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RecName: Full=Serine/threonine-protein kinase akt-2; AltName: Full=Protein kinase B akt-2; Short=PKB akt-2

UniProtKB/Swiss-Prot: Q9XTG7.1

Identical Proteins FASTA Graphics 

LOCUS       AKT2_CAEEL               528 aa            linear   INV 27-NOV-2024
DEFINITION  RecName: Full=Serine/threonine-protein kinase akt-2; AltName:
            Full=Protein kinase B akt-2; Short=PKB akt-2.
ACCESSION   Q9XTG7
VERSION     Q9XTG7.1
DBSOURCE    UniProtKB: locus AKT2_CAEEL, accession Q9XTG7;
            class: standard.
            extra accessions:O77145
            created: Jan 24, 2006.
            sequence updated: Nov 1, 1999.
            annotation updated: Nov 27, 2024.
            xrefs: AF072381.1, AAC62468.1, BX284606.5, CAA20936.1, Z92837.1,
            CAC70087.1, T21523, T43234, NP_001024612.1, NP_510357.3
            xrefs (non-sequence databases): AlphaFoldDB:Q9XTG7, SMR:Q9XTG7,
            BioGRID:46423, ComplexPortal:CPX-1129, DIP:DIP-26368N,
            IntAct:Q9XTG7, STRING:6239.F28H6.1a.1, iPTMnet:Q9XTG7,
            PaxDb:6239-F28H6.1a, PeptideAtlas:Q9XTG7,
            EnsemblMetazoa:F28H6.1a.1, EnsemblMetazoa:F28H6.1a.1,
            EnsemblMetazoa:WBGene00000103, EnsemblMetazoa:F28H6.1b.1,
            EnsemblMetazoa:F28H6.1b.1, GeneID:181524, KEGG:cel:CELE_F28H6.1,
            UCSC:F28H6.1b, AGR:WB:WBGene00000103, CTD:181524,
            WormBase:F28H6.1a, WormBase:CE18646, WormBase:F28H6.1b,
            WormBase:CE29298, eggNOG:KOG0690, GeneTree:ENSGT00940000168810,
            HOGENOM:CLU_000288_11_2_1, InParanoid:Q9XTG7, OMA:CETTANH,
            OrthoDB:3028764at2759, PhylomeDB:Q9XTG7, Reactome:R-CEL-1257604,
            Reactome:R-CEL-1474151, Reactome:R-CEL-165158,
            Reactome:R-CEL-165159, Reactome:R-CEL-198323,
            Reactome:R-CEL-198693, Reactome:R-CEL-199418,
            Reactome:R-CEL-203615, Reactome:R-CEL-211163,
            Reactome:R-CEL-354192, Reactome:R-CEL-389357,
            Reactome:R-CEL-389513, Reactome:R-CEL-392451,
            Reactome:R-CEL-450385, Reactome:R-CEL-450604,
            Reactome:R-CEL-5218920, Reactome:R-CEL-6804758,
            Reactome:R-CEL-6811558, Reactome:R-CEL-69202, Reactome:R-CEL-69656,
            Reactome:R-CEL-8849469, Reactome:R-CEL-8876198,
            Reactome:R-CEL-8948751, Reactome:R-CEL-9009391,
            Reactome:R-CEL-9604323, Reactome:R-CEL-9607240,
            Reactome:R-CEL-9614399, Reactome:R-CEL-9634638,
            Reactome:R-CEL-9755511, SignaLink:Q9XTG7, PRO:PR:Q9XTG7,
            Proteomes:UP000001940, Bgee:WBGene00000103, GO:1902911, GO:0005524,
            GO:0044024, GO:0046872, GO:0005547, GO:0106310, GO:0004674,
            GO:0008340, GO:0045087, GO:0008286, GO:0035556, GO:0006468,
            GO:0010468, GO:0008582, CDD:cd01241, FunFam:1.10.510.10:FF:000033,
            FunFam:2.30.29.30:FF:000404, FunFam:3.30.200.20:FF:001053,
            Gene3D:2.30.29.30, Gene3D:1.10.510.10, InterPro:IPR000961,
            InterPro:IPR011009, InterPro:IPR011993, InterPro:IPR001849,
            InterPro:IPR039026, InterPro:IPR017892, InterPro:IPR000719,
            InterPro:IPR017441, InterPro:IPR008271, PANTHER:PTHR24351:SF209,
            PANTHER:PTHR24351, Pfam:PF00169, Pfam:PF00069, Pfam:PF00433,
            SMART:SM00233, SMART:SM00133, SMART:SM00220, SUPFAM:SSF50729,
            SUPFAM:SSF56112, PROSITE:PS51285, PROSITE:PS50003, PROSITE:PS00107,
            PROSITE:PS50011, PROSITE:PS00108
KEYWORDS    Alternative splicing; ATP-binding; Developmental protein; Immunity;
            Innate immunity; Kinase; Magnesium; Metal-binding;
            Nucleotide-binding; Phosphoprotein; Reference proteome;
            Serine/threonine-protein kinase; Transferase.
