AGE1_CAEBR
ID AGE1_CAEBR Reviewed; 1159 AA.
AC P0C5E7; A8WTC1; Q620C1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Phosphatidylinositol 3-kinase age-1;
DE Short=PI3-kinase age-1;
DE Short=PI3K age-1;
DE Short=PtdIns-3-kinase age-1;
DE EC=2.7.1.137;
DE AltName: Full=Aging alteration protein 1;
GN Name=age-1; ORFNames=CBG02868;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog that regulates
CC longevity and diapause. Promotes cell survival during embryonic
CC development by recruiting akt-1/2 to the plasma membrane through the
CC production of PtdIns(3,4,5)P3. Could function in the development or
CC neuroendocrine signaling of the dauer pathway. Mediates susceptibility
CC to enteropathogenic E.coli infection. May negatively regulate AYI
CC interneuron neurite outgrowth. Plays a role in aversive olfactory
CC learning when an odor is associated with food deprivation. Regulates
CC this process by promoting the nuclear relocalization of egl-4 in AWC
CC olfactory neurons after odor conditioning.
CC {ECO:0000250|UniProtKB:Q94125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00877, ECO:0000255|PROSITE-ProRule:PRU00879,
CC ECO:0000255|PROSITE-ProRule:PRU00880}.
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DR EMBL; HE601438; CAP23732.2; -; Genomic_DNA.
DR AlphaFoldDB; P0C5E7; -.
DR SMR; P0C5E7; -.
DR STRING; 6238.CBG02868; -.
DR WormBase; CBG02868; CBP43879; WBGene00025837; Cbr-age-1.
DR eggNOG; KOG0904; Eukaryota.
DR HOGENOM; CLU_002191_1_3_1; -.
DR InParanoid; P0C5E7; -.
DR OMA; HANILHP; -.
DR OrthoDB; 204282at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0040024; P:dauer larval development; ISS:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR003113; PI3K_ABD.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51544; PI3K_ABD; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..1159
FT /note="Phosphatidylinositol 3-kinase age-1"
FT /id="PRO_0000304611"
FT DOMAIN 79..179
FT /note="PI3K-ABD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00877"
FT DOMAIN 272..363
FT /note="PI3K-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT DOMAIN 430..588
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 607..793
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 858..1159
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..870
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1028..1036
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1047..1073
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 133936 MW; 8D8D16AEF6CEFA08 CRC64;
MSMGRSSSTT FRNRTASHGS RSLGSAETAR IPRKLSSQLS HTHANILHPQ LQTMMEQWQM
RERPSLETEN GKGSLLLSSE GVADMIVLSS FGEVISVVFP WFLANVRTSF DIKLSEFKHQ
LFEQIGPMKW GKHSTQPQDY AFRQLNNFGE IEVIFNDDQQ LSCLELHGTF PMLFLFEPDG
FNRDKELMCD ISHCLGYSLD KLEESIDEEL RQFRASLWTQ TKKTCFERGV DGVDHYAFPE
EQYFCVGEKC PTDLESKVKA AKLDYQLFWT KRKSEANEVW EKMYKITIDF DPEFNPQSLM
RMFVKELQCM NLFDPEDPPD EEWILQLAGR TSFVTRPEIS LVSYDGIRSE LESYRCPGFV
VRRKSLVLKD YVRPKPLYEP HYVRVHERKM ALDVLSVSIG TEVKHSGNSD KVWTDFRPTA
SLEQITLWDL DSNLMIRPVN VTGLPFTASH DIYLGMEFKV YVGTLTLATI KIPRVPTTKL
VWKREFFTFD LYMKDMPPSA ILSVRVYSMK TTKMKEEIEL GWVNISLSDW RDELRQGQIK
LNLWGPEPSA NRSRIGHNGA KIGTSLSVTV EISSHGRRVK MPNEAQYKYL VDHRISWSDT
VEIVGDDYEA CIGDPGYKKL QDLVKKHESG VILDDSEQRH VWSWRNYIQK QEPDLLVVLS
ELRIVWTDRE NFSELYVMLE TWKAPSVAAA LTLLGKRCTD RVIRKFAVNK LNDQLSQFNV
HLFLLPLIQA LKYEPRAYSE VGMMLLTRAL SSYRIGHRLF WLLRSEICRL KDCATNNEEY
RRISLLMEAY LRGNEEHIKG IIRQVDMVDE LTRISSLVKG LSKEAAREKL RDQLRTISHK
MESIDSPLDP VYKFGEMVIE KAIVLGSAKQ PLRLVWKNKN PKSDLHLPFC EVIFKNGDDL
RQDMLVLQVL EVMDTIWKAA NIDCCLSPYG VLPMGEMIGI IEVVPNCKTI FEIQHKAGLV
NTAARSVDSN FMNKWIRKQC GFVDEKKKYK KGGGPTVDSA QATKKYFESV DRFLYSCVGY
SVATYIMGIK DRHSDNLMLT EDGKYFHIDF GHILGHGKTK LGIQRDRQPF ILTEQFLTII
RSGKPVDGNS HEIQKFKTLC LEAYEVMWNN LKYKFQKTLC CKGETKEKAR KFFAGVYEEA
FNGSWSTKTN WLFHAMKHY
