ID   AKT1_XENLA              Reviewed;         481 AA.
AC   Q98TY9;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-NOV-2008, entry version 51.
DE   RecName: Full=RAC-alpha serine/threonine-protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=RAC-PK-alpha;
DE   AltName: Full=Protein kinase Akt-1;
DE            Short=xAkt;
DE   AltName: Full=Protein kinase B, alpha;
DE            Short=PKB alpha;
GN   Name=akt1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Oocyte;
RX   PubMed=12374568; DOI=10.1042/BJ20021243;
RA   Andersen C.B., Sakaue H., Nedachi T., Kovacina K.S., Clayberger C.,
RA   Conti M., Roth R.A.;
RT   "Protein kinase B/Akt is essential for the insulin- but not
RT   progesterone-stimulated resumption of meiosis in Xenopus oocytes.";
RL   Biochem. J. 369:227-238(2003).
CC   -!- FUNCTION: General protein kinase capable of phosphorylating
CC       several known proteins. Signals downstream of phosphatidylinositol
CC       3-kinase (PI(3)K) to mediate the effects of various growth factors
CC       such as platelet-derived growth factor (PDGF), epidermal growth
CC       factor (EGF), insulin and insulin-like growth factor I (IGF-I).
CC       Plays a role in glucose transport by mediating insulin-induced
CC       translocation of the GLUT4 glucose transporter to the cell
CC       surface. Mediates the antiapoptotic effects of IGF-I. Mediates
CC       insulin-stimulated protein synthesis, partly by playing a role in
CC       both insulin-induced phosphorylation of 4E-BP1 and in insulin-
CC       induced activation of p70 S6 kinase. Promotes glycogen synthesis
CC       by mediating the insulin-induced activation of glycogen synthase
CC       (By similarity). Required for insulin-stimulated meiotic
CC       reinitiation during oocyte maturation.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated in response to insulin. Three
CC       specific sites, one in the kinase domain (Thr-309) and the two
CC       other ones in the C-terminal regulatory region (Ser-474 and Tyr-
CC       475), need to be phosphorylated for its full activation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Nucleus after activation by integrin-linked
CC       protein kinase 1 (ILK1) (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in the oocyte.
CC   -!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-
CC       kinase alpha (PI(3)K) results in its targeting to the plasma
CC       membrane.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AF317656; AAG59601.1; -; mRNA.
DR   RefSeq; NP_001083878.1; -.
DR   UniGene; Xl.738; -.
DR   HSSP; P31751; 1MRY.
DR   SMR; Q98TY9; 1-116.
DR   GeneID; 399170; -.
DR   KEGG; xla:399170; -.
DR   Xenbase; XB-FEAT-484952; akt1.
DR   HOVERGEN; Q98TY9; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015758; P:glucose transport; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signali...; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR015744; Akt.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000961; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_bd_CS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR22985:SF69; Akt; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW   Glycogen biosynthesis; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Sugar transport;
KW   Transferase; Transport.
FT   CHAIN         1    481       RAC-alpha serine/threonine-protein
FT                                kinase.
FT                                /FTId=PRO_0000223507.
FT   DOMAIN        5    108       PH.
FT   DOMAIN      151    409       Protein kinase.
FT   DOMAIN      410    481       AGC-kinase C-terminal.
FT   NP_BIND     157    165       ATP (By similarity).
FT   ACT_SITE    275    275       Proton acceptor (By similarity).
FT   BINDING     180    180       ATP (By similarity).
FT   MOD_RES     309    309       Phosphothreonine; by PDPK1 (By
FT                                similarity).
FT   MOD_RES     474    474       Phosphoserine (By similarity).
FT   MOD_RES     475    475       Phosphotyrosine (By similarity).
SQ   SEQUENCE   481 AA;  56042 MW;  FF56CFB9A6454303 CRC64;
     MNEVAIVKEG WLHKRGEYIK TWRPRYFLLK SDGTFIGYKE RPQDVDQLET PLNNFSVAKC
     QLMKTERPKP NTFIIRCLQW TTVIERTFHV DSPEEREEWI QVIQHVADNL KKQEEEMMEV
     RSGDSPSDNS GAEEMEVSHS KPKHKVTMNE FEYLKLLGKG TFGKVILVKE KATGRYYAMK
     ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT HDRLCFVMEY ANGGELFFHL
     SRERIFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN LMLDKDGHIK ITDFGLCKEG
     IKDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHEKLFE
     LILMEEIRFP RTLLPEAKSL LSGLLKKDPK QRLGGGPDDA KEIMQHKFFA GIVWQDVYEK
     KLVPPFKPQV TSETDTRYFD EEFTAQMITI TPPDQDDNFE FVDNERRPHF PQFSYSASGN
     A
//