AKT_MLVAT
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 03-AUG-2022, entry version 116.
DE RecName: Full=AKT kinase-transforming protein;
DE EC=2.7.11.1;
GN Name=V-AKT;
OS AKT8 murine leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11790;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1833819; DOI=10.1126/science.254.5029.274;
RA Bellacosa A., Testa J.R., Staal S.P., Tsichlis P.N.;
RT "A retroviral oncogene, akt, encoding a serine-threonine kinase containing
RT 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:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with mouse THEM4. {ECO:0000269|PubMed:11598301}.
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 polyprotein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000305}.
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DR EMBL; M80675; AAA42545.1; -; Genomic_DNA.
DR SMR; P31748; -.
DR ChEMBL; CHEMBL3627590; -.
DR PRIDE; P31748; -.
DR ABCD; P31748; 1 sequenced antibody.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
DR GO; GO:1990418; P:response to insulin-like growth factor stimulus; ISS:AgBase.
DR CDD; cd01241; PH_PKB; 1.
DR CDD; cd05594; STKc_PKB_alpha; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR034676; Akt1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039026; PH_PKB.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR039027; RAC_alpha.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF200; PTHR24351:SF200; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Oncogene;
KW Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..501
FT /note="AKT kinase-transforming protein"
FT /id="PRO_0000085614"
FT DOMAIN 26..129
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 171..429
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 430..501
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 135..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 295
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 177..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 347
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
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
