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Serine/threonine-protein kinase Sgk3 (EC 2.7.11.1) (Cytokine-independent survival kinase) (Serum/glucocorticoid-regulated kinase 3) (Serum/glucocorticoid-regulated kinase-like)

 SGK3_MOUSE              Reviewed;         496 AA.
Q9ERE3; Q3UAY2;
22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-JUN-2018, entry version 157.
RecName: Full=Serine/threonine-protein kinase Sgk3;
EC=2.7.11.1;
AltName: Full=Cytokine-independent survival kinase;
AltName: Full=Serum/glucocorticoid-regulated kinase 3;
AltName: Full=Serum/glucocorticoid-regulated kinase-like;
Name=Sgk3; Synonyms=Cisk, Sgkl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF LYS-191.
PubMed=11050396; DOI=10.1016/S0960-9822(00)00733-8;
Liu D., Yang X., Songyang Z.;
"Identification of CISK, a new member of the SGK kinase family that
promotes IL-3-dependent survival.";
Curr. Biol. 10:1233-1236(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Amnion, Bone marrow, Forelimb, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
CHARACTERIZATION, AND MUTAGENESIS OF ARG-90.
PubMed=11514587; DOI=10.1083/jcb.200105089;
Xu J., Liu D., Gill G., Songyang Z.;
"Regulation of cytokine-independent survival kinase (CISK) by the Phox
homology domain and phosphoinositides.";
J. Cell Biol. 154:699-705(2001).
[4]
FUNCTION IN THE REGULATION OF GRIA1/GLUR1.
PubMed=15774536; DOI=10.1113/jphysiol.2004.079582;
Strutz-Seebohm N., Seebohm G., Mack A.F., Wagner H.J., Just L.,
Skutella T., Lang U.E., Henke G., Striegel M., Hollmann M., Rouach N.,
Nicoll R.A., McCormick J.A., Wang J., Pearce D., Lang F.;
"Regulation of GluR1 abundance in murine hippocampal neurones by
serum- and glucocorticoid-inducible kinase 3.";
J. Physiol. (Lond.) 565:381-390(2005).
[5]
FUNCTION IN THE REGULATION OF GRIK2/GLUR6.
PubMed=15774535; DOI=10.1113/jphysiol.2004.079624;
Strutz-Seebohm N., Seebohm G., Shumilina E., Mack A.F., Wagner H.J.,
Lampert A., Grahammer F., Henke G., Just L., Skutella T., Hollmann M.,
Lang F.;
"Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase
isoforms in the regulation of GluR6 expression.";
J. Physiol. (Lond.) 565:391-401(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-129, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION.
PubMed=21113728; DOI=10.1007/s00535-010-0348-8;
Pasham V., Rotte A., Bhandaru M., Eichenmueller M., Froehlich H.,
Mack A.F., Bobbala D., Yang W., Pearce D., Lang F.;
"Regulation of gastric acid secretion by the serum and glucocorticoid
inducible kinase isoform SGK3.";
J. Gastroenterol. 46:305-317(2011).
[9]
FUNCTION.
PubMed=21451460; DOI=10.1038/ki.2011.67;
Bhandaru M., Kempe D.S., Rotte A., Capuano P., Pathare G., Sopjani M.,
Alesutan I., Tyan L., Huang D.Y., Siraskar B., Judenhofer M.S.,
Stange G., Pichler B.J., Biber J., Quintanilla-Martinez L.,
Wagner C.A., Pearce D., Foeller M., Lang F.;
"Decreased bone density and increased phosphaturia in gene-targeted
mice lacking functional serum- and glucocorticoid-inducible kinase
3.";
Kidney Int. 80:61-67(2011).
[10]
FUNCTION IN THE REGULATION OF SLC9A3/NHE3, AND SUBCELLULAR LOCATION.
PubMed=21865597; DOI=10.1091/mbc.E11-04-0328;
He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G.,
Naray-Fejes-Toth A., Yun C.C.;
"Serum- and glucocorticoid-induced kinase 3 in recycling endosomes
mediates acute activation of Na+/H+ exchanger NHE3 by
glucocorticoids.";
Mol. Biol. Cell 22:3812-3825(2011).
