ID A0A091VYW9_NIPNI Unreviewed; 1017 AA.
AC A0A091VYW9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
DE Flags: Fragment;
GN ORFNames=Y956_07504 {ECO:0000313|EMBL:KFQ94788.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ94788.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ94788.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ94788.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL410237; KFQ94788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VYW9; -.
DR STRING; 128390.A0A091VYW9; -.
DR eggNOG; KOG0169; Eukaryota.
DR Proteomes; UP000053283; Unassembled WGS sequence.
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 CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16222; EFh_PRIP1; 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; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF102; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 1; 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; 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:UP000053283};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 507..623
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 623..752
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ94788.1"
FT NON_TER 1017
FT /evidence="ECO:0000313|EMBL:KFQ94788.1"
SQ SEQUENCE 1017 AA; 114970 MW; 79744EFF9C2360E1 CRC64;
IPQDPSNQKC GRKKTVSFSS MPSEKKISSA SDCISFMQAG CELKKVRPNS RIYNRFFTLD
PDLQALRWEP SKKDLEKAKL DISAIKEIRL GKNTETFRNN GLADQISEDC ALSVIHGENY
ESLDLVANSA DVANIWVSGL RYLVSRSKQP LDLMESSHNT PRFAWLKTVF EAADVDGNGI
MLEDTSVELI KKLNPTLKES KIRLKFKEIQ KSKEKLTTRV TKEEFCEAFS ELCTRPEVYF
LLVQISKNKE YLDANDLMLF LEAEQGVTHI TEEMCLDIIR RYELSQEGRL KGFLAIDGFT
QYLLSPECDI FDPEHKKIVQ DMTQPLSHYY INASHNTYLI EDQLRGPADI NGYVRALKMS
CRSIELDVCD GPDNEPIICN RNNMTSPLAF RNVIEVINKL AFFASEYPLI LCLGNHCSVQ
QQKVMVQHMK RIFGNKLYTE APLSSEVYLP SPEKLKMKII VKGKKLPCDQ DILEGEVTDE
DEEAEISRRL SEDFSREPKL IWLCRELSDL VSLCKSVQYK DFETSMKAQN YWEMCSFSEA
EASRIANEYP EDFVNYNKKF LSRVYPSAMR IDSSNLNPQD FWNCGCQIVA MNYQTPGPMM
DLHTGWFLQN GGCGYVLRPS VMRDEVSYFS ANTKGIVPGV SPQVLHVKII SGQNFPKPKG
ACAKGDVIDP YVCIEIHGIP ADCTEQRTKT VQQNSDNPIF DESFEFQINL PELAMIRFVV
LDDDYIGDEF IGQYTIPLEC LQPGYRHIPL RSFVGDVMEH VTLFVHIAIT NRSGGGKAQK
RSLSVRIGKK AREYTMLRNT GLKTIDDIFK LAVHPLREAT DMRENMQNAM VSVKELCGLP
PIASLKQCIL TLSSRLVSSD NAPSVTLCMK DAFPYLEPLG TVPDVQKKVL AAYDLMIQES
RVLIETADIT HDKIVQCQKA GMEFHEELHN LGTKEGLKGR KLSKAIESFA WNITVLKGQG
DLLKNAKNEA LENMKQIQLA CLSCGLSKTG SGHVDAKSKR CLEAIQEKDT GDENGRL
//