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RAC-gamma serine/threonine-protein kinase (EC 2.7.11.1) (Protein kinase Akt-3) (Protein kinase B gamma) (PKB gamma) (RAC-PK-gamma)

 AKT3_RAT                Reviewed;         479 AA.
Q63484;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
05-DEC-2018, entry version 151.
RecName: Full=RAC-gamma serine/threonine-protein kinase;
EC=2.7.11.1;
AltName: Full=Protein kinase Akt-3;
AltName: Full=Protein kinase B gamma;
Short=PKB gamma;
AltName: Full=RAC-PK-gamma;
Name=Akt3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-454.
TISSUE=Brain;
PubMed=7488143; DOI=10.1006/bbrc.1995.2654;
Konishi H., Kuroda S., Tanaka M., Matsuzaki H., Ono Y., Kameyama K.,
Haga T., Kikkawa U.;
"Molecular cloning and characterization of a new member of the RAC
protein kinase family: association of the pleckstrin homology domain
of three types of RAC protein kinase with protein kinase C subspecies
and beta gamma subunits of G proteins.";
Biochem. Biophys. Res. Commun. 216:526-534(1995).
-!- FUNCTION: AKT3 is one of 3 closely related serine/threonine-
protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and
which regulate many processes including metabolism, proliferation,
cell survival, growth and angiogenesis. This is mediated through
serine and/or threonine phosphorylation of a range of downstream
substrates. Over 100 substrate candidates have been reported so
far, but for most of them, no isoform specificity has been
reported. AKT3 is the least studied AKT isoform. It plays an
important role in brain development and is crucial for the
viability of malignant glioma cells. AKT3 isoform may also be the
key molecule in up-regulation and down-regulation of MMP13 via
IL13. Required for the coordination of mitochondrial biogenesis
with growth factor-induced increases in cellular energy demands.
Down-regulation by RNA interference reduces the expression of the
phosphorylated form of BAD, resulting in the induction of caspase-
dependent apoptosis (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain
(Thr-305) and the other in the C-terminal regulatory region (Ser-
472), need to be phosphorylated for its full activation. IGF-1
leads to the activation of AKT3, which may play a role in
regulating cell survival. {ECO:0000250}.
-!- SUBUNIT: Interacts (via PH domain) with TCL1A; this enhances AKT3
phosphorylation and activation. Interacts with TRAF6 (By
similarity). Interacts with KCTD20 (By similarity). Interacts with
BTBD10 (By similarity). {ECO:0000250|UniProtKB:Q9WUA6}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Note=Membrane-associated after cell stimulation
leading to its translocation. {ECO:0000250}.
-!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-
kinase alpha (PI(3)K) results in its targeting to the plasma
membrane.
-!- PTM: Phosphorylation on Thr-305 and Ser-472 is required for full
activity.
-!- PTM: Ubiquitinated. When fully phosphorylated and translocated
into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed
by TTC3, leading to its degradation by the proteasome (By
similarity). {ECO:0000250}.
-!- PTM: O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating
phosphorylation at Thr-305 via disrupting the interaction between
AKT and PDK1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
-!- CAUTION: In light of strong homologies in the primary amino acid
sequence, the 3 AKT kinases were long surmised to play redundant
and overlapping roles. More recent studies has brought into
question the redundancy within AKT kinase isoforms and instead
pointed to isoform specific functions in different cellular events
and diseases. AKT1 is more specifically involved in cellular
survival pathways, by inhibiting apoptotic processes; whereas AKT2
is more specific for the insulin receptor signaling pathway.
Moreover, while AKT1 and AKT2 are often implicated in many aspects
of cellular transformation, the 2 isoforms act in a complementary
opposing manner. The role of AKT3 is less clear, though it appears
to be predominantly expressed in brain. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AABR03086280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D49836; BAA08637.1; -; mRNA.
PIR; JC4345; JC4345.
RefSeq; NP_113763.1; NM_031575.1.
UniGene; Rn.10506; -.
ProteinModelPortal; Q63484; -.
SMR; Q63484; -.
STRING; 10116.ENSRNOP00000054688; -.
iPTMnet; Q63484; -.
PhosphoSitePlus; Q63484; -.
PaxDb; Q63484; -.
PRIDE; Q63484; -.
GeneID; 29414; -.
KEGG; rno:29414; -.
UCSC; RGD:62390; rat.
CTD; 10000; -.
RGD; 62390; Akt3.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOVERGEN; HBG108317; -.
InParanoid; Q63484; -.
KO; K04456; -.
PhylomeDB; Q63484; -.
BRENDA; 2.7.11.1; 5301.
PRO; PR:Q63484; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
CDD; cd01241; PH_PKB; 1.
CDD; cd05593; STKc_PKB_gamma; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034675; Akt3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR039026; PH_PKB.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR039029; RAC_gamma-like.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24356:SF190; PTHR24356:SF190; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00233; PH; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Disulfide bond; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9Y243}.
CHAIN 2 479 RAC-gamma serine/threonine-protein
kinase.
/FTId=PRO_0000085613.
DOMAIN 5 107 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 148 405 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 406 479 AGC-kinase C-terminal.
NP_BIND 154 162 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 452 455 Poly-Asp.
ACT_SITE 271 271 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 177 177 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q9Y243}.
MOD_RES 305 305 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:Q9Y243}.
MOD_RES 447 447 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y243}.
MOD_RES 472 472 Phosphoserine; by PKC/PRKCZ.
{ECO:0000250|UniProtKB:Q9Y243}.
CARBOHYD 302 302 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 309 309 O-linked (GlcNAc) threonine.
{ECO:0000250}.
DISULFID 59 76 {ECO:0000250}.
DISULFID 293 307 {ECO:0000250}.
CONFLICT 452 454 DDD -> CPL (in Ref. 2; BAA08637).
{ECO:0000305}.
SEQUENCE 479 AA; 55796 MW; D75D83A027B1A6B9 CRC64;
MSDVTIVKED WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ
LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS
PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK
KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE
RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA
ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM
EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDPKEIM RHSFFSGVNW QDVYDKKLVP
PFKPQVTSET DTRYFDEEFT AQTITITPPE KDDDDGMDCM DNERRPHFPQ FSYSASGRE


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