-!- FUNCTION: Serine/threonine-protein kinase which is involved in the
regulation of a wide variety of ion channels, membrane
transporters, cell growth, proliferation, survival and migration.
Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels:
KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+)
channels: TRPV5 and TRPV6, chloride channel: BSND, creatine
transporter: SLC6A8, Na(+)/dicarboxylate cotransporter:
SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter:
SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and
SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and
SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6,
Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase.
Plays a role in the regulation of renal tubular phosphate
transport and bone density. Phosphorylates NEDD4L and GSK3B.
Positively regulates ER transcription activity through
phosphorylation of FLII. Negatively regulates the function of
ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from
being efficiently sorted to lysosomes.
{ECO:0000269|PubMed:15774535, ECO:0000269|PubMed:15774536,
ECO:0000269|PubMed:21113728, ECO:0000269|PubMed:21451460,
ECO:0000269|PubMed:21865597}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Two specific sites, one in the kinase domain
(Thr-320) and the other in the C-terminal regulatory region (Ser-
486), need to be phosphorylated for its full activation.
-!- SUBUNIT: Interacts with GSK3B and FLII. Interacts with PDPK1 in a
phosphorylation-dependent manner. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
{ECO:0000269|PubMed:21865597}. Early endosome
{ECO:0000269|PubMed:21865597}. Recycling endosome {ECO:0000250}.
Note=Endosomal localization is a prerequisite for complete kinase
activity. It is essential for its colocalization with the kinase
responsible for phosphorylating Ser-486 thus allowing PDPK1
phosphorylation of Thr-320 resulting in complete activation of
SGK3. Colocalizes with SLC9A3/NHE3 in the recycling endosomes (By
similarity). Localized in vesicle-like structures and in the early
endosome. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed, predominantly in the heart,
spleen and 7-day embryo.
-!- PTM: Activated by phosphorylation on Ser-486 by an unknown kinase
(may be mTORC2 but not confirmed), transforming it into a
substrate for PDPK1 which then phosphorylates it on Thr-320.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF312007; AAG34115.1; -; mRNA.
EMBL; AK030314; BAC26895.1; -; mRNA.
EMBL; AK031133; BAC27269.1; -; mRNA.
EMBL; AK031328; BAC27349.1; -; mRNA.
EMBL; AK146561; BAE27261.1; -; mRNA.
EMBL; AK151181; BAE30182.1; -; mRNA.
EMBL; AK171120; BAE42262.1; -; mRNA.
EMBL; AK171186; BAE42298.1; -; mRNA.
EMBL; AK171959; BAE42748.1; -; mRNA.
EMBL; AK172323; BAE42945.1; -; mRNA.
CCDS; CCDS14816.1; -.
RefSeq; NP_001032848.1; NM_001037759.1.
RefSeq; NP_573483.1; NM_133220.2.
RefSeq; NP_808215.2; NM_177547.3.
UniGene; Mm.336410; -.
PDB; 1XTE; X-ray; 1.60 A; A=7-160.
PDB; 1XTN; X-ray; 2.20 A; A/B=7-126.
PDBsum; 1XTE; -.
PDBsum; 1XTN; -.
ProteinModelPortal; Q9ERE3; -.
SMR; Q9ERE3; -.
BioGrid; 228417; 1.
CORUM; Q9ERE3; -.
ELM; Q9ERE3; -.
STRING; 10090.ENSMUSP00000095437; -.
iPTMnet; Q9ERE3; -.
PhosphoSitePlus; Q9ERE3; -.
EPD; Q9ERE3; -.
MaxQB; Q9ERE3; -.
PaxDb; Q9ERE3; -.
PRIDE; Q9ERE3; -.
Ensembl; ENSMUST00000097826; ENSMUSP00000095437; ENSMUSG00000025915.
Ensembl; ENSMUST00000166384; ENSMUSP00000130078; ENSMUSG00000025915.
Ensembl; ENSMUST00000168907; ENSMUSP00000126861; ENSMUSG00000025915.
Ensembl; ENSMUST00000171265; ENSMUSP00000127462; ENSMUSG00000025915.
GeneID; 170755; -.
KEGG; mmu:170755; -.
UCSC; uc007agu.1; mouse.
