ID   AKT_MLVAT               Reviewed;         501 AA.
AC   P31748;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=AKT kinase-transforming protein;
DE            EC=2.7.11.1;
GN   Name=V-AKT;
OS   AKT8 murine leukemia virus.
OC   Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
OC   Gammaretrovirus; Murine leukemia virus.
OX   NCBI_TaxID=11790;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92022574; PubMed=1833819;
RA   Bellacosa A., Testa J.R., Staal S.P., Tsichlis P.N.;
RT   "A retroviral oncogene, akt, encoding a serine-threonine kinase
RT   containing an SH2-like region.";
RL   Science 254:274-277(1991).
RN   [2]
RP   INTERACTION WITH THEM4.
RX   PubMed=11598301; DOI=10.1126/science.1062030;
RA   Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M.,
RA   Hemmings B.A.;
RT   "Carboxyl-terminal modulator protein (CTMP), a negative regulator of
RT   PKB/Akt and v-Akt at the plasma membrane.";
RL   Science 294:374-380(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with mouse THEM4.
CC   -!- DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4.
CC   -!- PTM: Autophosphorylated on threonine and serine residues.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Akt
CC       polyprotein.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M80675; AAA42545.1; -; Genomic_DNA.
DR   HSSP; P31749; 1H10.
DR   SMR; P31748; 24-142.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
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   1: Evidence at protein level;
KW   ATP-binding; Host-virus interaction; Kinase; Nucleotide-binding;
KW   Oncogene; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    501       AKT kinase-transforming protein.
FT                                /FTId=PRO_0000085614.
FT   DOMAIN       26    129       PH.
FT   DOMAIN      171    429       Protein kinase.
FT   DOMAIN      430    501       AGC-kinase C-terminal.
FT   NP_BIND     177    185       ATP (By similarity).
FT   ACT_SITE    295    295       Proton acceptor (By similarity).
FT   BINDING     200    200       ATP (By similarity).
FT   MOD_RES     347    347       Phosphotyrosine (By similarity).
SQ   SEQUENCE   501 AA;  57870 MW;  5AEFDE58CD42F773 CRC64;
     AREETLIIIP GLPLSLGATD TMNDVAIVKE GWLHKRGEYI KTWRPRYFLL KNDGTFIGYK
     ERPQDVDQRE SPLNNFSVAQ CQLMKTERPR PNTFIIRCLQ WTTVIERTFH VETPEEREEW
     ATAIQTVADG LKRQEEETMD FRSGSPSDNS GAEEMEVSLA KPKHRVTMNE FEYLKLLGKG
     TFGKVILVKE KATGRYYAMK ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT
     HDRLCFVMEY ANGGELFFHL SRERVFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN
     LMLDKDGHIK ITDFGLCKEG IKDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM
     YEMMCGRLPF YNQDHEKLFE LILMEEIRFP RTLGPEAKSL LSGLLKKDPT QRLGGGSEDA
     KEIMQHRFFA NIVWQDVYEK KLSPPFKPQV TSETDTRYFD EEFTAQMITI TPPDQDDSME
     CVDSERRPHF PQFSYSASGT A
//