ID A0A452SMS2_URSAM Unreviewed; 1204 AA.
AC A0A452SMS2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=PLCH2 {ECO:0000313|Ensembl:ENSUAMP00000033943.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000033943.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000033943.1}
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; A0A452SMS2; -.
DR Ensembl; ENSUAMT00000037809.1; ENSUAMP00000033943.1; ENSUAMG00000025867.1.
DR GeneTree; ENSGT00940000158374; -.
DR OMA; NCITCVI; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion 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 CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16221; EFh_PI-PLCeta2; 1.
DR CDD; cd13364; PH_PLC_eta; 1.
DR CDD; cd08633; PI-PLCc_eta2; 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; IPR028393; PLC-eta2_cat.
DR InterPro; IPR046971; PLC-eta2_EFh.
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:SF166; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-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; 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:UP000291022};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 103..211
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 235..263
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 264..300
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 688..801
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 802..931
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 533..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1204 AA; 132530 MW; 96AA57BB0A675660 CRC64;
VGRLAWGPCW TAGDSWANAG GAWEQPCRGL EGLSGGGGRS RREKGGPWSL CDTCHCLTFP
WPSAPSRTGG AVGCLAEALL WVGASVAVSP PWQLGPLVER CMSAMQAGTQ MLKLRGSSKG
LVRFYFLDEH RSCIRWRPSR KNEKAKISID SIQEVSEGRQ SEIFQRYPDG IFDPNCCFSI
YHGSHRESLD LVSPSGDEAR TWVTGLRYLM AGISDEDSLA RRQRTRDQYP WSRGQTFDEA
DKNGDGSLSI GEVLQLLHKL NVNLPRQRVK QMFKEADTDD HQGTLGFEEF CAFYKMMSTR
RDLYLLMLAY SDHKDHLDAA DLQRFLEVEQ KMAGVTLESC RDIIEQFEPC PENKSKGVLG
IDGFTNYTRS PAGDIFNPEH HGVHQDMTRP LSHYFITSSH NTYLVGDQLM SQSRVDMYAW
VLQAGCRCVE VDCWDGPDGE PIVHHGYTLT SKILFKDVIE TINKYAFVKN EYPVILSIEN
HCSVMQQKKM AQYLTGILGD KLDLSSVSSE DATMLPSPQM LKGKILVKGK KLPSSISEDA
EEGEVSDEDS ADEIDEDCKL LNGDVATNRK RVENIAKKKL DSLMKESKIR DCEDPNDFTV
STLPPSGKLG HRAEGRKAEE DVESGEDAGA SRRNNRVLMS GFSKRKKKSS KLKKAASMEE
GEEDLDSQGS QSRGASRQKK TMKLSRALSD LVKYTKSVGM HDVEAEVASS WQVSSFSETR
AQQILQQKPA QYLRFNQHQL SRIYPSSYRV DSSNYNPQPF WNAGCQMVAL NYQSEGRMLQ
LNRAKFSTNG NCGYVLKPQC MCQGVFNPNS EDPLPGQLKK QLVLRIISGQ QLPKPRDSML
GDRGEIIDPF VEVEVIGLPV DCNKEQTRVV DDNGFNPMWE ETLVFTVHMP EIALVRFLVW
DHDPIGRDFI GQRTLAFSSM MPGYRHVYLE GMEEASIFVH VAVSDISGKV KQALGLKGLF
LRGPKPGSLD SHAAGRPLPR PTVSQRLLRR TASAPTKSQK PGRKAFPELV LGTQDTGSEG
EARDVAAPRP GPALEASAPE EPGSRSPRGK APVGRSPAQG SLAQEQPPCA PEGPGPAGMA
ATCMKCVVGS CAGEDAEGLR RGRLPSPGPT AAHEAISQQP RARADSLGVP CTSVGRGRGA
PWQGPGGGSV SSDSSGLGSP EVVPRWPESA HRQAGALQRE MNALFVQKLE EIRSKSSVLS
TVRD
//
