P3C2G_RAT
ID P3C2G_RAT Reviewed; 1505 AA.
AC O70173;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma {ECO:0000305|PubMed:9516481};
DE Short=PI3K-C2-gamma;
DE Short=PtdIns-3-kinase C2 subunit gamma;
DE EC=2.7.1.137 {ECO:0000269|PubMed:9516481};
DE EC=2.7.1.154 {ECO:0000269|PubMed:9516481};
DE AltName: Full=Phosphoinositide 3-kinase-C2-gamma;
GN Name=Pik3c2g;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Regenerating liver;
RX PubMed=9516481; DOI=10.1074/jbc.273.13.7731;
RA Ono F., Nakagawa T., Saito S., Owada Y., Sakagami H., Goto K., Suzuki M.,
RA Matsuno S., Kondo H.;
RT "A novel class II phosphoinositide 3-kinase predominantly expressed in the
RT liver and its enhanced expression during liver regeneration.";
RL J. Biol. Chem. 273:7731-7736(1998).
CC -!- FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as
CC second messengers (PubMed:9516481). May play a role in SDF1A-stimulated
CC chemotaxis (By similarity). {ECO:0000250|UniProtKB:O70167,
CC ECO:0000269|PubMed:9516481}.
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:0000269|PubMed:9516481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000305|PubMed:9516481};
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:0000269|PubMed:9516481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000305|PubMed:9516481};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9516481}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9516481}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in normal liver. High
CC levels also found in regenerating liver. Very low levels found in heart
CC and testis. {ECO:0000269|PubMed:9516481}.
CC -!- DEVELOPMENTAL STAGE: Higher levels of expression found in adult liver
CC than in fetal liver. {ECO:0000269|PubMed:9516481}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
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DR EMBL; AB009636; BAA25634.1; -; mRNA.
DR RefSeq; NP_446375.1; NM_053923.1.
DR AlphaFoldDB; O70173; -.
DR SMR; O70173; -.
DR STRING; 10116.ENSRNOP00000043855; -.
DR PhosphoSitePlus; O70173; -.
DR PaxDb; O70173; -.
DR PRIDE; O70173; -.
DR GeneID; 116720; -.
DR KEGG; rno:116720; -.
DR UCSC; RGD:620231; rat.
DR CTD; 5288; -.
DR RGD; 620231; Pik3c2g.
DR eggNOG; KOG0905; Eukaryota.
DR InParanoid; O70173; -.
DR PhylomeDB; O70173; -.
DR BRENDA; 2.7.1.137; 5301.
DR BRENDA; 2.7.1.154; 5301.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-1660514; Synthesis of PIPs at the Golgi membrane.
DR PRO; PR:O70173; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:UniProtKB.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; ISO:RGD.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.1520.10; -; 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; 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; PTHR10048; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 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 1: Evidence at protein level;
KW ATP-binding; Chemotaxis; Kinase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..1505
FT /note="Phosphatidylinositol 3-kinase C2 domain-containing
FT subunit gamma"
FT /id="PRO_0000088801"
FT DOMAIN 278..370
FT /note="PI3K-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT DOMAIN 540..688
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 703..879
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 948..1226
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 1259..1371
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 1384..1505
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..960
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1090..1098
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1109..1135
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 13..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 170975 MW; 5ED4C2239968C4B2 CRC64;
MAYNWQTEPN RAEPQEGGHD HQQCHHADQH LSSRQVRLGF DQLVEELSNK TPLPEDEKEG
TCFVPDTPNL DSKWQSIYGP HPRHFNEFTS QSPHFSQLPF GKASAIGFNP AVLPAHQFIH
EGASWRNPTR KYHGGEDPRF SALTPSSTGL DKCHQQGQSG TEHCNYYVEP ENNVPHHYSP
YSMDSIPDSE EKGSGDADLV EPSLVFSKDS FLPRASENMS VESTEPIGCP LEIVEAPQGS
NKSLASFCNN VTKIRGLYHA SDTNSNSGKI WAITTAYPSR LFADTQFRVK ISTDNSAQLL
LLKPPANYLV KDLIAEILLL CANEQLSPKE YLLSICGSEE FLQTDHCLGS HKIFQKSKSV
IQLHLQRSRD TPGKLSRKRD DDRSRVHLNQ LLEFTHIWKI SRQCLSTVMK SYNLHVEHLL
KTQEDVEEKP LSSMFSCGRH PPQPHGNDII EDVRNICSVL GCIETKQVSD AVKELTLILQ
RPSQNFHQNS ETSKKGFIEN VTSELSRSLH QLVDVYCSSF CTDFRPARAP GGVSRDHAGL
HSHLSFTVCS LHNVPETWAH SYKAFSFSCW LTYAGKKLCQ VKSCRSLPVT KSFSFSVNWN
EIINFPLEIK SLPRESMLVI KLFGIDSATH SANLLAWTCL PLFPKEKSPL GSRLLSMTLQ
SEPPIEMMAP GVWDGSQPTP LTLQIDFPAA TWEYVKPETE ENRTDHQEPP RECLKHIARL
SQKQPPLLLS VEKRRYLWFY RFYCNNENSS LPLVLGSAPG WDEGTVSEMH AVLRRWTFSH
PLEALGLLTS RFPDQDIREV AVQQLDNFLT DELLDCLPQL VQAVKFEWSL ESPLVELLLH
RSLQSIRVAH RLFWLLRDAQ GEDYFKSWYQ ELLAALQFCA GEALIEELSK EQKLVKLLGD
IGEKVKSAGD AQRKDVLKKE IGSLEEFFKD IKTCHLPLNP ALCVKGIDRD ACSYFTSNAL
PLKITFINAN PMGKNISVIF KAGDDLRQDM LVLQIIQVMD NVWLQEGLDM QMIIYGCLAT
GKAQGFIEMV PDAVTLAKIH LHSGLIGPLK ENTIKKWFSQ HNHLKEDYEK ALRNFFYSCA
GWCVVTFILG VCDRHNDNIM LTKSGHMFHI DFGKFLGHAQ TFGGIKRDRA PFIFTSEMEY
FITEGGKNTQ HFQDFVELCC RAYNIVRKHS QLLLSLLEMM LHAGLPELRG IEDLKYVHDN
LRPQDTDLEA TSHFTTKIKQ SLECFPVKLN NLIHTLAQMP AFSLARPAPQ TPPQECCVLN
KTRTIQRVTI LGFSKTHSNL YLIEVTRSDN RKNLAKKSFE QFYRLHSQIQ KQFPLLTLPE
FPHWWHLPFT DSHHERIRDL SHYVEQVLHG SYEVANSDCV LSFFLSEHIQ QTLEDSPFVD
PGDHSPDKSP QVQLLMTYED TKLTILVKHL KNIHLPDGSA PSAHVEIYLL PHPSEVRRKK
TKCVPKCTDP TYNEIVVYDD VSGLQGHVLM LIVKSKTVFV GAVNIQLCSV PLNEEKWYPL
GNSII
