ID M3Y8Q6_MUSPF Unreviewed; 922 AA.
AC M3Y8Q6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN Name=PGAP1 {ECO:0000313|Ensembl:ENSMPUP00000007713.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000007713.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000007713.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins.
CC GPI inositol deacylation may important for efficient transport of GPI-
CC anchored proteins from the endoplasmic reticulum to the Golgi.
CC {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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; AEYP01078714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01078715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3Y8Q6; -.
DR STRING; 9669.ENSMPUP00000007713; -.
DR Ensembl; ENSMPUT00000007837.1; ENSMPUP00000007713.1; ENSMPUG00000007770.1.
DR eggNOG; KOG3724; Eukaryota.
DR GeneTree; ENSGT00390000016484; -.
DR HOGENOM; CLU_013735_1_0_1; -.
DR InParanoid; M3Y8Q6; -.
DR OMA; YGLYYYY; -.
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:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR GO; GO:0021871; P:forebrain regionalization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 667..689
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 735..759
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 819..838
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 886..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 777..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 104966 MW; 436E9B96D134A3AD CRC64;
MFLQSVSFWN LAFYALMVFM ATLGLWDVFF GFEENKCSMS YMFEYPEYQK IELPKKLAKR
YPAYELYLYG EGSYAEEHKI LPLTGIPVLF LPGNAGSYKQ VRSIGSIALR KAEDIDFKYH
FDFFSVNFNE ELVALYGGSL QRQTKFVHEC IKTILKLYKG QEFAPKSVAI IGHSMGGLVA
RALLTLKNFK QDLINLLITQ ATPHVAPVMP LDRFITDFYM TVNNYWILNA RHINLTTLSV
AGGFRDYQVR SGLTFLPKLS HHTSALSVVS SAVPKTWVST DHLSIVWCKQ LQLTTIRAFF
DLIDADTKQI TQNPKKKLSV LNHHFIRHPS KHFEENPAII SDLTGTSMWV PVKVSKWTYV
AYNESDKIYF TFPLANHRKI YTHVYCQSTM LDTNSWIFGC INSTSMCRQG IDLSWKAELL
PTIKSLTLRL QDYLSLSHLV VYVPSIHGSK FVVDCEFFKK ETRSIQLPVT HLFSFGLSSR
KVILNTSGLF YNIELLNFGQ IYQAFKINVV SKCSGVKEEI TSIYKLHIPW SYEDSLTIAQ
VPSSTEISLK LHIAQPENDS HVALLKMYTS SDCQYEVTVK TSFSQILGQV VRFHGGALPA
YVTSSILLAY GGQLYSLFST GHCLEYATVL DKEAKPYKVD PFVIMIKFLL GYKWFEELWD
VLMLPELDAI VLTSQSMCFP LVSLILFLFG TCTAYWGGLL SSTSVRLLSS LWLALRRPPE
LPKDIKMISA DLPFLTIVLI IVGWTTCGAF AILLTYLYYV FKIVHLQASL TMYKNSQTVN
PKHSRRSEKK SNHHKDSTVH HLRLSASDAE DSLRMHSTVI NLLTWIVLLS MPSLIYWLKN
VRYYFKLNPD PCKPLAFILI PTMAVLGNTH TVSIRSSKLL KTTSQFPLPL AIGIIAFGSA
HLYRVPCFIF IPLLLHALCN FI
//
