ID A0A261BJ96_9PELO Unreviewed; 1390 AA.
AC A0A261BJ96;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
DE Flags: Fragment;
GN ORFNames=FL83_15280 {ECO:0000313|EMBL:OZG10347.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG10347.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG10347.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG10347.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR000956-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG10347.1}.
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DR EMBL; NIPN01000125; OZG10347.1; -; Genomic_DNA.
DR Proteomes; UP000216463; 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; cd16200; EFh_PI-PLCbeta; 1.
DR CDD; cd13361; PH_PLC_beta; 1.
DR CDD; cd08591; PI-PLCc_beta; 1.
DR Gene3D; 2.30.29.240; -; 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; 2.
DR Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR037862; PLC-beta_PH.
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:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 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; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PIRSF; PIRSF000956; PLC-beta; 3.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF69989; C-terminal domain of PLC-beta; 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; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000216463};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 782..898
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 901..1026
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 507..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1255..1297
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1330..1372
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 555..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 400
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG10347.1"
SQ SEQUENCE 1390 AA; 156617 MW; A905E396AC68967E CRC64;
MAKEFQFNWK PNIPTSLLQG ACFDRYDDES TCLELNAQVR VDEYGFFFYW LVEGKDAVVL
DMGQIWEARP GGLPKDGRIM FELEQRGASE TIAERTIWMT HGQDLVNVQS FFLVAESVEM
AKMWKTGMNE ILKTSRIRHV CPTTQLWKWL TLNVNERRKI PIKVIIKTFS SGKPEKMVQK
CLNDLGLGGD KYTPVRVINR SMGKKFRNFY KCSRGRKRKE REELDVEILT FEKFLRLYNK
ICPRTEVQEL FVKLSGQKEY LTKDRLINFL NEEQRDPRLN EILFPFFDPP RTGQLIAKYE
IDNNYIENGK MSGDAFLRFL MSDENPPVFL DRIEMYMDMD QPLCHYYINS SHNTYLTGRQ
YGGKSSSEIY RQVLLSGCRC IELDCWDGTG ENKGEPIITH GKAMCTDVFF KDVLVQIRDT
AFARSDFPVI LSFENHCSKS NQLKMAKYCM DIFGDMLLSK PFDDAPLEPG VSLPSPNRLR
KKILIKNKRL KTDIERHQLD QFLREGKLDE EDELNETPEV VGEDSVSPRS GGSGGTGAAE
DVAMDDDTSD DDDDPSVQTS LNVMRTVPTV STTSNNGSNR SARSSLETPS PSGGLMVPDR
ASSTATSIKN AVLARSPNFS SLRQKLSFKR RQSPLGEIPV KETDEAHPEL KQNFIAKNLK
GFGFSKKQPD STSSTTLLTA SPTPSSSSMA PFLTNQSSTT SNNTITLNSP QIMERSRSEK
RSFRQKKGVF GDELHSDSAA LIDFMRTASS RKKKPVLTKE EEERIFAEYH YTGATTNIHP
LLSSLVNYTH PVKFSGFDVA EANNLHFHMS SFSESTGLGY LKQSAPEFVN YNKRQPSRIY
PKGARVDSSN FLPQIFWNAG CQMVSLNFQT PDVYMQLNMG KFEYNGGSGY LLKPDFLRRP
DRTFDPFSES PVDGVIAAHC SVRVISGQFL SDRKIGTYVE VEMYGLPTDT IRKEHKTKVI
PGNGLNPVYN EDPFVFRKVV LPELAVLRFA VYDENGKQLG QRILPLDGLQ AGYRHISLRS
DTNQSFILSP VLFVQIVIKT YVPDELSGLV DALADPRAFL SEQKKRQEAL AHMGVPNTKN
TALRNMKQPP RQNGSSADLL SNNSQPGTAR SDQINSMMTS VSIRSPNEQP APVAVDKFKQ
TNVDKLITNN RRSTKKEKGS RRSLTASVSS GCGSTSGTVP VGVCIPSGAS GSGSGAPSTP
GAGNSDGTGS PATTGSPVPQ DLINNDRVRS LVNTQTGEWS AMVRRHDEEE FELKKGQLKE
QFDLLKKLMS EAQKNQMQAL KLRLEAEGKD LKQTQTRKNM EDQKTITLDK GIKTKTERDR
RVKEQNEKNL KMFVEERKRL AMKAQKHEEQ LTKRHLDQLE QLEKDFQKAL EVEVGNYKEE
QLAAQPTSVV
//
