ID AKT2_CAEEL Reviewed; 528 AA. AC Q9XTG7; O77145; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 16-JUN-2009, entry version 73. DE RecName: Full=Serine/threonine-protein kinase akt-2; DE EC=2.7.11.1; DE AltName: Full=Protein kinase B akt-2; DE Short=PKB akt-2; GN Name=akt-2; ORFNames=F28H6.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RX MEDLINE=98382502; PubMed=9716402; RA Paradis S., Ruvkun G.; RT "Caenorhabditis elegans Akt/PKB transduces insulin receptor-like RT signals from AGE-1 PI3 kinase to the DAF-16 transcription factor."; RL Genes Dev. 12:2488-2498(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE RP SPLICING. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [3] RP FUNCTION. RX MEDLINE=99292684; PubMed=10364160; RA Paradis S., Ailion M., Toker A., Thomas J.H., Ruvkun G.; RT "A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 RT kinase signals that regulate diapause in Caenorhabditis elegans."; RL Genes Dev. 13:1438-1452(1999). RN [4] RP FUNCTION. RX MEDLINE=21614652; PubMed=11747825; DOI=10.1016/S0960-9822(01)00594-2; RA Henderson S.T., Johnson T.E.; RT "daf-16 integrates developmental and environmental inputs to mediate RT aging in the nematode Caenorhabditis elegans."; RL Curr. Biol. 11:1975-1980(2001). RN [5] RP FUNCTION. RX PubMed=11381260; DOI=10.1038/88850; RA Lin K., Hsin H., Libina N., Kenyon C.; RT "Regulation of the Caenorhabditis elegans longevity protein DAF-16 by RT insulin/IGF-1 and germline signaling."; RL Nat. Genet. 28:139-145(2001). RN [6] RP INTERACTION WITH PDK-1; SGK-1; AKT-1 AND DAF-16, AND FUNCTION. RX PubMed=15068796; DOI=10.1016/S1534-5807(04)00095-4; RA Hertweck M., Goebel C., Baumeister R.; RT "C. elegans SGK-1 is the critical component in the Akt/PKB kinase RT complex to control stress response and life span."; RL Dev. Cell 6:577-588(2004). CC -!- FUNCTION: Acts downstream age-1 and pdk-1 in the daf-2/insulin CC receptor-like transduction pathway, which controls longevity and CC prevents developmental arrest at the dauer stage. Phosphorylates CC Forkhead-related daf-16 transcription factor, which inhibits its CC entry into the nucleus and antagonizes its function. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with pdk-1, sgk-1, akt-1 and daf-16. Part of a CC complex containing sgk-1, akt-1 and akt-2. CC -!- INTERACTION: CC Q22847:-; NbExp=1; IntAct=EBI-320656, EBI-316760; CC O18676:daf-16; NbExp=1; IntAct=EBI-320656, EBI-1770827; CC P34766:pal-1; NbExp=1; IntAct=EBI-320656, EBI-311911; CC P34707-1:skn-1; NbExp=1; IntAct=EBI-320656, EBI-434984; CC P34707-3:skn-1; NbExp=1; IntAct=EBI-320656, EBI-434993; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=Q9XTG7-1; Sequence=Displayed; CC Name=b; CC IsoId=Q9XTG7-2; Sequence=VSP_017047, VSP_017048; CC -!- TISSUE SPECIFICITY: Expressed in neurons, muscle cells of the CC pharynx, rectal gland cells, and spermatheca. CC -!- DEVELOPMENTAL STAGE: Expressed in late stage embryos and CC throughout life. 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; AF072381; AAC62468.1; -; mRNA. DR EMBL; AL031621; CAA20936.1; -; Genomic_DNA. DR EMBL; Z92837; CAA20936.1; JOINED; Genomic_DNA. DR EMBL; Z92837; CAB07403.1; -; Genomic_DNA. DR EMBL; AL031621; CAB07403.1; JOINED; Genomic_DNA. DR EMBL; AL031621; CAC70087.1; -; Genomic_DNA. DR EMBL; Z92837; CAC70087.1; JOINED; Genomic_DNA. DR EMBL; Z92837; CAD21654.1; -; Genomic_DNA. DR EMBL; AL031621; CAD21654.1; JOINED; Genomic_DNA. DR PIR; T21523; T21523. DR PIR; T43234; T43234. DR RefSeq; NP_510357.3; -. DR UniGene; Cel.18147; -. DR HSSP; P31751; 1MRY. DR DIP; DIP:26368N; -. DR IntAct; Q9XTG7; 10. DR Ensembl; F28H6.1; Caenorhabditis elegans. DR GeneID; 181524; -. DR WormBase; WBGene00000103; akt-2. DR WormPep; F28H6.1a; CE18646. DR WormPep; F28H6.1b; CE29298. DR OMA; Q9XTG7; NIDEPEE. DR BRENDA; 2.7.11.1; 672. DR NextBio; 914298; -. DR ArrayExpress; Q9XTG7; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0043053; P:dauer entry; IMP:WormBase. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011993; PH_type. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR001849; Pleckstrin_homology. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR015744; Serine/threonine_Kinase_Rac. 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 Alternative splicing; ATP-binding; Complete proteome; KW Developmental protein; Kinase; Nucleotide-binding; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 528 Serine/threonine-protein kinase akt-2. FT /FTId=PRO_0000085616. FT DOMAIN 12 115 PH. FT DOMAIN 180 437 Protein kinase. FT DOMAIN 438 515 AGC-kinase C-terminal. FT NP_BIND 186 194 ATP (By similarity). FT ACT_SITE 303 303 Proton acceptor (By similarity). FT BINDING 209 209 ATP (By similarity). FT VAR_SEQ 470 483 EFTSMPVQLTPPRR -> VRYVSILLKVSEAI (in FT isoform b). FT /FTId=VSP_017047. FT VAR_SEQ 484 528 Missing (in isoform b). FT /FTId=VSP_017048. SQ SEQUENCE 528 AA; 61058 MW; 9750E8F0AE4F6AE7 CRC64; MSTENAHLQK EDIVIESWLH KKGEHIRNWR PRYFILFRDG TLLGFRSKPK EDQPLPEPLN NFMIRDAATV CLDKPRPNMF IVRCLQWTTV IERTFYADSA DFRQMWIEAI QAVSSHNRLK ENAGNTSMQE EDTNGNPSGE SDVNMDATST RSDNDFESTV MNIDEPEEVP RKNTVTMDDF DFLKVLGQGT FGKVILCREK SSDKLYAIKI IRKEMVVDRS EVAHTLTENR VLYACVHPFL TLLKYSFQAQ YHICFVMEFA NGGELFTHLQ RCKTFSEART RFYGSEIILA LGYLHHRNIV YRDMKLENLL LDRDGHIKIT DFGLCKEEIK YGDKTSTFCG TPEYLAPEVI EDIDYDRSVD WWGVGVVMYE MMCGRLPFSA KENGKLFELI TTCDLKFPNR LSPEAVTLLS GLLERVPAKR LGAGPDDARE VSRAEFFKDV DWEATLRKEV EPPFKPNVMS ETDTSFFDRE FTSMPVQLTP PRRGEELPTV DEEEELQANF IQFASYYVSG SLERSYDTNR SADKYEIR //