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Database: UniProt
Entry: SGK1_CHICK
LinkDB: SGK1_CHICK
Original site: SGK1_CHICK 
ID   SGK1_CHICK              Reviewed;         432 AA.
AC   Q6U1I9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 126.
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;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Malkiewicz S.A., Porter T.E.;
RT   "Sgk is a glucocorticoid-induced gene in the chicken embryonic pituitary
RT   gland.";
RL   Submitted (SEP-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; AY380825; AAQ88435.1; -; mRNA.
DR   RefSeq; NP_989807.1; NM_204476.1.
DR   AlphaFoldDB; Q6U1I9; -.
DR   SMR; Q6U1I9; -.
DR   STRING; 9031.ENSGALP00000068769; -.
DR   PaxDb; 9031-ENSGALP00000031130; -.
DR   Ensembl; ENSGALT00000031766; ENSGALP00000031130; ENSGALG00000013971.
DR   Ensembl; ENSGALT00010015194.1; ENSGALP00010008927.1; ENSGALG00010006359.1.
DR   Ensembl; ENSGALT00015010227; ENSGALP00015005621; ENSGALG00015004366.
DR   GeneID; 395133; -.
DR   KEGG; gga:395133; -.
DR   CTD; 6446; -.
DR   VEuPathDB; HostDB:geneid_395133; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   GeneTree; ENSGT00940000155726; -.
DR   HOGENOM; CLU_000288_63_5_1; -.
DR   InParanoid; Q6U1I9; -.
DR   OrthoDB; 3028764at2759; -.
DR   PhylomeDB; Q6U1I9; -.
DR   TreeFam; TF320906; -.
DR   Reactome; R-GGA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-GGA-2672351; Stimuli-sensing channels.
DR   Reactome; R-GGA-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-GGA-9031628; NGF-stimulated transcription.
DR   PRO; PR:Q6U1I9; -.
DR   Proteomes; UP000000539; Chromosome 3.
DR   Bgee; ENSGALG00000013971; Expressed in lung and 13 other cell types or tissues.
DR   ExpressionAtlas; Q6U1I9; baseline and differential.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05575; STKc_SGK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF184; SERINE_THREONINE-PROTEIN KINASE SGK1; 1.
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; Protein kinase-like (PK-like); 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..432
FT                   /note="Serine/threonine-protein kinase Sgk1"
FT                   /id="PRO_0000380130"
FT   DOMAIN          99..356
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          357..432
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          67..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        223
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         105..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   432 AA;  48890 MW;  83AB52AFF2609953 CRC64;
     MTVKAAEASG PALTYSKMRG MVAILIAFMK QRRMGLNDFI QKIATNSYAC KHPEVQSILK
     ISQPQEPELM NANPSPPPSP SQQINLGPSS NPHAKPSDFH FLKVIGKGSF GKVLLARHKA
     EEQFYAVKVL QKKAILKKKE EKHIMSERNV LLKNVKHPFL VGLHFSFQTA DKLYFVLDYI
     NGGELFYHLQ RERCFLEPRA RFYAAEIASA LGYLHSLNIV YRDLKPENIL LDSQGHIVLT
     DFGLCKENIE HNGTTSTFCG TPEYLAPEVL HKQPYDRTVD WWCLGAVLYE MLYGLPPFYS
     RNTAEMYDNI LNKPLQLKPN ITNSARHLLE GLLQKDRTKR LGAKEDFTEI KNHIFFSPIN
     WDDLINKKIT PPFNPNVSGP SDLRHFDPEF TDEPVPNSIG QSPDSILITA SVKEAAEAFL
     GFSYAPPVDS FL
//
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