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
//