ID A0A2K5MB38_CERAT Unreviewed; 1250 AA.
AC A0A2K5MB38;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma {ECO:0000256|PIRNR:PIRNR000952};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000952};
GN Name=PLCG1 {ECO:0000313|Ensembl:ENSCATP00000022431.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000022431.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000022431.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mediates the production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an
CC important role in the regulation of intracellular signaling cascades.
CC {ECO:0000256|PIRNR:PIRNR000952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR AlphaFoldDB; A0A2K5MB38; -.
DR Ensembl; ENSCATT00000046640.1; ENSCATP00000022431.1; ENSCATG00000034738.1.
DR GeneTree; ENSGT00940000158901; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000034738; Expressed in thymus and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd13362; PH_PLC_gamma; 1.
DR CDD; cd13234; PHsplit_PLC_gamma; 1.
DR CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR CDD; cd11970; SH3_PLCgamma1; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016279; PLC-gamma.
DR InterPro; IPR035023; PLC-gamma_C-SH2.
DR InterPro; IPR035024; PLC-gamma_N-SH2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR035724; PLCgamma1_SH3.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10336:SF173; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF000952; PLC-gamma; 3.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000952};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR000952};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR000952};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000952}.
FT DOMAIN 27..142
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 152..187
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 509..616
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 627..715
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 750..810
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 854..890
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 912..1029
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1030..1153
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1231..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000952-1"
FT MOD_RES 1208
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000952-1"
SQ SEQUENCE 1250 AA; 143540 MW; 895A7D456AA73DA2 CRC64;
MAGAASPCAN GCGPGAPSDA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI
TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL
SLQATSEDEV NMWIKGLTWL MEDTLQAPTP LQIERWLRKQ FYSVDRNRED RISAKDLKNM
LSQVNYRVPN MRFLRERLTD LEQRSGDITY GQFAQLYRSL MYSAQKTVHE PPLTFSSCRA
GERPELCRVS LPEFQQFLLD YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT
FLFSKENSVW NSQLDAVLWL LRAHPASSQE GLSDHTLDCW DGPDGMPVIY HGHTLTTKIK
FSDVLQTIKE HAFVASEYPV ILSIEDHCSI AQQRNMAQHF KKVLGDTLLT KPVEISADGL
PSPNQLKRKI LIKHKKLAEG SAYEEVPTSM MYSENDISNS IKNGILYLED PVNHVRTGPV
PLWSIPGMEP AQVWGWASSS TELHSNEKWF HGKLGAGRDG RHIAERLLTE YCIETGAPDG
SFLVRESETF VGDYTLSFWR NGKVQHCRIH SRQDAGTPKF FLTDNLVFDS LYDLITHYQQ
VPLRCNEFEM RLSEPVPQTN AHESKEWYHA SLTRAQAEHM LMRVPRDGAF LVRKRNEPNS
YAISFRAEGK IKHCRVQQEG QTVMLGNSEF DSLVDLISYY EKHPLYRKMK LRYPINEEAL
EKIGTAEPDY GALYEGRNPG FYVEANPMPT FKCAVKALFD YKAQREDELT FTKSAIIQNV
EKQEGGWWRG DYGGKKQLWF PSNYVEEMVN PVALEPEREH LDENSPLGDL LRGVLDVPAC
QIAIRPEGKN NRLFVFSISM ASVAHWSLDV AADSQEELQD WVKKIREVAQ TADARLTEGK
IMERRKKIAL ELSELVVYCR PVPFDEEKIG TERACYRDMS SFPETKAEKY VNKAKGKKFL
QYNRLQLSRI YPKGQRLDSS NYDPLPMWIC GSQLVALNFQ TPDKPMQMNQ ALFMTGRHCG
YVLQPSTMRD EAFDPFDKSS LRGLEPCAIS VEVLGARHLP KNGRGIVCPF VEIEVAGAEY
DSTKQKTEFV VDNGLNPVWP AKPFHFQISN PEFAFLRFVV YEEDMFSDQN FLAQATFPVK
GLKTGYRAVP LKNNYSEDLE LASLLIKIDI FPAKQENGDL SPFSGTSLRE RGSDASGQLF
HGRAREGSFE SRYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL
//
