ID A0A2K5EK13_AOTNA Unreviewed; 831 AA.
AC A0A2K5EK13;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-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=PLCD1 {ECO:0000313|Ensembl:ENSANAP00000033563.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000033563.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000033563.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR AlphaFoldDB; A0A2K5EK13; -.
DR STRING; 37293.ENSANAP00000033563; -.
DR GlyCosmos; A0A2K5EK13; 2 sites, No reported glycans.
DR Ensembl; ENSANAT00000051622.1; ENSANAP00000033563.1; ENSANAG00000034450.1.
DR GeneTree; ENSGT00940000158392; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; 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:0046488; P:phosphatidylinositol metabolic process; IEA:Ensembl.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16217; EFh_PI-PLCdelta1; 1.
DR CDD; cd13363; PH_PLC_delta; 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; 3.
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; IPR046975; PLC-delta1_EF.
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:SF80; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-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; 2.
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; 2.
DR PROSITE; PS50222; EF_HAND_2; 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 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:UP000233020};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 42..151
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 567..684
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 684..812
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 395..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92951 MW; 0239558B01480A4C CRC64;
MQCLGIRSRS RSRELYLQEQ SLKVAALNGQ RLGLQDDKDL QALLKGSQLL KVKSSSWRRE
RFYKLQEDCK TIWQESRKVM RTPESQLFSI EDIQEVRMGR RTEGLEKFAR DVPEDRCFSI
VFKDQRNTLD LIAPSPADAQ HWVLGLRKII HHSGSMDQRQ KLQHWIHSCL RKADKNKDNK
MSFKELQNFL KELNIQVDDS YARKIFRECD RSQTDSLEDE EIEAFYKMLT QRAEIDRTFA
EAAGSGETLS VDQLVAFLRH QQREEAAGPA LALSLIERYE PSETAKAQRQ MTKDGFLMYL
LSADGSAFSL AHRRVYQDMG QPLSHYLVSS SHNTYLLEDQ LTGPSSTEAY IRCCPRKPWG
GSLGGTQDRT WRVLAATLPT GHCAKAAAAW SWTAGTGPTR NPSSTMATLS LPRSSSATCS
GPSGTTPSRW ACPWPARSGL LGVASPPNVP LGLQASPYPV ILSLENHCTL EQQRVMARHL
HGILGPMLLN RPLDGVTNSL PSPEQLKGKI LLKGKKLGGL LPPGGEGGPE ATVVSDEDEA
AEMEDEAVRS RVQHKPKEDK LRLAQELSDM VIYCKSVHFG GFSSPGTPGQ AFYEMASFSE
NRALRLLQES GNSFVRHNVG RLSRIYPAGW RTDSSNYSPV EMWNGGCQIV ALNFQTPGPE
MDVYQGRFQD NGACGYVLKP AFLRDPNATF NPRALAQGPW WARKRLNIRV ISGQQLPKVN
KNKNSIVDPK VTVEIHGVSR DVASRQTAVI TNNGFNPWWD TEFAFEVVVP DLALVRFVVE
DYDASSKNDF IGQSTIPLNS LKQGYRHVHL LSKNGDQHPS ATLFVKISLQ D
//