SOURCE      Caenorhabditis elegans
  ORGANISM  Caenorhabditis elegans
            Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
            Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
            Caenorhabditis.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Paradis,S. and Ruvkun,G.
  TITLE     Caenorhabditis elegans Akt/PKB transduces insulin receptor-like
            signals from AGE-1 PI3 kinase to the DAF-16 transcription factor
  JOURNAL   Genes Dev 12 (16), 2488-2498 (1998)
   PUBMED   9716402
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE
            SPECIFICITY, AND DEVELOPMENTAL STAGE.
REFERENCE   2  (residues 1 to 528)
  CONSRTM   C. elegans Sequencing Consortium
  TITLE     Genome sequence of the nematode C. elegans: a platform for
            investigating biology
  JOURNAL   Science 282 (5396), 2012-2018 (1998)
   PUBMED   9851916
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
            SPLICING.;
            STRAIN=Bristol N2
            Erratum:[Science 1999 Jan 1;283(5398):35]
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Paradis,S., Ailion,M., Toker,A., Thomas,J.H. and Ruvkun,G.
  TITLE     A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3
            kinase signals that regulate diapause in Caenorhabditis elegans
  JOURNAL   Genes Dev 13 (11), 1438-1452 (1999)
   PUBMED   10364160
  REMARK    FUNCTION.
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Henderson,S.T. and Johnson,T.E.
  TITLE     daf-16 integrates developmental and environmental inputs to mediate
            aging in the nematode Caenorhabditis elegans
  JOURNAL   Curr Biol 11 (24), 1975-1980 (2001)
   PUBMED   11747825
  REMARK    FUNCTION.
            Erratum:[Curr Biol. 2005 Apr 12;15(7):690]
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Lin,K., Hsin,H., Libina,N. and Kenyon,C.
  TITLE     Regulation of the Caenorhabditis elegans longevity protein DAF-16
            by insulin/IGF-1 and germline signaling
  JOURNAL   Nat Genet 28 (2), 139-145 (2001)
   PUBMED   11381260
  REMARK    FUNCTION.
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Evans,E.A., Chen,W.C. and Tan,M.W.
  TITLE     The DAF-2 insulin-like signaling pathway independently regulates
            aging and immunity in C. elegans
  JOURNAL   Aging Cell 7 (6), 879-893 (2008)
   PUBMED   18782349
  REMARK    FUNCTION, AND DISRUPTION PHENOTYPE.
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Tullet,J.M., Hertweck,M., An,J.H., Baker,J., Hwang,J.Y., Liu,S.,
            Oliveira,R.P., Baumeister,R. and Blackwell,T.K.
  TITLE     Direct inhibition of the longevity-promoting factor SKN-1 by
            insulin-like signaling in C. elegans
  JOURNAL   Cell 132 (6), 1025-1038 (2008)
   PUBMED   18358814
  REMARK    FUNCTION.
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Hertweck,M., Gobel,C. and Baumeister,R.
  TITLE     C. elegans SGK-1 is the critical component in the Akt/PKB kinase
            complex to control stress response and life span
  JOURNAL   Dev Cell 6 (4), 577-588 (2004)
   PUBMED   15068796
  REMARK    FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PDK-1; SGK-1; AKT-1
            AND DAF-16, AND DISRUPTION PHENOTYPE.