CTD; 23678; -.
MGI; MGI:2182368; Sgk3.
eggNOG; KOG0598; Eukaryota.
eggNOG; KOG2101; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00920000148938; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; Q9ERE3; -.
KO; K13304; -.
OMA; FTEEMVP; -.
OrthoDB; EOG091G06FF; -.
PhylomeDB; Q9ERE3; -.
TreeFam; TF320906; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
EvolutionaryTrace; Q9ERE3; -.
PRO; PR:Q9ERE3; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000025915; -.
CleanEx; MM_SGK3; -.
ExpressionAtlas; Q9ERE3; baseline and differential.
Genevisible; Q9ERE3; MM.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
GO; GO:0017081; F:chloride channel regulator activity; IBA:GO_Central.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0017080; F:sodium channel regulator activity; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0032411; P:positive regulation of transporter activity; IBA:GO_Central.
GO; GO:0001558; P:regulation of cell growth; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
CDD; cd06870; PX_CISK; 1.
CDD; cd05604; STKc_SGK3; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR037900; CISK_PX.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001683; Phox.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR037709; SGK3_dom.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
Pfam; PF00787; PX; 1.
SMART; SM00312; PX; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50195; PX; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasmic vesicle;
Endosome; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 496 Serine/threonine-protein kinase Sgk3.
/FTId=PRO_0000086650.
DOMAIN 12 124 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 162 419 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 420 496 AGC-kinase C-terminal.
NP_BIND 168 176 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 195 205 Nuclear localization signal.
{ECO:0000250}.
ACT_SITE 286 286 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 191 191 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 320 320 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:Q96BR1}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000250|UniProtKB:Q96BR1}.
MUTAGEN 90 90 R->A: Diminishes binding to
phosphoinositides.
{ECO:0000269|PubMed:11514587}.
MUTAGEN 191 191 K->A: No activity.
{ECO:0000269|PubMed:11050396}.
CONFLICT 114 114 R -> G (in Ref. 2; BAC27349).
{ECO:0000305}.
CONFLICT 204 204 Q -> P (in Ref. 2; BAC27349).
{ECO:0000305}.
STRAND 15 26 {ECO:0000244|PDB:1XTE}.
STRAND 29 40 {ECO:0000244|PDB:1XTE}.
STRAND 43 50 {ECO:0000244|PDB:1XTE}.
HELIX 51 64 {ECO:0000244|PDB:1XTE}.
HELIX 66 68 {ECO:0000244|PDB:1XTE}.
HELIX 84 101 {ECO:0000244|PDB:1XTE}.
HELIX 105 108 {ECO:0000244|PDB:1XTE}.
HELIX 111 116 {ECO:0000244|PDB:1XTE}.
TURN 117 120 {ECO:0000244|PDB:1XTE}.
HELIX 122 124 {ECO:0000244|PDB:1XTE}.
SEQUENCE 496 AA; 57145 MW; 4B7D2804A5948BAD CRC64;
MQRDCIMDYK ESCPSVSIPS SDEHREKKKR FTVYKVLVSV GRSEWFVFRR YAEFDKLYNS
LKKQFPAMAL KIPAKRIFGD NFDPDFIKQR RAGLNEFIQN LVRYPELYNH PDVRAFLQMD
SPRHQSDPSE DEDERSTSKP HSTSRNINLG PTGNPHAKPT DFDFLKVIGK GSFGKVLLAK
RKLDGKFYAV KVLQKKIVLN RKEQKHIMAE RNVLLKNVKH PFLVGLHYSF QTTEKLYFVL
DFVNGGELFF HLQRERSFPE PRARFYAAEI ASALGYLHSI KIVYRDLKPE NILLDSMGHV
VLTDFGLCKE GIAISDTTTT FCGTPEYLAP EVIRKQPYDN TVDWWCLGAV LYEMLYGLPP
FYCRDVAEMY DNILHKPLNL RPGVSLTAWS ILEELLEKNR QNRLGAKEDF LEIQNHPFFE
SLSWTDLVQK KIPPPFNPNV AGPDDIRNFD AVFTEETVPY SVCVSSDYSI VNASVLEADD
AFVGFSYAPP SEDLFL


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