ID A0A3Q1H9Y3_ANATE Unreviewed; 1149 AA.
AC A0A3Q1H9Y3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000001658.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000001658.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|RuleBase:RU361133};
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DR AlphaFoldDB; A0A3Q1H9Y3; -.
DR STRING; 64144.ENSATEP00000001658; -.
DR Ensembl; ENSATET00000001680.2; ENSATEP00000001658.1; ENSATEG00000001204.2.
DR GeneTree; ENSGT00940000155660; -.
DR InParanoid; A0A3Q1H9Y3; -.
DR OMA; CNRNSMT; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000265040; Unplaced.
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; cd13364; PH_PLC_eta; 1.
DR CDD; cd08597; PI-PLCc_PRIP_metazoa; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
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:SF84; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 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; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 116..226
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 645..761
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 761..890
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 128064 MW; 58A812AD2023390A CRC64;
MSEFGEKRSA AGPPVAGWGG AAASGGAGTS LETHQEEPVS NGNCSVSHTV KRVQNESSCE
SPTWEGTGSD SATKPIPRRS SLIKDGSRAG RERKKTVSFS CSLSEKKISS AADCIHSMVE
GSELKKIRTN SRVYQRYYLL DTGLQALCWE PSKKESDKAR IFLASVREVR TGRNTETFRT
SGVYEQISED CAFSIIYGEM YESLDLVANS AEVANIWVTG LRYLMQYGKH AVDMLASSQD
SLRLCWLEQL FSSAADSHSQ GNVEEGIHLQ SAVGLIQSVN PGVSSGKVEQ RFKELQRLRE
RMCGLTIDNG SGVKDHTENK KATGKNERVT KPEFIEVFHD FCTRPEIYFL LVQFSSNKEF
LDTQDLMRFL EAEQGMAQVS EETSLKLIQS HEPSKKGREQ RYLSLDGFTS YLTSAECHLF
DREHDTVCQD MSQPLSHYYI SSSHNTYLIE DQFKGPSDIS GYIRALKMGC RCVEVDVWDG
PDDEPVVCAG PTLSPPLSLR CVLEAIGRFA FVASEYPLII CIENHCSLLQ QKVMYQHLVR
ILGERLYTDP PDERDSYLPS PHALRHRILI KGKKLGPGSD GGDGGVSEED EGAEMCQRMK
AANSGGTGLV GNEKDMSQKS LLSTAINQSN PPHLPPKQFQ LLKELSDLVI LCHSVRFTDF
TTSSKSQKPW EMCSFHESLA LRLASESPGD FVNHNKHFLS RVFPKPMRVD SSNMNPQDLW
KCGCQIVSMN FQTAGLMMDL NTAWFRQNGN CGYVLRPAIM RQEVSYFSAD TRDTVPGVSP
QLLHVKVISG QNLPKPRGSG AKGDVVDPYV YVEIHGIPAD CTERRTRTVT QNGDNPIFDE
SFEFQINLPE LAMVRFVVLD DDFIGDEFIG QYTIPLECLQ PGYRHVPLQF LTGEELPHAK
LFVHVALTNR RGGGKPHKRG LSVRKARKGR DYTALRDLGI RAVDEVFKMA APLLREATDL
RENMQNSVAV FRELCGVSAV GNLMRCVLAL SSRVSGPEGM PLLLFDLRDY YPTLEPQGPL
PDVLRRVVST YEMMVQASRA VNELSDGIYD RILHIQTTAM EFHEKLDNLA AKEGLKGRKV
SRALESFSWN ITILKGQTDL LQHAKAEVQE NIKQVRDAAL TGNLAKESLG VRRVRSQTRG
QSQDDTPII
//
