ID M4ALX9_XIPMA Unreviewed; 1306 AA.
AC M4ALX9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma {ECO:0000256|PIRNR:PIRNR000952};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000952};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000015473.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000015473.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000015473.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR RefSeq; XP_005801748.1; XM_005801691.1.
DR STRING; 8083.ENSXMAP00000015473; -.
DR Ensembl; ENSXMAT00000015496.2; ENSXMAP00000015473.1; ENSXMAG00000015379.2.
DR GeneID; 102217766; -.
DR KEGG; xma:102217766; -.
DR CTD; 5335; -.
DR eggNOG; KOG1264; Eukaryota.
DR GeneTree; ENSGT00940000158901; -.
DR HOGENOM; CLU_002738_5_0_1; -.
DR InParanoid; M4ALX9; -.
DR OMA; YMRNPLY; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
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; PF00169; PH; 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 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; 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; PS50222; EF_HAND_2; 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|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000952};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR000952};
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:UP000002852};
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 26..140
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 150..185
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 544..651
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 662..750
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 785..845
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 866..925
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 947..1064
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1065..1188
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1233..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1306 AA; 149941 MW; E4CA532CA9AD14C9 CRC64;
MAGTSGFLSN GPVPWMDDTE MNNLYRDLEL GTVMTLFYSK KSQRPERRTF QVKLETRTII
WTRSTDKIEG EIDIREIKEI RPGQKSRDFE RYVEDSAVRL DNFCFVILYG TEFRLKSLSL
AATSDEEMSM WVKGLKWLRD DTLKSPTPLQ IERWLRKQFY AADRNREDRI SYKDLKNMLS
QVNYKVPNMR FIKDKLPDSE TRNGDVTFSQ FAQLYRNLMF DAQKNVEIPF MQRFTGNVVD
ERITLEDFQS FLVECQKELW ASDNNKVQEF MFSYLKDPLR EVEDPYFHPE EFLTYLFSKE
NTIWDSSLDM VCAENMNNPL SHYWISSSHN TYLTGDQFAS ESSLEAYARC LRMGCRCIEL
DCWDGPDSMP VIYHGHTLTT KIKFNDVLNT IKDHAFVTSE YPIILSIEDH CSIVQQRNMA
TQFKKVFGDM LLTKAVDMAA DGLPSPNQLK KKILIKHKKL AEGSAYEEVP TATPYSENDI
SNSIKNGILY LEDPINHDWY PHFFVLTHNK IYYSEETTNN VGNDEDEELK EVLNTMDQHV
TEKWFHGKLG AGRDGRQIAE RLLSDYCQET GAPDGSFLVR ESETFVGDYT LSFWRLGRVQ
HCRIHSRQEA GSPKFYLTDN LVFDSLFALI THYQHVALRC NEFEMKLTEP VPQTNAHESK
EWYHANLSRS QAENMLMRVP RDGAFLVRKR TEPNSFAISF RAEGKIKHCR VLQEGQVVLL
GTSEFDSLVD LISYHEKHPL YRKMKLRYPI NDDTLEKIGT AEPDYGSLYE GRNPGFYVEA
NQMPTLKCTV KAMYEYKAQR DDELSFSKNA IITNVDKQEG GWWKGDCGGK KQMWFPANYV
EEISQAAAEP DRTEITENSP LGDLLRGSVD VTSCQIITRT EGKGSRPFVF SLVQNNTVQG
TLLDVAANSA EELQDWKTKI QEVAATSEAK LEEGKIMERR KKIALELSDL VIYCRPVPFD
EEKIGTERAC FQDMSSFPET KAEKYVNKTK GKKFLQYNRL QLSRIYPRGQ RLDSSNYDPF
PMWLCGSQLV ALNFQTADKP MQMNQALFML NGKSGYVLQP PIMRDDTFDP FDKNTLRGVD
QVSMKIEVLG ARHLPKHGRG IVSPLIEIEV CGADYDNDKQ KTESAADNGL NPTFPRKSFS
FTVCNSAFAF LRFGVYEIDM FNDQNFLAQA TFPIQSLKTG YRSVPLKNSY SEDLELASLL
VHMEITRGRD ENGEVLSPFS AAGSVSAPAS AQVGRELGSV SSTSSTMSPL PQSPSQAMSY
RGREGSFESR YQSPIDDFRV SQEALLDQMD PQNRRMLRRT SRLSPY
//
