ID A0A2I2ZFQ5_GORGO Unreviewed; 1032 AA.
AC A0A2I2ZFQ5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ENSGGOP00000045902.1};
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:ENSGGOP00000045902.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000045902.1, 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:ENSGGOP00000045902.1, 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:ENSGGOP00000045902.1}
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; A0A2I2ZFQ5; -.
DR STRING; 9593.ENSGGOP00000045902; -.
DR Ensembl; ENSGGOT00000066906.1; ENSGGOP00000045902.1; ENSGGOG00000016029.3.
DR GeneTree; ENSGT00940000155660; -.
DR InParanoid; A0A2I2ZFQ5; -.
DR OMA; MRTSWIS; -.
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:Ensembl.
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:0002322; P:B cell proliferation involved in immune response; IEA:Ensembl.
DR GO; GO:0002337; P:B-1a B cell differentiation; IEA:Ensembl.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
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 46..156
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 523..639
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 639..768
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1006..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 117070 MW; 3C567DA994C48945 CRC64;
TGPVPWCMTC TVAQDGTKQK RERKKTVSFS SMPTEKKISS ASDCINSMVE GSELKKVRSN
SRIYHRYFLL DADMQSLRWE PSKKDSEKAK IDIKSIKEVR TGKNTDIFRS NGISDQISED
CAFSVIYGEN YESLDLVANS ADVANIWVTG LRYLISYGKH TLDMLESSQD NMRTSWVSQM
FSEIDVDNLG HITLCNAVQC IRNLNPGLKT SKIELKFKEL HKSKDKAGTE VTKEEFIEVF
HELCTRPEIY FLLVQFSSNK EFLDTKDLMM FLEAEQGVAH INEEISLEII HKYEPSKEGR
EKGWLSIDGF TNYLMSPDCY IFDPEHKKVC QDMKQPLSHY FINSSHNTYL IEDQFRGPSD
ITGYIRALKM GCRSVELDVW DGPDNEPVIY TGHTMTSQIV FRSVIDIINK YAFFASEYPL
ILCLENHCSI KQQKVMVQHM KKLLGDKLYT TSPNVEESYL PSPDVLKGKI LIKAKKLSSN
CSGVEGDVTD EDEGAEMSQR MGKENMEQPN NVPVKRFQLC KELSELVSIC KSVQFKEFQV
SFQVQKYWEV CSFNEVLASK YANENPGDFV NYNKRFLARV FPSPMRIDSS NMNPQDFWKC
GCQIVAMNFQ TPGLMMDLNI GWFRQNGNCG YVLRPAIMRE EVSFFSANTK DSVPGVSPQL
LHIKIISGQN FPKPKGSGAK GDVVDPYVYV EIHGIPADCA EQRTKTVHQN GDAPIFDESF
EFQINLPELA MVRFVVLDDD YIGDEFIGQY TIPFECLQTG YRHVPLQSLT GEVLAHASLF
VHVAITNRRG GGKPHKRGLS VRKGKKSREY ASLRTLWIKT VDEVFKNAQP PIRDATDLRE
NMQNAVVSFK ELCGLSSVAN LMQCMLAVSP RFLGPDNTPL VVLNLSEQYP TMELQGIVPE
VLKKIVTTYD MMIQSLKALI ENADAVYEKI VHCQKAAMEF HEHLHSIGTK EGLKERKLQK
AVESFTWNIT ILKGQADLLK YAKNETLENL KQIHFAAVSC GLNKPGTENA DVQKPRRSLE
VIPEKANDET GE
//
