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Database: UniProt
Entry: F7HWA9_CALJA
LinkDB: F7HWA9_CALJA
Original site: F7HWA9_CALJA 
ID   F7HWA9_CALJA            Unreviewed;       526 AA.
AC   F7HWA9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Serine/threonine-protein kinase Sgk1 {ECO:0000256|ARBA:ARBA00041082};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   AltName: Full=Serum/glucocorticoid-regulated kinase 1 {ECO:0000256|ARBA:ARBA00042467};
GN   Name=SGK1 {ECO:0000313|EMBL:JAB17667.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000005062.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000005062.1, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000005062.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB17667.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:JAB42587.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB32673.1}, and Hippocampus
RC   {ECO:0000313|EMBL:JAB17667.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000005062.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR   EMBL; GAMS01005469; JAB17667.1; -; mRNA.
DR   EMBL; GAMR01001259; JAB32673.1; -; mRNA.
DR   EMBL; GAMP01010168; JAB42587.1; -; mRNA.
DR   RefSeq; XP_002747028.1; XM_002746982.4.
DR   Ensembl; ENSCJAT00000005333.4; ENSCJAP00000005062.1; ENSCJAG00000002727.5.
DR   eggNOG; KOG0598; Eukaryota.
DR   GeneTree; ENSGT00940000155726; -.
DR   HOGENOM; CLU_000288_63_48_1; -.
DR   OMA; CWTDMSL; -.
DR   OrthoDB; 3028764at2759; -.
DR   TreeFam; TF320906; -.
DR   Proteomes; UP000008225; Chromosome 4.
DR   Bgee; ENSCJAG00000002727; Expressed in kidney and 6 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05575; STKc_SGK; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 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; IPR036871; PX_dom_sf.
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   SUPFAM; SSF64268; PX domain; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:JAB17667.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          193..450
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          451..526
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          161..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   526 AA;  59932 MW;  BBA5851EFF394854 CRC64;
     MVNKDMNGFP VKKCSAFQFF KKRVRRWIKS PMVSVDKHQS PSLKYTGPSM VHIPPGEPDF
     EPSLCQTCLG EHAFQRGVLP QEKESCSWET QSGCEVREPC NPANILTKPD PRTFWTNDDS
     AFMKQRRMGL NDFIQKIANN SYACKHPEVQ SILKISQPQE PELMNANPSP PPSPSQQINL
     GPSSNPHAKP SDFHFLKVIG KGSFGKVLLA RHKAEEVFYA VKVLQKKAIL KKKEEKHIMS
     ERNVLLKNVK HPFLVGLHFS FQTADKLYFV LDYINGGELF YHLQRERCFL EPRARFYAAE
     IASALGYLHS LNIVYRDLKP ENILLDSQGH IVLTDFGLCK ENIEHNSTTS TFCGTPEYLA
     PEVLHKQPYD RTVDWWCLGA VLYEMLYGLP PFYSRNTAEM YDNILNKPLQ LKPNITNSAR
     HLLESLLQKD RTKRLGAKDD FMEIKSHVFF SLINWDDLIN KKITPPFNPN VSGPNDLRHF
     DPEFTEEPVP NSIGKSPDSI LVTASVKEAA EAFLGFSYAP PTDSFL
//
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