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Qi,W., Huang,X., Neumann-Haefelin,E., Schulze,E. and Baumeister,R.
  TITLE     Cell-nonautonomous signaling of FOXO/DAF-16 to the stem cells of
            Caenorhabditis elegans
  JOURNAL   PLoS Genet 8 (8), e1002836 (2012)
   PUBMED   22916022
  REMARK    FUNCTION.
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Nakagawa,A., Sullivan,K.D. and Xue,D.
  TITLE     Caspase-activated phosphoinositide binding by CNT-1 promotes
            apoptosis by inhibiting the AKT pathway
  JOURNAL   Nat Struct Mol Biol 21 (12), 1082-1090 (2014)
   PUBMED   25383666
  REMARK    FUNCTION, DOMAIN, AND MUTAGENESIS OF LYS-209.
COMMENT     On or before Jan 24, 2006 this sequence version replaced
            gi:74960870, gi:7500109.
            [FUNCTION] Acts downstream of PI3 kinase age-1 and kinase pdk-1 in
            the daf-2/insulin receptor-like transduction pathway
            (PubMed:10364160, PubMed:11381260, PubMed:11747825,
            PubMed:15068796, PubMed:18782349, PubMed:22916022, PubMed:9716402).
            Essential role in regulating developmental arrest at the dauer
            stage (PubMed:10364160). Phosphorylates Forkhead-related daf-16 and
            the longevity-promoting skn-1 transcription factors, which inhibits
            their entry into the nucleus and antagonizes their functions
            (PubMed:11381260, PubMed:11747825, PubMed:15068796,
            PubMed:18358814). Role in immune function and pathogen resistance
            (PubMed:18782349). Downstream of age-1 and together with akt-1 and
            sgk-1, promotes cell survival during embryonic development
            (PubMed:25383666). Plays a role in maintaining the gonadal basement
            membrane through antagonizing akt-1 activity (PubMed:22916022).
            {ECO:0000269|PubMed:10364160, ECO:0000269|PubMed:11381260,
            ECO:0000269|PubMed:11747825, ECO:0000269|PubMed:15068796,
            ECO:0000269|PubMed:18358814, ECO:0000269|PubMed:18782349,
            ECO:0000269|PubMed:22916022, ECO:0000269|PubMed:25383666,
            ECO:0000269|PubMed:9716402}.
            [CATALYTIC ACTIVITY] Reaction=L-seryl-[protein] + ATP =
            O-phospho-L-seryl-[protein] + ADP + H(+); Xref=Rhea:RHEA:17989,
            Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
            ChEBI:CHEBI:456216; EC=2.7.11.1.
            [CATALYTIC ACTIVITY] Reaction=L-threonyl-[protein] + ATP =
            O-phospho-L-threonyl-[protein] + ADP + H(+); Xref=Rhea:RHEA:46608,
            Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
            ChEBI:CHEBI:456216; EC=2.7.11.1.
            [COFACTOR] Name=Mg(2+); Xref=ChEBI:CHEBI:18420.
            ACTIVITY REGULATION: Phosphorylated and activated by pdk-1.
            {ECO:0000269|PubMed:15068796}.
            [SUBUNIT] Interacts with pdk-1, sgk-1, akt-1 and daf-16. Part of a
            complex containing sgk-1, akt-1 and akt-2.
            {ECO:0000269|PubMed:15068796}.
            [INTERACTION] Q9XTG7; Q17941: akt-1; NbExp=2; IntAct=EBI-320656,
            EBI-1770718; Q9XTG7; O16850: daf-16; NbExp=3; IntAct=EBI-320656,
            EBI-324028; Q9XTG7; Q2PJ68: sgk-1; NbExp=3; IntAct=EBI-320656,
            EBI-1770776.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=a {ECO:0000312|WormBase:F28H6.1a}; IsoId=Q9XTG7-1;
            Sequence=Displayed; Name=b {ECO:0000312|WormBase:F28H6.1b};
            IsoId=Q9XTG7-2; Sequence=VSP_017047, VSP_017048.
