ID A0A1V4KLZ9_PATFA Unreviewed; 1467 AA.
AC A0A1V4KLZ9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN Name=PLCH1 {ECO:0000313|EMBL:OPJ85458.1};
GN ORFNames=AV530_001686 {ECO:0000313|EMBL:OPJ85458.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ85458.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ85458.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ85458.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ85458.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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|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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ85458.1}.
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DR EMBL; LSYS01002834; OPJ85458.1; -; Genomic_DNA.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050429; F:calcium-dependent phospholipase C activity; 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 CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16220; EFh_PI-PLCeta1; 1.
DR CDD; cd13364; PH_PLC_eta; 1.
DR CDD; cd08632; PI-PLCc_eta1; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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 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; IPR028392; PLC-eta1_cat.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR046972; PLCeta1_EF.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF51; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF13499; EF-hand_7; 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; SM00054; EFh; 2.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 113..147
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 161..196
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 197..233
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 622..734
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 736..864
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 551..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1467 AA; 163947 MW; 8BB7193C74EC6077 CRC64;
MNCCLMVIID VNEIQVTNLM ADLEVYKNLS PEKVERCMSV MQSGTQMVKL KSGTKGLVRL
FYLDEHRTCI RWRPSRKSEK AKIVIDSIYK VTEGRQSEIF HRHAEGNFDP SCCFTIYHGS
HMESLDLITS NPEEARTWIT GLKYLMAGIS DEDSLAKRQR THDHWVKQTF EEADKNGDGL
LNIEEIHQLM HKLNVNLPRR KVRQMFQEAD TDENQGTLNF EEFSVFYKMM SLRRDLYLLL
LSYSDKKDHL TVEELAQFLK VEQKMNNVTP EYCLDIIQKF EVSEENKKQN VLGIEGFTNF
MRSPACDVFN PLHCEVHQDM DQPLCNYFIA SSHNTYLTGD QLLSQSRAEM YARVLQDGCR
CIEVDCWDGP DGEPVVHHGY TLTSKILFRD VAETINKYAF IKNEFPVILS IENHCSIQQQ
QKIAQYLKEI FGDKLDLSSV ITGDSRQLPS PQNLKGKILV KGKKLPHTLG ADAEEGEVSD
EDSADEIEDD CKLKPCYSNG ATEHQVESFI RTKLESLIKE SQIRDKEDPD SFTVRALLKA
THEGLNVNLK QNLDTKEGGK KSHSRSLMGN FGKHKKAVKA TSKYHSTSDD EENQHNPSGR
ETGQLHSRLA RRRKTVKLCR ALSDLVVYTN SVAAQDIVDD GSTGNVLSFS ETRAHQAVQQ
KAEQFMLYNQ KQLTRVYPSA YRIDSSNFNP LPYWNVGCQL VALNYQSEGR VMQLNDAKFR
VNGNCGYVLK PQQMCKGTFN PYSADPLPAS PKKQLILKII SGQQLPKPPD SMLGDRGEII
DPFVEVEIIG LPVDCCKDQT RVVDDNGFNP VWEETLTFTV HMPEIALVRF LVWDHDPIGR
DFVGQRTLAF SSLVPGYRHV YLEGLTEASI FVHITINEIY GKNKQLIGLR GLFNKNSKHN
SAETSGHYIR KRSIGDRILR RTASAPAKGR KKSKMGFLEA AEIKDSASEP VDLKDKEGVV
RRTSRTLQAR PASMPVDKYL LVGLPCPEGE TAHDAKGKEN TSANSDDNTN EKETNSKDSG
FACSEKTANT SNLASQFKKN DQKKPTVDSL VPSLQEQPAH LVFARGGAET NHLPGHQEKN
PSGETVPLMQ GSDFDISTEK TNDKTCAHNK KEGDTKGSKE EKITFTRTSL SQKVEMGNPK
NDTIKKSTAA ALALTGISSD VPSDVPDLHS TLTMQDSDIS RLIDEVSLAN ESEMDSAVSA
LIGQVDVTDP KRKHGTSWEA PESTSSFASN SLIFEETLVD PLIGDNSESS SLVELDGDSR
ELLVTVCEYK REDMSQLASP LKLRHKQDAG LDKQKNIMCT SQRSQLNTHS PMLKTTLAFP
SPSAIKQTSP CKSKSLGDLT SEDISCNFEN ALTEQLRKLV SLEQEDGGHA RCPRQAEEDC
PRALVRKLSS RSQSRVRNIA SRAKERQEAA GKHRAPNASS VAGVVLRNKP SASPHVVNRH
STGSYIASQG MTGNTLKNEA GYRTGAA
//
