ID M1D2M2_SOLTU Unreviewed; 211 AA.
AC M1D2M2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN Name=102585322 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079881};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079881, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400079881}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079881};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 AlphaFoldDB; M1D2M2; -.
DR EnsemblPlants; PGSC0003DMT400079881; PGSC0003DMT400079881; PGSC0003DMG400031110.
DR Gramene; PGSC0003DMT400079881; PGSC0003DMT400079881; PGSC0003DMG400031110.
DR HOGENOM; CLU_065036_2_0_1; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1D2M2; baseline and differential.
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; PTHR47909; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR47909:SF2; GPI INOSITOL-DEACYLASE; 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};
KW Membrane {ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Transport {ECO:0000256|RuleBase:RU365011}.
SQ SEQUENCE 211 AA; 22687 MW; 47E1B2A903F71103 CRC64;
MLQSHNQATF VVGGSGSLSI IGHSAGGWLA RVYLQEFGSS DISLLLTLGT PHLPPPKGLP
GVIDQTRGLL YYVEKNCAKA VYSPELRYVC IAGRYIQGSR FFDSSSTHSS EFVDGAEQPM
SEVAAVSNTN AEIETGSTFR TRFVGQGYKQ VCGQADVWGD GVVPEVSAHL KGALNVTLEG
VYHSPVGSDD ATRPWYGSPA VVEQWIRHLL V
//
