SGK1_CAEBR
ID SGK1_CAEBR Reviewed; 464 AA.
AC A8XNJ6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Serine/threonine-protein kinase sgk-1 {ECO:0000250|UniProtKB:Q2PJ68};
DE EC=2.7.11.1;
DE AltName: Full=Serum- and glucocorticoid-inducible kinase homolog {ECO:0000250|UniProtKB:Q2PJ68};
DE AltName: Full=Serum/glucocorticoid-regulated kinase 1 {ECO:0000250|UniProtKB:O00141};
GN Name=sgk-1 {ECO:0000312|WormBase:CBG16386};
GN ORFNames=CBG16386 {ECO:0000312|WormBase:CBG16386};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Acts downstream of PI3 kinase age-1 and kinase pdk-1 in the
CC daf-2/insulin receptor-like transduction pathway (By similarity).
CC Essential role in regulating development, stress response, and
CC longevity (By similarity). Phosphorylates Forkhead-related daf-16 and
CC the longevity-promoting skn-1 transcription factors, which inhibits
CC their entry into the nucleus and antagonizes their function (By
CC similarity). Plays a role in the intracellular trafficking of proteins
CC such as mig-14 to the cell membrane, and this may be through positively
CC regulating ceramide synthesis (By similarity). Acts downstream of rict-
CC 1 to regulate fat storage, size, and development (By similarity).
CC Downstream of age-1 and together with akt-1/2, promotes cell survival
CC during embryonic development (By similarity). Does not appear to play a
CC role in immune function (By similarity).
CC {ECO:0000250|UniProtKB:Q2PJ68}.
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 Evidence={ECO:0000250|UniProtKB:Q2PJ68};
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; Evidence={ECO:0000250|UniProtKB:Q2PJ68};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q2PJ68};
CC -!- ACTIVITY REGULATION: Phosphorylated and activated by pdk-1.
CC {ECO:0000250|UniProtKB:Q2PJ68}.
CC -!- SUBUNIT: Interacts with pdk-1, akt-1, akt-2 and daf-16. Part of a
CC complex containing sgk-1, akt-1 and akt-2. Interacts with let-92
CC phosphatase regulatory subunit pptr-1. {ECO:0000250|UniProtKB:Q2PJ68}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q2PJ68}. Nucleus
CC {ECO:0000250|UniProtKB:Q2PJ68}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q2PJ68}. Note=Localized both in the cytoplasm
CC and in the nucleus in neurons, exclusively cytoplasmic in the
CC intestine. Localizes to the apical cell membrane and diffusely
CC throughout the cytoplasm in intestinal cells (By similarity).
CC {ECO:0000250|UniProtKB:Q2PJ68}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE600961; CAP34085.3; -; Genomic_DNA.
DR AlphaFoldDB; A8XNJ6; -.
DR SMR; A8XNJ6; -.
DR STRING; 6238.CBG16386; -.
DR PRIDE; A8XNJ6; -.
DR WormBase; CBG16386; CBP40619; WBGene00036341; Cbr-sgk-1.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_63_48_1; -.
DR InParanoid; A8XNJ6; -.
DR OMA; HFSFQNK; -.
DR OrthoDB; 614710at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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:0035556; P:intracellular signal transduction; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Developmental protein; Kinase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT CHAIN 1..464
FT /note="Serine/threonine-protein kinase sgk-1"
FT /id="PRO_0000396516"
FT DOMAIN 136..393
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 394..464
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 142..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 464 AA; 54252 MW; 16854FBD790BC2DE CRC64;
MGSLYYSGSR MVRKDEVSCK LVMGDDKKTV VYAVRIGDGP IMQKVYEEYE KFFLTDVKDM
VPEKFTIFPK KKLLQSKKTF FEKRRLWIQD VCQHLVDNQT KSEDVCRFFH IEAPDDDDNT
VDLGPSERKT ATANDFDFLT TIGKGSFGRV YQVRHKETKK IYAMKVLSKE HIRKKNEVKH
VMAERNVLIN NFKHPFLVSL HFSFQNKEKL YFVLDHLNGG ELFSHLQREK HFTESRSRFY
AAEIACALGY LHEKNIIYRD LKPENLLLDD KGYLVLTDFG LCKEDMQGSK TTSTFCGTPE
YLAPEIILKK PYDKTVDWWC LGSVLYEMIF GLPPFYSKDH NEMYDKIINQ PLRLKHTISV
PCTELITGLL QKDRSKRLGH KNDFRDIQDH PFFLPVDWDK LLNRELKAPF IPKVKNAMDI
SNISKEFVEI QIDPASLAPQ QLAVTHRDHD FENFTFVDTN RVLV
