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Database: UniProt
Entry: W5Q1Q6_SHEEP
LinkDB: W5Q1Q6_SHEEP
Original site: W5Q1Q6_SHEEP 
ID   W5Q1Q6_SHEEP            Unreviewed;      1005 AA.
AC   W5Q1Q6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 60.
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:ENSOARP00000016644.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000016644.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000016644.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000016644.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000016644.1}
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|ARBA:ARBA00023674};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
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DR   EMBL; AMGL01012655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01012664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5Q1Q6; -.
DR   SMR; W5Q1Q6; -.
DR   STRING; 9940.ENSOARP00000016644; -.
DR   PaxDb; 9940-ENSOARP00000016644; -.
DR   Ensembl; ENSOART00000016881.1; ENSOARP00000016644.1; ENSOARG00000015517.1.
DR   eggNOG; KOG0169; Eukaryota.
DR   HOGENOM; CLU_002738_0_1_1; -.
DR   OMA; MRTSWIS; -.
DR   Proteomes; UP000002356; Chromosome 1.
DR   Bgee; ENSOARG00000015517; Expressed in longissimus thoracis muscle and 55 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|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          32..142
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          509..625
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          625..754
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..1005
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  113729 MW;  DD87AC8F2E6F1FAC CRC64;
     DGSKQKRERK KTVSFSSMPT EKKISSASDC ISAMVEGSEL KKVRSNSRIY HRYFLLDADM
     QSLRWEPSKK DSEKAKIDIK SIKEVRTGKN TDIFRSNGVS DQISEDCAFS VIYGENYESL
     DLVANSADVA NIWVTGLRYL ISYGKHTLDM LESSQDNMRT SWVSQMFSEI DVDNLGHITL
     CSAVQCIRNL NPGLKTSKIE LKFKELHKSK DKTGTDVTKE EFVEVFHELC TRPEIYFLLV
     QFSSNKEFLD TKDLMMFLEA EQGVAHINEE ISLEIIHKYE PSKEGQEKGW LSIDGFTNYL
     MSPDCYIFDP EHKKVCQDMK QPLSHYFINS SHNTYLIEDQ FRGPSDITGY IRALKMGCRS
     VELDVWDGPD NEPVIYTGHT MTSQIVFRSV IDIINKFAFF ASEYPLILCL ENHCSIKQQK
     VMVRHMKKIL GDKLYTASPN VEESYLPSPD VLKGKILVKA KKLSSSCSGV EGDVTDEDEG
     AEMSQRMGKE STELPNHLPA KRFQLCKELS ELVSICKSVQ FKEFQVSFQA QKYWEVCSFN
     EVLASKYANE NPGDFVNYNK RFLARVFPSP MRIDSSNMNP QDFWKCGCQI VAMNFQTPGL
     MMDLNVGWFR QNGNCGYVLR PAIMREEVSF FSANTKDSVP GVSPQLLHIK VISGQNFPKP
     KGSGAKGDVV DPYVYVEIHG IPADCAEQRT RTVHQNGDAP IFDESFEFQV NLPELAMVRF
     VVLDDDYIGD EFIGQYTIPF ECLQTGLAHA SLFVHVAITN RRGGGKPHKR GLSVRKGKKS
     REYASLRTLW IKTVDEVFKN AQPPIRDATD LRENMQNAVV SFKELCGLSS VANLMQCMLA
     VSPRFLGPDN TPLVVLNLSE QYPTMELQGI VPEVLKKIVT TYDMMIQSLK ALIENADAVY
     EKIVHCQKAA MEFHEHLQSI GTREGLKERK LQKAVESFTW NITILKGQAD LLKYAKNETV
     ENLKQIHYAA VSCGLNKPGT ENADAPKPRR SLEVIPEKAN DETGA
//
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