ID A0A099YTZ9_TINGU Unreviewed; 994 AA.
AC A0A099YTZ9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
DE Flags: Fragment;
GN ORFNames=N309_11153 {ECO:0000313|EMBL:KGL72867.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL72867.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL72867.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL72867.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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|RuleBase:RU361133};
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DR EMBL; KL885381; KGL72867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099YTZ9; -.
DR STRING; 94827.A0A099YTZ9; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0050811; F:GABA receptor binding; IEA:InterPro.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate 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 GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:InterPro.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16223; EFh_PRIP2; 1.
DR CDD; cd13364; PH_PLC_eta; 1.
DR CDD; cd08597; PI-PLCc_PRIP_metazoa; 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; 1.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR028382; PLCL2_EFh.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF84; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 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; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 128..238
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 605..721
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 721..850
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL72867.1"
FT NON_TER 994
FT /evidence="ECO:0000313|EMBL:KGL72867.1"
SQ SEQUENCE 994 AA; 110976 MW; D98A986AAE451842 CRC64;
GSSGAGGLPS SPGPGQGKVA FKAGDGEGGG GGGGGRSRFD SAGGRVSNGD CALVGAGEES
GPALPGSPES SSKEKGFSTS QQRDGKPGIP RRSSIIDGTK QKRERKKTVS FSSMPTEKKI
SSASDCINAM VEGSELKKIR SNSRVYHRYF LLDADMQSLR WEPSKKDSEK AKIDIKSIKE
VRTGKNTDIF RSNGIYDQIS EDCAFSIIYG DNYESLDLVA NSADIANIWV TGLRYLISYG
KHTLDMIGSS QDNMRTSWVS QMFSESDVDN LGHIPLCNAV QFIKDLSPGL KTNKIELKFK
ELHRSKEKSG TEVTKEEFIE VFHELCTRPE IYFLLVQFSS NKEFLDTKDL MMFLEAEQGM
AHVTEEISLE IIQSYEPAKD GQEKGWLSID GFTNYLTSPD CHIFDPEHKK VCQDMKQPLS
HYFINSSHNT YLIEDQFRGP SDITGYIRAL KMGCRSVELD VWDGPDNEPV IYTGHTMTSQ
IVFRSVIDII NKYAFFASEY PLILCLENHC SIKQQKVMVQ HMKKILGDKL HTQSPNIEES
YLPSPESLKG KILIKAKKLS SNCSGLEGDV TDEDEGAEMS QRVGKEGVEQ QNSMTGKRFQ
LCKELSELVS ICKSVQFKEF QVSFQLQKYW EVCSFNEVLA SKYANENPGD FVNYNKRFLA
RVFPSPMRID SSNMNPQDFW KCGCQIVAMN FQTPGLMMDL NIGWFRQNGN CGYVLRPAIM
REEVSFFSAN TKDTVPGVSP QLLHIKIISG QNFPKPKGSG AKGDVVDPYV YVEIHGIPAD
CAEQRTKTMH QNGDNPIFDE SFEFQINLPE LAMVRFVVLD DDYIGDEFIG QYTIPFECLQ
TGYRHVPLQS LTGETLAHAS LFVHVAITNR RGGGKPHKRG LSVRKGKKSR EYASMRTLWI
KTIDEVFKNA LQPIRDATDL RENMQNAVVS FKELCGLSPV ANLMQCILAV STRLVGPDNA
PLIVLNLNDQ YPTMELQGIV PEVLKKIVTA YDMV
//
