ID A0A6G1S836_9ACAR Unreviewed; 532 AA. AC A0A6G1S836; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 29-SEP-2021, entry version 6. DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011}; DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011}; GN Name=PGAP1_0 {ECO:0000313|EMBL:MDE46103.1}; GN ORFNames=g.11565 {ECO:0000313|EMBL:MDE46103.1}; OS Aceria tosichella (wheat curl mite). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Acariformes; Trombidiformes; Prostigmata; Eupodina; Eriophyoidea; OC Eriophyidae; Eriophyinae; Aceriini; Aceria. OX NCBI_TaxID=561515 {ECO:0000313|EMBL:MDE46103.1}; RN [1] {ECO:0000313|EMBL:MDE46103.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LincolnNE {ECO:0000313|EMBL:MDE46103.1}; RA Scully E.D., Geib S.M., Palmer N.A., Gupta A.K., Sarath G., Tatineni S.; RT "Transcriptome assembly of Aceria tosichella (Wheat curl mite) Type 2."; RL Submitted (OCT-2018) 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}. 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; GGYP01001332; MDE46103.1; -; Transcribed_RNA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR012908; PGAP1-like. DR InterPro; IPR039529; PGAP1/BST1. DR PANTHER; PTHR15495; PTHR15495; 1. DR Pfam; PF07819; PGAP1; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, KW ECO:0000256|RuleBase:RU365011}; Hydrolase {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 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 7..27 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU365011" FT COILED 294..314 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 532 AA; 60507 MW; 335FC4FD5D3B3321 CRC64; MKALKLGFWL HLSLVIITSY IVITYFFEPH DNQCQMTFMM EPPKFKPITI YNSMQESLTT PSSNNNNNDK YNTHDYKLFM YREHGFPLEN NLQYDLKDSM PILFVPGNAG SYQQVRSLAS TCIRRQFQSV DAFKFIFYTI DFRAQLSGLD GGLIESQIQF VHLAVKKIIS MHPIETNGVI LVGHSVGGFI AKALLTNPDF DPASIPLLIN LASPITRPFV NFDSKMRHLY HSTHDAWSQR QNLSSTLSIS ISGGPSDRLV PTHLSLDPQY DISLTTSSID EVWLTTDHVS ITWCRELMNK LAQLLSALMD KKKTRLVDGK EQQIAIALNE LVTDASNQID NISMGSISRE QPVLNTITIQ EFTGLFVAYR STLIESPLII NMTTNREHGD LFVWLEHIGT IKKNGIYGCD DVVLASSKAH CIGKIDLSPR MRTIPSRRYE PNKKSFIIKD ESHLVKYLIM DFTITSRLNG ESRKFKTPEP IPFPESISIQ TIDDQEMKSL YIPTLFEYLM TIPWSKTSLA HEIVPKPALP MR //