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AKT serine/threonine kinase 2

 F1PRG4_CANLF            Unreviewed;       481 AA.
F1PRG4;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
30-AUG-2017, entry version 52.
SubName: Full=AKT serine/threonine kinase 2 {ECO:0000313|Ensembl:ENSCAFP00000008032};
Name=AKT2 {ECO:0000313|Ensembl:ENSCAFP00000008032};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000008032, ECO:0000313|Proteomes:UP000002254};
[1] {ECO:0000313|Ensembl:ENSCAFP00000008032, ECO:0000313|Proteomes:UP000002254}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000008032,
ECO:0000313|Proteomes:UP000002254};
PubMed=16341006; DOI=10.1038/nature04338;
Broad Sequencing Platform;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2] {ECO:0000313|Ensembl:ENSCAFP00000008032}
IDENTIFICATION.
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000008032};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000256|SAAS:SAAS00594266}.
-!- SIMILARITY: Belongs to the protein kinase superfamily.
{ECO:0000256|RuleBase:RU000304}.
-!- CAUTION: The sequence shown here is derived from an Ensembl
automatic analysis pipeline and should be considered as
preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000008032}.
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EMBL; AAEX03000946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_013969563.1; XM_014114088.1.
UniGene; Cfa.10875; -.
STRING; 9615.ENSCAFP00000008032; -.
PaxDb; F1PRG4; -.
Ensembl; ENSCAFT00000008666; ENSCAFP00000008032; ENSCAFG00000005388.
GeneID; 449021; -.
CTD; 208; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
InParanoid; F1PRG4; -.
OMA; KATGMYY; -.
OrthoDB; EOG091G06FF; -.
TreeFam; TF102004; -.
Reactome; R-CFA-165158; Activation of AKT2.
Reactome; R-CFA-165181; Inhibition of TSC complex formation by PKB.
Reactome; R-CFA-3769402; Deactivation of the beta-catenin transactivating complex.
Proteomes; UP000002254; Chromosome 1.
Bgee; ENSCAFG00000005388; -.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
GO; GO:0071486; P:cellular response to high light intensity; IEA:Ensembl.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0010748; P:negative regulation of plasma membrane long-chain fatty acid transport; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IEA:Ensembl.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
GO; GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0097473; P:retinal rod cell apoptotic process; IEA:Ensembl.
CDD; cd05595; STKc_PKB_beta; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034677; Akt2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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; SSF50729; SSF50729; 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.
3: Inferred from homology;
ATP-binding {ECO:0000256|RuleBase:RU000304,
ECO:0000256|SAAS:SAAS00593399};
Complete proteome {ECO:0000313|Proteomes:UP000002254};
Kinase {ECO:0000256|RuleBase:RU000304, ECO:0000256|SAAS:SAAS00593706};
Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
ECO:0000256|SAAS:SAAS00593399};
Reference proteome {ECO:0000313|Proteomes:UP000002254};
Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304,
ECO:0000256|SAAS:SAAS00593706};
Transferase {ECO:0000256|RuleBase:RU000304,
ECO:0000256|SAAS:SAAS00593706}.
DOMAIN 5 108 PH. {ECO:0000259|PROSITE:PS50003}.
DOMAIN 152 409 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
DOMAIN 410 481 AGC-kinase C-terminal.
{ECO:0000259|PROSITE:PS51285}.
SEQUENCE 481 AA; 55638 MW; BAA30EF561852A85 CRC64;
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPDAPDQTLP PLNNFSVAEC
QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM RAIQMVANSL KQRGPGEDPM
DYKCGSPSDP SAAEEMEVAV SKARAKVTMN DFDYLKLLGK GTFGKVILVR EKASGRYYAM
KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH
LSRERVFTEE RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE
LILMEEIRFP RTLSPEAKSL LAGLLKKDPK QRLGGGPSDA REVMEHRFFL SVSWQDVVQK
KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLG SLELDQRTHF PQFSYSASIR
E


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