Q9XTG7 (AKT2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase akt-2
EC=2.7.11.1

Alternative name(s):
Protein kinase B akt-2
Short name=PKB akt-2

Gene names

Name:	akt-2
ORF Names:	F28H6.1

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts downstream of age-1 and pdk-1 in the daf-2/insulin receptor-like transduction pathway. Essential role in regulating developmental arrest at the dauer stage. Phosphorylates Forkhead-related daf-16 and the longevity-promoting skn-1 transcription factors, which inhibits their entry into the nucleus and antagonizes their functions. Role in immune function and pathogen resistance. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Phosphorylated and activated by pdk-1. Ref.8
Subunit structure	Interacts with pdk-1, sgk-1, akt-1 and daf-16. Part of a complex containing sgk-1, akt-1 and akt-2. Ref.8
Tissue specificity	Expressed in neurons, muscle cells of the pharynx, rectal gland cells, and spermatheca. Ref.1
Developmental stage	Expressed in late stage embryos and throughout life. Ref.1
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. Ref.6 Ref.8
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 PH domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Immunity Innate immunity
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	dauer entry Inferred from mutant phenotype Ref.8. Source: WormBase determination of adult lifespan Inferred from mutant phenotype. Source: WormBase innate immune response Inferred from electronic annotation. Source: UniProtKB-KW insulin receptor signaling pathway Inferred from mutant phenotype Ref.1. Source: WormBase
Cellular component	intracellular Inferred from direct assay Ref.1. Source: WormBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.8. Source: IntAct protein serine/threonine kinase activity Inferred from direct assay Ref.7. Source: WormBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
akt-1	Q17941	2	EBI-320656,EBI-1770718
daf-16	O16850	3	EBI-320656,EBI-324028
sgk-1	Q2PJ68	3	EBI-320656,EBI-1770776

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform a (identifier: Q9XTG7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform b (identifier: Q9XTG7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     470-483: EFTSMPVQLTPPRR → VRYVSILLKVSEAI
     484-528: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 528	528	Serine/threonine-protein kinase akt-2		PRO_0000085616
Regions
	Domain	12 – 115	104	PH
	Domain	180 – 437	258	Protein kinase
	Domain	438 – 515	78	AGC-kinase C-terminal
	Nucleotide binding	186 – 194	9	ATP By similarity
Sites
	Active site	303	1	Proton acceptor By similarity
	Binding site	209	1	ATP By similarity
Natural variations
	Alternative sequence	470 – 483	14	EFTSM…TPPRR → VRYVSILLKVSEAI in isoform b.		VSP_017047
	Alternative sequence	484 – 528	45	Missing in isoform b.		VSP_017048

