ID U3K4I3_FICAL Unreviewed; 1517 AA.
AC U3K4I3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 67.
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:ENSFALP00000009937.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000009937.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000009937.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000009937.2}
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 59894.ENSFALP00000009937; -.
DR Ensembl; ENSFALT00000009977.2; ENSFALP00000009937.2; ENSFALG00000009519.2.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000158374; -.
DR HOGENOM; CLU_002738_0_0_1; -.
DR Proteomes; UP000016665; Chromosome 21.
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 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; 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:UP000016665};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 17..125
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 139..174
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 175..211
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 607..720
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 721..850
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 447..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1517 AA; 168181 MW; 78E9E07806D4CF12 CRC64;
MMDLGSPSQK HMERCMSSMQ AGTQMIKLRG GSKGLVRFYY LDDHRSCIRW RPSRKNEKAK
ISIDSIQEVC EGKQSEIFQR YADGSFDPNC CFSIYYGDHM ESLDLVSSSA EEARTWITGL
KYLMAGISDE DSLSKRQRTR DQWLKQTFDE ADKNGDGSLS ISEVLQLMHK LNVNLPRQKV
KQMFKEADTD DNQGTLDFEE FCAFYKMMST RRDLYLLMLT YSNHKDYLDT DDLKRFLETE
QKMTNVTKEH CLEIISKFEP CPENKKEGAL GIDGFTNYMR SPSGDIFNPE HYQVNQDMSY
PLSHYFITSS HNTYLMGDQL MSQSRVDMYA WVLQSGCRCV EVDCWDGPDG EPIVHHGYTL
TSKILFRDVI ETINKYAFIK NEYPVILSIE NHCSIVQQKK MAQYLTEILG DKLDLSSVHN
DDSTKLPSPA SLKGKILVKG KKLPANISED AEEGEVSDED SADEIDDDCK LMNGDASANR
KRVENIAKKK LDSLIKESKI RDCEDPNNFT VSTLPSSGKA GLKSDSKKSK LEDDVESGED
FSASKRHSRS LMGSFSKRKK KGSKLKKASS LEEGEDDSDS QGNLARSSVH YSRVNRQKKT
MKLSRALSDL VKYTKSVGSH DVETEISSSW QVSSFSETKA HQILQQKPAQ YLRFNQHQLS
RIYPSSYRVD SSNYNPQPFW NAGCQLVALN YQSEGRMLQL NRAKFSANGN CGYVLKPNCM
CQGVFNPNSE DPLPGQLKKQ LVLRIISGQQ LPKPRDSMLG DRGEIIDPFV EVEVIGLPVD
CFKEQTRVVD DNGFNPMWEE TLVFTVHMPE IALIRFLVWD HDPIGRDFIG QRTIAFSSMM
PGYRHVYLEG IEEASIFVHV AINDICGKAK QALGLKGLFL RNPKQASLDS HAAGQLHRKH
SFSSHILRRT ASAPTKSQKK NKKGFPEIAF DTKDSSSAGA GEGREVEAAS QPRFVQEPES
ASPTPAPRDG AGGEAPGKGL KDVCHFSIQS DSEEGSGSDH STEAPSEGSS TPNQPQEPPP
SREQGTNLAE DQGQDVPRAA DPSLVAPEDE RTSVAGCPTE GNGWTRCSEA EDQGGSAAHP
QKARLVEAAG HSAGQPVGSC QKQNNQPGQV LTDMKSTSES KVQNLGAAAV PPQQSNVITG
TQADSPQKGQ AAQALPVSVS QMSSYTLARR AKNEGLKTSD SSALIKIPSS LSPAAEVYFD
ATVNDRIWSK LDCSSHRDSM SSSSSMSSND TVIDLSLPSL ARKSLPDLGI RQDSLEPLAI
RKGMRPRSAT ACSHEMPMVS KSKSNPNLRC GQLPADELCP RPLARSPQDA FSSIPRRHTW
SRLYMESLRQ SSNKSKAHDT VGNNQAKSKS LGDLTSDDIV CTFESKYRSI SRSFVTRSMR
EQRRSSGLRG QARPRDELTE QLKRLTAFQQ ENDITSPISL EPSESEEEGE SAGLLRRSSS
RSQSRVRYIA NRARQAQERQ RLQGRARLGG SPIEERGNPE GACSVGRAGC SDPAAHGAPP
ASPKGQPDTE VFFMLKL
//
