Reviewed, UniProtKB/Swiss-Prot Q63484 (AKT3_RAT)

Names and origin

Protein names

Recommended name:
    RAC-gamma serine/threonine-protein kinase
    EC=2.7.11.1
Alternative name(s):
    RAC-PK-gamma
    Protein kinase Akt-3
    Protein kinase B, gamma
      Short name=PKB gamma

Gene names

Name:

Akt3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme 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 By similarity.
Subunit structure	Interacts (via PH domain) with TCL1A; this enhances AKT3 phosphorylation and activation By similarity.
Domain	Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI3K) results in its targeting to the plasma membrane.
Post-translational modification	Phosphorylation on Thr-305 and Ser-472 is required for full activity. Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 PH domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cellular response to insulin stimulus Inferred from mutant phenotype. Source: MGI positive regulation of sodium ion transport Inferred from mutant phenotype. Source: MGI protein amino acid phosphorylation Inferred from direct assay. Source: RGD
Cellular component	cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome soluble fraction Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from direct assay. Source: RGD protein kinase C binding Ref.2 Inferred from direct assay. Source: RGD protein serine/threonine kinase activity Ref.2 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	RAC-gamma serine/threonine-protein kinase		PRO_0000085613
Regions
	Domain	5 – 107	103	PH
	Domain	148 – 405	258	Protein kinase
	Domain	406 – 479	74	AGC-kinase C-terminal
	Nucleotide binding	154 – 162	9	ATP By similarity
	Compositional bias	452 – 455	4	Poly-Asp
Sites
	Active site	271	1	Proton acceptor By similarity
	Binding site	177	1	ATP By similarity
Amino acid modifications
	Modified residue	120	1	Phosphoserine By similarity
	Modified residue	123	1	Phosphoserine By similarity
	Modified residue	305	1	Phosphothreonine; by PDPK1 By similarity
	Modified residue	472	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	452 – 454	3	DDD → CPL in BAA08637. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q63484-1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: D75D83A027B1A6B9	FASTA	479	55,796
	10 20 30 40 50 60 MSDVTIVKED WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ 70 80 90 100 110 120 LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS 130 140 150 160 170 180 PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK 190 200 210 220 230 240 KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE 250 260 270 280 290 300 RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA 310 320 330 340 350 360 ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM 370 380 390 400 410 420 EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDPKEIM RHSFFSGVNW QDVYDKKLVP 430 440 450 460 470 PFKPQVTSET DTRYFDEEFT AQTITITPPE KDDDDGMDCM DNERRPHFPQ FSYSASGRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." 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. Nature 428:493-521(2004) [PubMed: 15057822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"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." Konishi H., Kuroda S., Tanaka M., Matsuzaki H., Ono Y., Kameyama K., Haga T., Kikkawa U. Biochem. Biophys. Res. Commun. 216:526-534(1995) [PubMed: 7488143] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-454. Tissue: Brain.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABR03086280 Genomic DNA. No translation available. D49836 mRNA. Translation: BAA08637.1.
IPI	IPI00209156.
PIR	JC4345.
RefSeq	NP_113763.1.
UniGene	Rn.10506
3D structure databases
HSSP	HSSP built from PDB template 1GZK based on UniProtKB P31751.
SMR	Q63484. Positions 1-115.
ModBase	Search...
PTM databases
PhosphoSite	Q63484.
Genome annotation databases
GeneID	29414.
KEGG	rno:29414.
Organism-specific databases
RGD	62390. Akt3.
Phylogenomic databases
HOVERGEN	Q63484.
Enzyme and pathway databases
BRENDA	2.7.11.1. 248.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR017892. Pkinase_C. IPR001849. Pleckstrin_homology. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. IPR015744. Serine/threonine_Kinase_Rac. [Graphical view]
PANTHER	PTHR22985:SF69. Akt. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00233. PH. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	609088.

Entry information

Entry name

AKT3_RAT

Accession

Primary (citable) accession number: Q63484

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 28, 2006
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)