ID A0A016WPD3_9BILA Unreviewed; 690 AA.
AC A0A016WPD3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN Name=Acey_s0560.g3470 {ECO:0000313|EMBL:EYC41669.1};
GN Synonyms=Acey-T19B10.8 {ECO:0000313|EMBL:EYC41669.1};
GN ORFNames=Y032_0560g3470 {ECO:0000313|EMBL:EYC41669.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC41669.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
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:EYC41669.1}.
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DR EMBL; JARK01000160; EYC41669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WPD3; -.
DR Proteomes; UP000024635; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
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 TRANSMEM 427..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 471..489
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 495..514
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 521..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 566..585
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 653..686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 690 AA; 77156 MW; 9BA2C45FE402FCE2 CRC64;
MMYICSLVVA SVLAGTLFMV HVGLHRENAC HMTYMWRYIS LVPFNVDGND VSRYGLYRYM
EGFVNDKTMA ISHDHIPVLF VPGSGGSAKQ VRSVASIMMN KTEMTSAPFR MHFYAVDFDE
ELSFLSGSIL NRQRDFVVRA ISTIQKMYSR KIILIGHSLG GTVLHALPAH PRFSISNMGL
VIILASPISA PPIVMDEAMI SFYESMQRAW VSRNDELRHV GLVSYSGGSK DFQVPDHLAT
IHGSHHIVHR PSWSIRGVDT PVDHLCILWC NQLTRHSTRI LYNYGIEEVS KDVPRPANAL
VEEFFHEESH ASANGSESLK DAVKIGIFDY PWVSRVYRGT MENSKKFYEL EFISPYMVYS
VSLESPCDMS MLFIYPNTLA RSATAKESAK VMTIDLPYEL SSSVGHIALE GKTGCDFDLT
VRPDVFYAWY LLLISNVNVV IHFTFSVLVA LTLLEKLKSF DRIRFRSQLG YYVNCGIAVL
LFLSFTYSSG IRECIFAVTI FYSISSVYFV AVVVRYVRDK VLCVIPLCLK LCNVVLTLVV
ILLLPVNPYL ANGVIALVIA LHRSSGPFSI LLSIATGGIC ASLGLAGPSR DATFHFLKHL
MGISSLEFIP VLNLLSSNFD FTHIFTKLVF LFMLSRAITF VRLPPHLVSL KDFMLAVLLV
VPGFMASHVN MSLEACAMIA SVLLYIISAF
//