Sequences

	Sequence		Length	Mass (Da)
	Isoform a [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 9750E8F0AE4F6AE7	FASTA	528	61,058
	10 20 30 40 50 60 MSTENAHLQK EDIVIESWLH KKGEHIRNWR PRYFILFRDG TLLGFRSKPK EDQPLPEPLN 70 80 90 100 110 120 NFMIRDAATV CLDKPRPNMF IVRCLQWTTV IERTFYADSA DFRQMWIEAI QAVSSHNRLK 130 140 150 160 170 180 ENAGNTSMQE EDTNGNPSGE SDVNMDATST RSDNDFESTV MNIDEPEEVP RKNTVTMDDF 190 200 210 220 230 240 DFLKVLGQGT FGKVILCREK SSDKLYAIKI IRKEMVVDRS EVAHTLTENR VLYACVHPFL 250 260 270 280 290 300 TLLKYSFQAQ YHICFVMEFA NGGELFTHLQ RCKTFSEART RFYGSEIILA LGYLHHRNIV 310 320 330 340 350 360 YRDMKLENLL LDRDGHIKIT DFGLCKEEIK YGDKTSTFCG TPEYLAPEVI EDIDYDRSVD 370 380 390 400 410 420 WWGVGVVMYE MMCGRLPFSA KENGKLFELI TTCDLKFPNR LSPEAVTLLS GLLERVPAKR 430 440 450 460 470 480 LGAGPDDARE VSRAEFFKDV DWEATLRKEV EPPFKPNVMS ETDTSFFDRE FTSMPVQLTP 490 500 510 520 PRRGEELPTV DEEEELQANF IQFASYYVSG SLERSYDTNR SADKYEIR
	Isoform b [UniParc]. Checksum: 7977EE98BF40CD83	FASTA	483	55,757
	10 20 30 40 50 60 MSTENAHLQK EDIVIESWLH KKGEHIRNWR PRYFILFRDG TLLGFRSKPK EDQPLPEPLN 70 80 90 100 110 120 NFMIRDAATV CLDKPRPNMF IVRCLQWTTV IERTFYADSA DFRQMWIEAI QAVSSHNRLK 130 140 150 160 170 180 ENAGNTSMQE EDTNGNPSGE SDVNMDATST RSDNDFESTV MNIDEPEEVP RKNTVTMDDF 190 200 210 220 230 240 DFLKVLGQGT FGKVILCREK SSDKLYAIKI IRKEMVVDRS EVAHTLTENR VLYACVHPFL 250 260 270 280 290 300 TLLKYSFQAQ YHICFVMEFA NGGELFTHLQ RCKTFSEART RFYGSEIILA LGYLHHRNIV 310 320 330 340 350 360 YRDMKLENLL LDRDGHIKIT DFGLCKEEIK YGDKTSTFCG TPEYLAPEVI EDIDYDRSVD 370 380 390 400 410 420 WWGVGVVMYE MMCGRLPFSA KENGKLFELI TTCDLKFPNR LSPEAVTLLS GLLERVPAKR 430 440 450 460 470 480 LGAGPDDARE VSRAEFFKDV DWEATLRKEV EPPFKPNVMS ETDTSFFDRV RYVSILLKVS EAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor." Paradis S., Ruvkun G. Genes Dev. 12:2488-2498(1998) [PubMed: 9716402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[3]	"A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans." Paradis S., Ailion M., Toker A., Thomas J.H., Ruvkun G. Genes Dev. 13:1438-1452(1999) [PubMed: 10364160] [Abstract] Cited for: FUNCTION.
[4]	"daf-16 integrates developmental and environmental inputs to mediate aging in the nematode Caenorhabditis elegans." Henderson S.T., Johnson T.E. Curr. Biol. 11:1975-1980(2001) [PubMed: 11747825] [Abstract] Cited for: FUNCTION.
[5]	"Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling." Lin K., Hsin H., Libina N., Kenyon C. Nat. Genet. 28:139-145(2001) [PubMed: 11381260] [Abstract] Cited for: FUNCTION.
[6]	"The DAF-2 insulin-like signaling pathway independently regulates aging and immunity in C. elegans." Evans E.A., Chen W.C., Tan M.-W. Aging Cell 7:879-893(2008) [PubMed: 18782349] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]	"Direct inhibition of the longevity-promoting factor SKN-1 by insulin-like signaling in C. elegans." Tullet J.M., Hertweck M., An J.H., Baker J., Hwang J.Y., Liu S., Oliveira R.P., Baumeister R., Blackwell T.K. Cell 132:1025-1038(2008) [PubMed: 18358814] [Abstract] Cited for: FUNCTION.
[8]	"C. elegans SGK-1 is the critical component in the Akt/PKB kinase complex to control stress response and life span." Hertweck M., Goebel C., Baumeister R. Dev. Cell 6:577-588(2004) [PubMed: 15068796] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH PDK-1; SGK-1; AKT-1 AND DAF-16, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF072381 mRNA. Translation: AAC62468.1. AL031621, Z92837 Genomic DNA. Translation: CAA20936.1. Z92837, AL031621 Genomic DNA. Translation: CAB07403.1. AL031621, Z92837 Genomic DNA. Translation: CAC70087.1. Z92837, AL031621 Genomic DNA. Translation: CAD21654.1.
PIR	T21523. T43234.
RefSeq	NP_001024612.1. NM_001029441.2. NP_510357.3. NM_077956.4.
UniGene	Cel.18147.
3D structure databases
ProteinModelPortal	Q9XTG7.
SMR	Q9XTG7. Positions 9-508.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-26368N.
IntAct	Q9XTG7. 10 interactions.
MINT	MINT-1058855.
STRING	Q9XTG7.
Proteomic databases
PRIDE	Q9XTG7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	F28H6.1a; F28H6.1a; F28H6.1.
GeneID	181524.
KEGG	cel:F28H6.1.
UCSC	F28H6.1b. c. elegans.
Organism-specific databases
CTD	181524.
WormBase	F28H6.1a; CE18646; WBGene00000103; akt-2. F28H6.1b; CE29298; WBGene00000103; akt-2.
Phylogenomic databases
eggNOG	meNOG06525.
GeneTree	EMGT00050000001097.
HOGENOM	HBG755340.
InParanoid	Q9XTG7.
OMA	PRTISAE.
PhylomeDB	Q9XTG7.
Gene expression databases
ArrayExpress	Q9XTG7.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR011993. PH_type. IPR017892. Pkinase_C. IPR001849. Pleckstrin_homology. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
KO	K04456.
Pfam	PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	914298.

Entry information

Entry name

AKT2_CAEEL

Accession

Primary (citable) accession number: Q9XTG7
Secondary accession number(s): O77145

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	November 1, 1999
Last modified:	November 16, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project