ID   A0A1D6I157_MAIZE        Unreviewed;       614 AA.
AC   A0A1D6I157;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   ORFNames=ZEAMMB73_Zm00001d019947 {ECO:0000313|EMBL:ONM53977.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM53977.1};
RN   [1] {ECO:0000313|EMBL:ONM53977.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM53977.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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|RuleBase:RU365011}.
CC   -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC       {ECO:0000256|RuleBase:RU365011}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM007650; ONM53977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6I157; -.
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   PANTHER; PTHR47346:SF1; GPI INOSITOL-DEACYLASE; 1.
DR   PANTHER; PTHR47346; HYDROLASES, ACTING ON ESTER BOND; 1.
DR   Pfam; PF07819; PGAP1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU365011};
KW   Hydrolase {ECO:0000256|RuleBase:RU365011, ECO:0000313|EMBL:ONM53977.1};
KW   Membrane {ECO:0000256|RuleBase:RU365011};
KW   Protein transport {ECO:0000256|RuleBase:RU365011};
KW   Transport {ECO:0000256|RuleBase:RU365011}.
SQ   SEQUENCE   614 AA;  67047 MW;  90268DB65A906CA6 CRC64;
     MGGGGGFRGS CRVGAVLLFS AWVALAALSR LLRPVPNGCV MTYMYPTYIP IAATPRNISS
     DRYGLFLYHE GWKQIDFAKH IRGLRGVPVL FIPGNGGSYK QVRSLAAESF RAYQNGPLEP
     TFYQEASSSL PGDGLNNFSI PSRYGRMLDW FAVDLEGEHS AMDGQILEEH TEYVVYAIHR
     ILDQYKESHL ERSKGGAQSS PDLPSSVILV GHSMGGFVAR AAVVHPNLRK SAVETILTLS
     SPHQYPPIAL QPSLGHFFSH VNEEWRKGYK TGVSHAISSK LSNVVVVSVS GGIHDYQIRS
     RLASLDGIVP STHGFMVGSS SMKNVWLSME HQSILWCNQL AVQVAHTLLS IIDPVDRQPF
     SSTQKRVFVF TKMLQSAVPQ SLSSMTHVPA SLSRNLPANE NQDAGELHKK DSLSCPSSTE
     WTSDGLEKDL YIQSNSVTVL AMDGRRRWLD IKKLGSNGRG HFVFVTNLAP CSGVRIHLWP
     EKHHSPVQNE LPASKKIVEV TSKMVQIPAG PAPKQVEPGS QTEQPPPSAF LLLSPGEMSG
     FRFMTISVAP RPTISGRPPP AASMAVGQFF SPEEGASSFS IGTIIRSSFA PCLGMGFCIW
     PAHHSKYILR DCSG
//