ID A0A091DNE4_FUKDA Unreviewed; 1590 AA.
AC A0A091DNE4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ORFNames=H920_06816 {ECO:0000313|EMBL:KFO31775.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO31775.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO31775.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO31775.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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|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 EMBL; KN122247; KFO31775.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000000323; -.
DR eggNOG; KOG0169; Eukaryota.
DR Proteomes; UP000028990; 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:UP000028990};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 47..155
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 180..210
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 211..247
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 636..749
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 750..879
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 541..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 172926 MW; 53709867510E804B CRC64;
MPGPQPSATS RGTGAVACLA EVLLWAGGSV VVLPCWQLSP LVERCMSAMQ EGTQMVKLRG
SSKGLARFYY LDEHRSCLRW RPSRKNEKAK ISIDSIQEVS EGRQSEIFQR YPDGSFDPNC
CFSIYHGSHR ESLDLVSPSG DEARTWVTGL RYLLAGISDE DSLARRQRTR DQYPWAPGWL
KQTFDEADKN GDGSLNISEV LQLLHKLNVN LPRQRVKQMF READTDDRQG MLGFEEFCAF
YKMMSTRRDL YLLLLTYSNH KDYLDAADLQ RFLEVEQKMQ GVTLQSCYDI IQQFEPCPEN
KCKGVLGIDG FTNYTRSPAG DIFNPEHHGV HQDMTQPLSH YFITSSHNTY LVGDQLMSQS
RADMYTRVLQ AGCRCVEVDC WDGPDGEPIV HHGYTLTSKI LFRDVIETIN KYAFLKNKYP
VILSIENHCS VAQQKKMAQY LTDILGDKLD LSAVSGEDAT MLPSPQMLKG KILVKGKKLP
ANISEDAEEG EVSDEDSADE IDEDCKLLNG DASTNRKRVE NIAKKKLDSL IKESKIRDCE
DPNDFAVSTL PPGKPGHRAE ARKNKAEEDV ESREDTRASR RDGRLLMSSF SKRKKKGSKL
KKVASMEEGD EDPDSAGSQT RGTARQKKTM KLSRALSDLV KYTKSVGSHD VEMEVASSWQ
VSSFSETKAH QILQQKPAQY LRFNQHQLSR IYPSSYRVDS SNYNPQPFWN AGCQMVALNY
QSEGRMLQLN RAKFSANGNC GYVLKPPCMC QGVFNPNSED PLPGRPKKQL ALRVISGQQL
PKPRDSMLGD RGEIIDPFVE VEVIGLPVDC SKEQTRVVDD NGFNPMWEET LVFMMHMPEI
ALVRFLVWDH DPIGRDFIGQ RTLAFSSMMP GYRHVYLEGM EEASIFVHVA ISDISGKAKQ
ALGLKGLFLR GTKPGSLDSH AAGQPPPRPS VSQRLLRRTA SAPTKSQKPG RKGFPELALG
TQDVGSEEAA DDTVPPSPCP TLETPAHDGP GSSIPRGKAP GAAAVAAERR SPVQVRPLRG
LKGSGPAGMA STCMKCVVGS CTGTDNEGLW RERQPSPGPA GRLTTICQQP QAWVEAPGSP
CSPGPRAAPG RSKEASKGSG AQRQGAGGSS SSVSLDSSSL DNPGSPQVAP CPPGGAHRQL
GALQGEMNAL FTQKLEEMRN SSPMFSTGTE SRVPGARPFS TQRSISPLCS LEPIEEEAAT
PTSPPRGRSL HSAGPVAKAA SPLQIARGPP GPLQLRTGVH GNSEEAPGKL LNGEGPTGSQ
TDSRSQPRAL VLLPAVRRAK SEGQVPLEPL GAWRPLAGPA PIPAVYSDAT GSDRTWQRLE
PGSHRDSVSS SSSMSSSDTV IDLSLTSLVL GRSRESLAGT PLGRLPPRPC TASTAPPDLL
PVTKSKSNPN LRDAGQLPPT PDALTQAPRL SGPRPWPSRG RLALVGLQDC TAAAKSKSLG
DLTADDFAPS FKGSSRSLGR GLGPRGSTQR DTLTEQLRWL TGFQQAGDIT SATSLGPAGD
RAERDPSFLR RSSSRSQSRV RAIASRARQA QERQQRCRNL DPQAPPEEER GAPEGACSVG
LEGCVDATGP PDGTPEQVPG AAESLLLLRL
//