQKDRT KRIGAKNDFM EIKNHIFFSP
INWDDLINKK ITPPFNPNVS GPSDLQHFDP EFTEEPVPNS IGQSPDSILI TASIKEAAEA
FMGFSYAPPM ESYL
