ID G3RLT6_GORGO Unreviewed; 1445 AA.
AC G3RLT6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 gamma {ECO:0000313|Ensembl:ENSGGOP00000016747.3};
GN Name=PIK3C2G {ECO:0000313|Ensembl:ENSGGOP00000016747.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000016747.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000016747.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000016747.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000016747.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
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; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABD030083097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030083098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030083099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030083100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030083101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030083102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000017218.3; ENSGGOP00000016747.3; ENSGGOG00000017159.3.
DR GeneTree; ENSGT00940000159982; -.
DR HOGENOM; CLU_002191_2_0_1; -.
DR Proteomes; UP000001519; Chromosome 12.
DR Bgee; ENSGGOG00000017159; Expressed in liver and 1 other cell type or tissue.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd05177; PI3Kc_C2_gamma; 1.
DR CDD; cd06896; PX_PI3K_C2_gamma; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
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; IPR037707; PI3K-C2-gamma_dom.
DR InterPro; IPR002420; PI3K-type_C2_dom.
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; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF29; PHOSPHATIDYLINOSITOL 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT GAMMA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 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; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 285..371
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 482..628
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 643..819
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 888..1166
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1199..1311
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1328..1445
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1445 AA; 165580 MW; 41983239B3329E56 CRC64;
MAYSWQTDPN PNESHEKQYE HQEFLFVNQP HSSSQVSLGF DQIVDEISGK IPHCESEIDE
NTFFVPTAPK WDSTGHSLNE AHQISLNEFT SKSHELSWHQ VRKAPAIGFS PSMLPKPQNM
NKECSWGSPI GKHHGADDSR FSILAPSFTS LDKINLEKEL ENENHNYHIG FESSIPPTNS
SFSSDFMPKE ENKRSGHVNI VEPSLILLQG SLQPGMWEST WRKNIESIGC SIQLVEVPQS
SNTSLASFCN KVKKIREGYH AADVSFNSGK IWSTTTAFPY QLFSKTKFNI HIFIDNSTQP
LHFMPCANYL VKDLIAEILH FCTNDHLLPK DHILSVCGSE EFLQNDHCLG SHKMFQKDKS
VIQLHLQKSR EAPGKLSRKH EEDHSQFYLN QLLEFMHIWK VSRQCLLTLI RKYDFHLKYL
LKTQENVDNI IEEVKKICSV LGCVETKQIT DAVNELSLIL QRKAENFYQS SETSAKGLIE
KVTTELSTSV YQLINVYCNS FYADFQPVNV PRCISYLNPG LPSHLSFTVY AAHNIPETWV
HRINFPLEIK SLPRESMLTV KLFGIACATN NANLLAWTCL PLFPKEKSIL GSMLFSMTLQ
SEPPVEMIAP GVWDVSQPSP VTLQIDFPAT GWEYMKPDSE ENRSNLEEPL KECIKHIARL
SQKQTPLLLS EEKKRYLWFY RFYCNNENCS LPLVLGSAPG WDERTVSEMH TILRRWTFSQ
PLEALGLLTF SFPDQEIRKV AVQQLDNLLN DELLEYLPQL VQAVKFEWNL ESPLVQLLLH
RSLQSIQVAH RLYWLLKNAE NEAYFKSWYQ KLLAALQFCA GKALNDEFSK EQKLIKILGD
IGEKVKSASD HQRQEVLKKE TGRLEEFFQD VNTCHLPLNP ALCIKGIDHD ACSYFTSNAL
PLKITFINAN PMGKNISIIF KAGDDLRQDM LVLQIIQVMD NIWLQEGLDM QMIIYRCLST
GKDQGLVQMV PDAVTLAKIH RHSGLIGPLK ENTIKKWFSQ HNHLKADYEK ALRNFFYSCA
GWCVVTFILG VCDRHNDNIM LTKSGHMFHI DFGKFLGHAQ TFGGIKRDRA PFIFTSEMEY
FITEGGKNPQ HFQDFVELCC HAYNIIRKHS QLLLNLLEMM LYAGLPELSG IQDLKYVYNN
LRPQDTDLEA TSHFTKKIKE SLECFPVKLN NLIHTLAQMS AISPAKSTSQ TFPQESCLLS
TTRSIERATI LGFSKKSSNL YLIQVTHSNN KTSLIEKSFE QFSKLHSQLQ KQFASLTLPE
FPHWWHLPFT NSDHRRFRDL NHYMEQILNG SHEVTNSDCV LSFFLSEAVQ QTVEESSLVY
LGEKFPDKKP KVQLVISYED VKLTILVKHM KNIHLPDGSA PSAHVEFYLL PYPSEVRRRK
TKSVPKCTDP TYNEIVVYDE VTELQGHVLM LIVKSKTVFV GAINIRLCSV PLNEEKWYPL
GNSII
//
