ID A0A2K6PDY0_RHIRO Unreviewed; 1655 AA.
AC A0A2K6PDY0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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|Ensembl:ENSRROP00000014772.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000014772.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000014772.1}
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 RefSeq; XP_010379599.1; XM_010381297.1.
DR Ensembl; ENSRROT00000038904.1; ENSRROP00000014772.1; ENSRROG00000031577.1.
DR GeneTree; ENSGT00940000157185; -.
DR Proteomes; UP000233200; Unplaced.
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; 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; 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:UP000233200};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 2..110
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 124..159
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 160..196
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 583..695
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 697..825
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 508..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1655 AA; 185039 MW; 8ACB07C032566565 CRC64;
MSVMQSGTQM IKLKRGSKGL VRLFYLDEHR TRLRWRPSRK SEKAKILIDS IYKVTEGRQS
EIFHRQAEGN FDPSCCFTIY HGNHMESLDL ITSNPEEART WITGLKYLMA GISDEDSLAK
RQRTHDQWVK QTFEEADKNG DGLLNIEEIH QLMHKLNVNL PRRKVRQMFQ EADTDENQGT
LTFEEFCVFY KMMSLRRDLY LLLLSYSDKK DHLTVEELAQ FLKVEQKMNN VTTDYCLDII
KKFEVSEENK VKNVLGIEGF TNFMRSPACD VFNPLHHEVY QDMDQPLCNY YIASSHNTYL
TGDQLLSQSK VDMYARVLQE GCRCVEVDCW DGPDGEPVVH HGYTLTSKVL FRDVVETINK
HAFVKNEFPV ILSIENHCSI QQQRKIAQYL KGIFRDKLDL SSVDTGECKQ LPSPQSLKGK
ILVKGKKLPY HLGDDAEEGE VSDEDSADEI EDECKFKLHY NNGTTEHQVE SFIRKKLESL
LKESQIRDKE DPDSFTVRAL LKATHEGLNA HLKQSPDVKE SGKKSHGRSL MTNFGKHKKT
TKSRSKSYST DDEEDTQQNT VKEGGQLYRL GRRRKTMKLC RELSDLVVYT NSVAAQDIVD
DGTTGNVLSF SETRAHQVVQ QKSEQFMIYN QKQLTRIYPS AYRIDSSNFN PLPYWNAGCQ
LVALNYQSEG RMMQLNRAKF KTNGNCGYVL KPQQMCKGTF NPFSGDPLPA NPKKQLILKV
ISGQQLPKPP DSMFGDRGEI IDPFVEVEII GLPVDCCKDQ TRVVDDNGFN PVWEETLTFT
VHMPEIALVR FLVWDHDPIG RDFVGQRTVT FSSLVPGYRH VYLEGLTEAS IFVHITINEI
YGKNRQLQGL KGLFNKNPRH SSAENNSHYV RKRSIGDRIL RRTASAPAKG RKKSKMGFQE
MVEIKDSVSE ATRDQDGVLR RTTRSLQARP VSMPVDRNLL GALSLPVSET AKDVEGKENS
LAEDKDGRRK GKASIKDPHF LNFNKTLSSS SSALLHKDII QGDAIVSTAH MSVTGEQLGV
SSPRGGRTTS NATSNCQENP CPNKSLSPRQ HLAPDPVVNP TQDLHGVKIK EKRNAEGFVE
GKSILPGSIL SHSNLEIKNL EVNRGKGRAA TSFSLSDVSM LCSDIPDLHS TAILQESEIS
HLIDNVTLTN ENEPGSSISA LIGQFDETND QALTVVSHLH NTSVMSGHCP LPSLGLKMPI
KHGFSKGKSK SSFLCSSPEL IALSSPETTK HATNTVYETT CTPISKTKPD DDLSSKAQTG
AIESNLPGSP NTSHDWLPKS PTKGEDWETL KSCSPASSPD LTLEDVIADP TLCFNSGESS
LVEIDGESEN LSLTTCEYRR ESTSQLASPL KLKYSQGVVE HFQRGLRNGY CKETHHPSVP
EIFNSIQDVK TQSISYLAYQ GAGFVHNHFS DSDAKIFQTC VPQQSSAQDM HVPVPKQLAH
LPLPALKLPS PCKSKSLGDL TSEDIACNFE SKYQCISKSF ITTGIKDKKG VTVKTKSLEP
IDALTEQLRK LVSFDQEDSC QVIYSKQDAN QLPRALVRKL SSRSQSRVRN IASRAKEKQE
ANKQKVPNPS NGAGVVLRNK PSAPTPAVNR HSTGSYIAGY LKNTKGGGLE GRGIPEGACT
ALHYGHVDQL CSDNSVLQTE PSSDDKPEIY FLLRL
//
