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}.
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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
//