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Database: UniProt
Entry: A0A091DNE4_FUKDA
LinkDB: A0A091DNE4_FUKDA
Original site: A0A091DNE4_FUKDA 
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
//
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