ID G3RIX0_GORGO Unreviewed; 1001 AA.
AC G3RIX0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=PLCL2 {ECO:0000313|Ensembl:ENSGGOP00000015637.3};
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:ENSGGOP00000015637.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000015637.3, 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:ENSGGOP00000015637.3, 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:ENSGGOP00000015637.3}
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-4,5-
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|RuleBase:RU361133};
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DR EMBL; CABD030020075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030020076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030020077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030020078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030020079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3RIX0; -.
DR Ensembl; ENSGGOT00000016085.3; ENSGGOP00000015637.3; ENSGGOG00000016029.3.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000155660; -.
DR HOGENOM; CLU_002738_0_1_1; -.
DR TreeFam; TF313216; -.
DR Proteomes; UP000001519; Chromosome 3.
DR Bgee; ENSGGOG00000016029; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0050811; F:GABA receptor binding; IEA:InterPro.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:InterPro.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16223; EFh_PRIP2; 1.
DR CDD; cd13364; PH_PLC_eta; 1.
DR CDD; cd08597; PI-PLCc_PRIP_metazoa; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR028382; PLCL2_EFh.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF84; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 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 PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 15..125
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 492..608
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 608..737
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 975..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 113630 MW; 27B68F6E4FDC7B47 CRC64;
MPTEKKISSA SDCINSMVEG SELKKVRSNS RIYHRYFLLD ADMQSLRWEP SKKDSEKAKI
DIKSIKEVRT GKNTDIFRSN GISDQISEDC AFSVIYGENY ESLDLVANSA DVANIWVTGL
RYLISYGKHT LDMLESSQDN MRTSWVSQMF SEIDVDNLGH ITLCNAVQCI RNLNPGLKTS
KIELKFKELH KSKDKAGTEV TKEEFIEVFH ELCTRPEIYF LLVQFSSNKE FLDTKDLMMF
LEAEQGVAHI NEEISLEIIH KYEPSKEGRE KGWLSIDGFT NYLMSPDCYI FDPEHKKVCQ
DMKQPLSHYF INSSHNTYLI EDQFRGPSDI TGYIRALKMG CRSVELDVWD GPDNEPVIYT
GHTMTSQIVF RSVIDIINKY AFFASEYPLI LCLENHCSIK QQKVMVQHMK KLLGDKLYTT
SPNVEESYLP SPDVLKGKIL IKAKKLSSNC SGVEGDVTDE DEGAEMSQRM GKENMEQPNN
VPVKRFQLCK ELSELVSICK SVQFKEFQVS FQVQKYWEVC SFNEVLASKY ANENPGDFVN
YNKRFLARVF PSPMRIDSSN MNPQDFWKCG CQIVAMNFQT PGLMMDLNIG WFRQNGNCGY
VLRPAIMREE VSFFSANTKD SVPGVSPQLL HIKIISGQNF PKPKGSGAKG DVVDPYVYVE
IHGIPADCAE QRTKTVHQNG DAPIFDESFE FQINLPELAM VRFVVLDDDY IGDEFIGQYT
IPFECLQTGY RHVPLQSLTG EVLAHASLFV HVAITNRRGG GKPHKRGLSV RKGKKSREYA
SLRTLWIKTV DEVFKNAQPP IRDATDLREN MQNAVVSFKE LCGLSSVANL MQCMLAVSPR
FLGPDNTPLV VLNLSEQYPT MELQGIVPEV LKKIVTTYDM MIQSLKALIE NADAVYEKIV
HCQKAAMEFH EHLHSIGTKE GLKERKLQKA VESFTWNITI LKGQADLLKY AKNETLENLK
QIHFAAVSCG LNKPGTENAD VQKPRRSLEV IPEKANDETG E
//
