SGK1_DANRE
ID SGK1_DANRE Reviewed; 433 AA.
AC Q7ZTW4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine/threonine-protein kinase Sgk1;
DE EC=2.7.11.1;
DE AltName: Full=Serum/glucocorticoid-regulated kinase 1;
GN Name=sgk1; Synonyms=sgk; ORFNames=wu:fc20a09;
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 [MRNA].
RA Nishikawa R., Carr J., Smith V., West W., Haluska D., Marass P.,
RA Marquis H., Stanton B.A., Sato J.D.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein kinase that may play an important role in cellular
CC stress response. May be involved in the regulation of processes such as
CC cell survival, neuronal excitability and renal sodium excretion (By
CC 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; EF512629; ABO88209.1; -; mRNA.
DR EMBL; BC052134; AAH52134.1; -; mRNA.
DR EMBL; BC067618; AAH67618.1; -; mRNA.
DR RefSeq; NP_954682.1; NM_199212.1.
DR AlphaFoldDB; Q7ZTW4; -.
DR SMR; Q7ZTW4; -.
DR STRING; 7955.ENSDARP00000031762; -.
DR PaxDb; Q7ZTW4; -.
DR Ensembl; ENSDART00000035031; ENSDARP00000031762; ENSDARG00000025522.
DR Ensembl; ENSDART00000193557; ENSDARP00000155076; ENSDARG00000115600.
DR GeneID; 324140; -.
DR KEGG; dre:324140; -.
DR CTD; 6446; -.
DR ZFIN; ZDB-GENE-030131-2860; sgk1.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000164496; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q7ZTW4; -.
DR OMA; HICITDF; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q7ZTW4; -.
DR TreeFam; TF320906; -.
DR Reactome; R-DRE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-DRE-9031628; NGF-stimulated transcription.
DR PRO; PR:Q7ZTW4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000025522; Expressed in granulocyte and 26 other tissues.
DR ExpressionAtlas; Q7ZTW4; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IMP:ZFIN.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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..433
FT /note="Serine/threonine-protein kinase Sgk1"
FT /id="PRO_0000380131"
FT DOMAIN 100..357
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 358..433
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 66..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 106..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 433 AA; 48983 MW; F2AA4771E245FF56 CRC64;
MTIQTETSVS APDLTYSKTR GLVANLSAFM KQRKMGLNDF IQKLSANSYA CKHPEVQSIL
NLTPPQDVEL MNSNPSPPPS PSQQINLGPS SNPTAKPSDF DFLKVIGKGS FGKVLLARHR
SDEKFYAVKV LQKKAILKKK EEKHIMSERN VLLKNVKHPF LVGLHYSFQT TDKLYFVLDY
INGGELFYHL QRERCFLEPR ARFYAAEIAS ALGYLHSLNI VYRDLKPENI LLDSQGHIIL
TDFGLCKENI EPNGTTSTFC GTPEYLAPEV LHKQPYDRTV DWWCLGAVLY EMLYGLPPFY
SRNTAEMYDN ILNKPLQLKP NISNAARHLL EGLLQKDRTK RLGFTDDFTE IKNHMFFSPI
NWDDLNAKKL TPPFNPNVTG PNDLRHFDPE FTDEPVPNSI GCSPDSALVT SSITEATEAF
LGFSYAPAMD SYL