            [TISSUE SPECIFICITY] Expressed in neurons, muscle cells of the
            pharynx, rectal gland cells, and spermatheca.
            {ECO:0000269|PubMed:9716402}.
            [DEVELOPMENTAL STAGE] Expressed in late stage embryos and
            throughout life. {ECO:0000269|PubMed:9716402}.
            [DOMAIN] The PH domain binds to phosphatidylinositol
            3,4,5-trisphosphate (PtdIns(3,4,5)P3) resulting in its targeting to
            the plasma membrane. {ECO:0000269|PubMed:25383666}.
            [DISRUPTION PHENOTYPE] Defective egg-laying and increased
            resistance to pathogens. Simultaneous knockdown of akt-1 and akt-2
            result in dauer formation and a weak extension to life span.
            {ECO:0000269|PubMed:15068796, ECO:0000269|PubMed:18782349}.
            [SIMILARITY] Belongs to the protein kinase superfamily. AGC Ser/Thr
            protein kinase family. RAC subfamily. {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Caenorhabditis elegans"
                     /db_xref="taxon:6239"
     gene            1..528
                     /gene="akt-2"
                     /locus_tag="F28H6.1"
     Protein         1..528
                     /product="Serine/threonine-protein kinase akt-2"
                     /EC_number="2.7.11.1"
                     /note="Protein kinase B akt-2; PKB akt-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..528
                     /region_name="Mature chain"
                     /note="Serine/threonine-protein kinase akt-2.
                     /id=PRO_0000085616."
     Region          11..116
                     /region_name="PH_PKB"
                     /note="Protein Kinase B-like pleckstrin homology (PH)
                     domain; cd01241"
                     /db_xref="CDD:269947"
     Region          12..115
                     /region_name="Domain"
                     /note="PH.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00145."
     Site            order(21,23..26,30,32,59..60,62,93)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269947"
     Region          121..153
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          180..437
                     /region_name="Domain"
                     /note="Protein kinase.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00159."
     Region          184..509
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(186..189,192,194,207,209,241,257..260,303,307..308,
                     310,320..321)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            209
                     /site_type="mutagenized"
                     /note="K->M: Probable loss of kinase activity. Increased
                     apoptosis during embryonic development in an akt-1 tm399
                     mutant background. /evidence=ECO:0000269|PubMed:25383666."
     Site            303
                     /site_type="active"
                     /note="Proton acceptor.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00159,
                     ECO:0000255|PROSITE-ProRule:PRU10027."
     Region          438..515
                     /region_name="Domain"
                     /note="AGC-kinase C-terminal.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00618."
     Region          470..483
                     /region_name="Splicing variant"
                     /note="EFTSMPVQLTPPRR -> VRYVSILLKVSEAI (in isoform b).
                     /evidence=ECO:0000303|PubMed:9716402. /id=VSP_017047."
     Region          484..528
                     /region_name="Splicing variant"
                     /note="Missing (in isoform b).
                     /evidence=ECO:0000303|PubMed:9716402. /id=VSP_017048."
ORIGIN      
        1 mstenahlqk edivieswlh kkgehirnwr pryfilfrdg tllgfrskpk edqplpepln
       61 nfmirdaatv cldkprpnmf ivrclqwttv iertfyadsa dfrqmwieai qavsshnrlk
      121 enagntsmqe edtngnpsge sdvnmdatst rsdndfestv mnidepeevp rkntvtmddf
      181 dflkvlgqgt fgkvilcrek ssdklyaiki irkemvvdrs evahtltenr vlyacvhpfl
      241 tllkysfqaq yhicfvmefa nggelfthlq rcktfseart rfygseiila lgylhhrniv
      301 yrdmklenll ldrdghikit dfglckeeik ygdktstfcg tpeylapevi edidydrsvd
      361 wwgvgvvmye mmcgrlpfsa kengklfeli ttcdlkfpnr lspeavtlls gllervpakr
      421 lgagpddare vsraeffkdv dweatlrkev eppfkpnvms etdtsffdre ftsmpvqltp
      481 prrgeelptv deeeelqanf iqfasyyvsg slersydtnr sadkyeir
//
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