ID A0A401NVS2_SCYTO Unreviewed; 1296 AA.
AC A0A401NVS2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma {ECO:0000256|PIRNR:PIRNR000952};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000952};
GN ORFNames=scyTo_0000350 {ECO:0000313|EMBL:GCB64970.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB64970.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB64970.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- FUNCTION: Mediates the production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an
CC important role in the regulation of intracellular signaling cascades.
CC {ECO:0000256|PIRNR:PIRNR000952}.
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};
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:GCB64970.1}.
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DR EMBL; BFAA01000066; GCB64970.1; -; Genomic_DNA.
DR STRING; 75743.A0A401NVS2; -.
DR OMA; HICTHRN; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd13362; PH_PLC_gamma; 1.
DR CDD; cd08592; PI-PLCc_gamma; 1.
DR CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR CDD; cd11970; SH3_PLCgamma1; 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; 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; IPR018247; EF_Hand_1_Ca_BS.
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; IPR035724; PLCgamma1_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:SF173; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF16457; PH_12; 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; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 3.
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; 2.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
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|PIRNR:PIRNR000952, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000952,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR000952};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216};
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};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000952}.
FT DOMAIN 32..151
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 554..661
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 672..760
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 795..855
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 877..937
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 959..1076
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1074..1200
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1296 AA; 150077 MW; 4BDC7CF2BE8BA621 CRC64;
MAVVAGGGGF HNGLLQQDQG APSEPQIAEL CRSLEVGTVM TLYYSKKSQR PERRTLQVKL
ETRQIIWSRG AEKLEGEIDI REIKEIRSGR NSRDFERYQD DPAKPDLSRP DLTHCFVILY
GMEFRLKTLS LAATSEEEMN MWTTGLNWLL ADTMKSPTPL QIERWLRKQF YNMDRNREDR
ITVKDLKSLL SQVNYRVPNM KFLREKITDM ELRSGDVTYC QFAQLYRSLM YDAQKHMEVR
FLQRSCERPE LSQVSLQDFQ QFLLEYQKEL WATDIHQVRE FMFNYLRDPL REIEDPFFYL
DEFLTFLFSK ENSIWDLRFD LVCLEEMSNP LSHYWISSSH NTYLTGDQFS SESSLEAYAR
CLRMGCRCIE LDCWDGPEGM PVIYHGHTLT SKIKFNDVLT TIKEHAFVTS EYPVVLSIED
HCSIVQQRNM ANVFKKVFGD MLLTKPVDIT ADGLPSPNQL RRKFLIKHKK LAEGSAYEEV
STSTYSENDI SNSIKNGILY LEDPINHEWN PHYFVLTSSK IYYTEETSAN QANEDDEEQR
EPCSGTDLHV TEKWFHGKLG AGRDGRQIAE RLLTEYCIET GAPNGSFLVR ESETFVGDYT
LSFWRSGKVQ HCRIHSRQEA GNPKFYLTDN LVFDSLYALI THYQQLPLRC NEFEMRLTEP
VPQTNAHESK EWYHANLSRA QAEHMLMRVP RDGAFLVRKR NEPNSYAISF RAEGKIKHCR
VQQEGQVVIL GSSEFDSLVD LVSYYEKNPL YRKMKLRYPI NEETLEKIGT AEPDYGALYE
GRQPGFYVEA NQMPTFKCTV KAMYDYKAQQ DDELSFCKNC IIQNVVKQDG GWWKGDYGGK
RQFWFPANYV EEIMSPTTSE PERLPLSENS PLGNLLRGFL DVPSCQIAVH PEGKGSRPYV
FKINVGSFNR SGETMDLAAE TMEDLNDWVT KIREAAQTAD ARKEEGKMME RRKKIALELS
DLVVYCRPVP FDEEKIGSDR ACYRDMSSFP ETKAEKYVNR VKGKKFLQYN RLQLSRIYPK
GQRLDSSNYD PLPMWICGSQ LVALNFQTPD KPMQMNQSLF TLNGKCGYVL QPSLMRDEQF
DPFDKHSVRP VDSLIVQLQV LGARHLPKNG RGITSPFVEV EVCGADYDNC KYKTEIVAVN
GLNPTWTAKP FSINICNPDF SFLRFVVYEE DVFSDQNFLA EATVPVKAIR TGYRSVPLKN
SYSEDLELAA LMVHLDVLES VIRENGDAVL CPSNPSLRER SADHSSQLLA YRGREGSFDN
RYQQEELRLF QEPQLEHTET RERRLLRRTR ISGDNR
//
