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Database: UniProt
Entry: U3JWC7_FICAL
LinkDB: U3JWC7_FICAL
Original site: U3JWC7_FICAL 
ID   U3JWC7_FICAL            Unreviewed;      1372 AA.
AC   U3JWC7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 71.
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=PLCG2 {ECO:0000313|Ensembl:ENSFALP00000007081.2};
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:ENSFALP00000007081.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000007081.2, 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:ENSFALP00000007081.2}
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};
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DR   STRING; 59894.ENSFALP00000007081; -.
DR   Ensembl; ENSFALT00000007112.2; ENSFALP00000007081.2; ENSFALG00000006754.2.
DR   eggNOG; KOG1264; Eukaryota.
DR   GeneTree; ENSGT00940000157517; -.
DR   HOGENOM; CLU_002738_5_1_1; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000016665; Chromosome 11.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0097708; C:intracellular vesicle; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0140031; F:phosphorylation-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0061760; P:antifungal innate immune response; IEA:Ensembl.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0002316; P:follicular B cell differentiation; IEA:Ensembl.
DR   GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Ensembl.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IEA:Ensembl.
DR   GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IEA:Ensembl.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR   GO; GO:0032747; P:positive regulation of interleukin-23 production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0150078; P:positive regulation of neuroinflammatory response; IEA:Ensembl.
DR   GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
DR   GO; GO:0012501; P:programmed cell death; IEA:Ensembl.
DR   GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0001878; P:response to yeast; IEA:Ensembl.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16215; EFh_PI-PLCgamma2; 1.
DR   CDD; cd13362; PH_PLC_gamma; 1.
DR   CDD; cd13234; PHsplit_PLC_gamma; 1.
DR   CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR   CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR   CDD; cd11969; SH3_PLCgamma2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
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   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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; IPR016279; PLC-gamma.
DR   InterPro; IPR035023; PLC-gamma_C-SH2.
DR   InterPro; IPR035024; PLC-gamma_N-SH2.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR035723; PLCgamma2_SH3.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10336:SF25; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF000952; PLC-gamma; 2.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00326; SH3; 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   SUPFAM; SSF55550; SH2 domain; 2.
DR   SUPFAM; SSF50044; SH3-domain; 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.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361133};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          21..131
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          532..636
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          647..736
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          769..829
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          930..1044
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          1038..1169
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   1372 AA;  161417 MW;  60FE0AC9E94D3EFA CRC64;
     MPRKNIDYGV LPEYEKSQIK RTLELGTVMT IFSLKKSSPE RRTIQVIMET RQVAWSKTAD
     KIEGFLDLME IKEIRPGKNS KDFERCKARH REEHCFTIFY GTQFVLNTLS LAADSKDDTD
     KWLCGLNILY QEVMSAPTPA ITESWLRKQI YSVDQTRKNS ISLRELKTVL PQANFKVSSM
     KYLKDKFAEI GAHKEELTFE QFHLFYKKIM FEQQKLILDE FKKDSSVFIL GNTDRPDASA
     VHLHDFQRFL LHEQQESWAQ DLSKVRERMT KFIDDTMRET AEPFLFVDEF LAYLFAKENS
     IWDEKYDSID VQDMNNPLSH YWISSSHNTY LTGDQLRSES STEAYIRCLR MGCRCIELDC
     WDGPDGKPII YHGWTRTTKI KFDDVVQAIK DHAFVTSEYP VILSIEEHCS VEQQRHMAKV
     FKEVFGDQLL MKPVEASADQ LPSPTQLKEK IIIKHKKLGP KGDIDVNLEE KKEEKKQQGE
     LYMWDTIEQK WTRHYCAIAD EKLSFSDDIE QSADEDSSKE VKRTELHLKE KWFHGKMKGG
     RTTAEKLLQE YCAEMGGKDG TFLVRESEAF PDDYTLSFWR SGRVQHCRIR STSDGDAVKY
     YLTDNLTFDS IYDLIQHYKE AHLRCAEFEL RLTDAVPNPS PHETKDWYYN NLSRGEAEDM
     LMRIPRDGAF LIRKRDEPDS FAMTFRAEGK VKHFRIQQEG RHFVLGTSAY FESLVELVTY
     YEKHPLYRKM KLRYPVTEEL LERYSTEKDI NSLYEVKMYV EPSEITPTVP QRTVKALYDY
     RAKRSDELSF SRGALIHNVT KETGGWWKGD YGEKVQHYFP SNYVEDLSSP NSAELENQII
     EDNPLGSLCR GILVLNTYNV VKMPQGKHKK PFVFILEPKN PEDPCVEFAT DKVEELFEWY
     QSIREITWKT AEEENRRKYW EKNQLIAIEL SDLVIYCKPT SKTKDNLDNP DFREIRSFVE
     NKAESIVKQK PLELLKYNLK GLTRVYPKGQ RVDSSNYDPF RLWLCGSQMV ALNFQTPDKY
     MQLNHALFSL NGRTGYVLQP ESMRNEEYDP MPNDSKRKLQ MIMTVRVLGA RHLPKLGRSI
     TCPFVEVEIC GAEYDNSKFK TTVVNDNGLN PIWAPNAEQV KFEIYDPNLA FLRFVVYEED
     IFSDPNFLAH ATFPIKGIKS GFRSIPLKNG YSEDIELASL LVHCEMQQVL ESEEELYSSC
     RQLRKRQEEL NTQLFLYDSH MNLRNPNRDA ILKEFNVNEH KLQIYQETCN RILDYVSFWA
     CFLRNYLDFQ YSFELWIMCH FGHVFYEITL ISNILLKESE EELYSSCRQL RKRQEELNTQ
     LFLYDSHMNL RNPNRDAILK EFNVNEHKLQ IYQETCNRRL KEKKVSNSKF YS
//
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