ID A0A131ZTS7_SARSC Unreviewed; 455 AA.
AC A0A131ZTS7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 28-JUN-2023, entry version 36.
DE SubName: Full=Glycerophosphocholine phosphodiesterase GPCPD1-like protein {ECO:0000313|EMBL:KPM02176.1};
GN ORFNames=QR98_0005830 {ECO:0000313|EMBL:KPM02176.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM02176.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM02176.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM02176.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-
CC sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892;
CC Evidence={ECO:0000256|ARBA:ARBA00000110};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KPM02176.1}.
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DR EMBL; JXLN01001104; KPM02176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A131ZTS7; -.
DR VEuPathDB; VectorBase:SSCA005587; -.
DR OMA; FAMCTHI; -.
DR OrthoDB; 1005457at2759; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR22958:SF1; GLYCEROPHOSPHOCHOLINE PHOSPHODIESTERASE GPCPD1; 1.
DR PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF03009; GDPD; 2.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 165..427
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 455 AA; 53388 MW; 4874F8EB417B85C4 CRC64;
MNEIHYKLTG FEIIDVFDSI QDDEMTDEDS KNYGEEYTTE IAVMNDYEFK FKNQEPYGRL
LKKNEFVMFR IKIPITGVVG IRVDLFHKIN KNVFEKIAFC YIYPLDTKES NGMCMVPITS
KLGKIIARFK VDYFIAKPYD GMSIEQIKRK SKTRNLKSWQ LKKNGFDIGH RGAGSARRFD
SYEKLLENTI ESFNFAYKKG ADMVELDVQL SKDKIPIVYH DFNVNLVLQK RDEEMETFEM
NIKDLTYNQL QKLKIKPMLK GKEFYDFEDN DSKPHGRPFA SLRTVLESVD ANCGFNVEIK
YPQRQINGNW EAEKSHDLNE VRQKQDRYPV LFLTQGLTTK WTKYENPLNH SIEMAAYLAL
SMDLFGVAVH AEDIIKDTSL IQFVKSKSLI LFCWGDDLNN KELIENLKKQ GVDGAIYDKY
EFVNIFENRN SFWGYFLSRI DLLIQNDDRF HLSKN
//
