ID W2FZX9_PHYPR Unreviewed; 905 AA.
AC W2FZX9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=L915_17342 {ECO:0000313|EMBL:ETK76224.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETK76224.1};
RN [1] {ECO:0000313|EMBL:ETK76224.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK76224.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins
CC which plays important roles in the quality control and ER-associated
CC degradation of GPI-anchored proteins. {ECO:0000256|RuleBase:RU365011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|ARBA:ARBA00006931, ECO:0000256|RuleBase:RU365011}.
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DR EMBL; KI688649; ETK76224.1; -; Genomic_DNA.
DR AlphaFoldDB; W2FZX9; -.
DR EnsemblProtists; ETK76224; ETK76224; L915_17342.
DR VEuPathDB; FungiDB:PPTG_04210; -.
DR Proteomes; UP000053236; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..905
FT /note="GPI inositol-deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004816449"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 444..463
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 483..504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 525..542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 554..577
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 589..610
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 630..651
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 779..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 808..825
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 834..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..852
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 99482 MW; F7D00E4D312D8795 CRC64;
MSSHRLLLPL LTLLSVLLTG LYVADVVSTK NYESACEMTW SWPVYTPVTW RSVPSHPKYQ
LYRVDMKFAR DDLSGVPVLF VPGHMGSYKQ ARSLSRHLWD TNETLFDVFA LDLDEEPTGL
NGNFITDQAT YLNDVVRAIL REYKRQNKKS NKKLVIPDSV VIVAHSMGGI VARTAELLPN
YKKRSIQHVV GLGVPYENPS FPFDAEMNAV YDRIHSKKGK NDQVVYVSIA GGHKDTLVQT
ALTSIDTLAD SSRAFVALAS AISTVQTPVD HFCLLWCHQL LKVVAESLYK AVNLETRELV
SNPNVRLAIA KEVLFGGSSS EDGVVIETVA NESLHRSYVL DGYYPGEYAG YALLLPYFLT
NLLRTRFMTV IVIMYVLALQ FFSAQVAQWQ TRFNLQSTPS PQDLSQENFP SFTSMLHPAA
HTPALLKNIA NALHDKSNLG KTTTVGIAVL AAAAAGYFGY GQLLSSGQDA DSLTAFATMA
GEILILYAYA LGLLYALTQL FSLLQRFVVS PVVSLVGNIT DQLKLRRWMI IAFIHAVVQI
LGQIKSPSSD SSKVLGLAVL SSFVVFVLYL LVLGGNNDGT SDQQRMQRSL FAVLFLSIFP
WGGKVAYFAG VVRTPPSELS NGMLMEGGSY IAVLSLFTYL ISLSLECMIP LPPTAFFGAS
SGQDAASVYG KSSSNSNSNV KITAENCPKC IFEDGGPGSV LVEYSDRTTR RIVTGKTGEV
VYVGRTFRVV SCDCVYRFKN SRDFCAFCIR SCRLCGGGNG NFQEAAKYKD FLEESKVDLA
MHALVPMTFQ ICAVIQAMYS LYRSHMSFYL TPACVVALVI YHIVLRHPIE ARRIKNKQRK
KTTKKKKSSN KSKSKTTTTT TTATSSTTGA TVSTDTTSRK KKKKRKSGTS TSSASSPLIE
EVATS
//
