ID A0A100IEC7_ASPNG Unreviewed; 1139 AA.
AC A0A100IEC7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=ABL_03281 {ECO:0000313|EMBL:GAQ39714.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ39714.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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|ARBA:ARBA00003496,
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ39714.1}.
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DR EMBL; BCMY01000004; GAQ39714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IEC7; -.
DR PaxDb; 5061-CADANGAP00005415; -.
DR VEuPathDB; FungiDB:An07g02530; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1157732; -.
DR VEuPathDB; FungiDB:ATCC64974_45040; -.
DR VEuPathDB; FungiDB:M747DRAFT_110575; -.
DR OMA; WVRNLAV; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
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 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 113..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 782..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 880..898
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 945..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 997..1020
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1040..1057
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1069..1088
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1094..1111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 126860 MW; 367A78418092AAE9 CRC64;
MHRRSSGSPA EDDAEESLAP VSRTPTDPSP APQVLDPPEK SRPQAAARTG TSFDLRRDAS
NPRSRNSSLW RTSSSTESRS SAVMMPLASQ RLPMEASPDG HLRFRPSRLR SPWPVSILTA
LTTLVASIFL FFILRSFSER QIGGDGCGIP VMSPTFLRMV GFDTEHTRFA SKYNLFLYRE
EGVDPYNQEN LGLNGAPVLF LPGNAGSYRQ VRSLAAEASR HYADVVRHDE ERLKSGTRSL
DFFMIDFNED LAAFHGQTLL DQAEYVNEAV SYILSLYHDP RRSRRDPGLP DPSAVILVGH
SMGGIVARTA LTMTNYQANS VNTIVTMSAP HAKPPVSFES DIVHTYKQIN DYWRDAYSQT
WANNNPLWHL TLISIAGGSR DTVVPSDYAS ISSLVPDTHG FTVFTSTIPD VWIGMDHLSI
TWCDQFRKAI IKSLFDVVDV RRASQTKPRA ERMRIFKKWY LTGLEPTAER TLPQKEPSTL
LTLEDSTNII LPQGQRLILR ELGHSPNTNV HLLPVPPQGV SGKKFTLLTD QKLDNPGEQG
TLEVLFCSVF PLHNGKFASI FSMNMDFSGS SAGSTRLACK NAAEDGIHLP ASTRTSKQAY
DRTSPFSYLQ YDLEDLVEHQ FVAVVDKARS PTRGWVVAEF SDSSDSVIRA RVGLGGLLSA
GLKMRLPANR PMLTEVRIPA LHSSLLNYKL KIVRRGYGEQ PELFAPLLRQ SIPDPHESKF
FVNVKQVNVN LHGVAPFMPP PLREQATLGG VSFHLWTDPS SESTVDISLS VDVLGSLGEL
VMRYRTVFAA FPILVIALVL RKQFQVYDET GYFITFAEGL DSTLRSSLPI LLLAMSLLAS
SLATSTTLPP SDDPFHWRTN STESPIDFTK NDLLLGSQDA FFWFLVPVFG LISVGVCVMM
NYVALSLLSV LSFFYGLMNS KSGYIKRDDK GNLPIFSAPT PRRRLINTAI LLILVATTIP
YQFAYMVACI VQLATCVRAQ WHAKETKSTT HYNFANLTYS IFLLMLWILP INILVLLVWA
HNLVVHWFMP FSSHHNVLSI MPFILLVEAM TTGTMVPRVS SRLKNVTSLI LFALAIYSAV
YGVSYGYLLH HLTNLFAAWL VGIYLFSSGF SPRRLWRILE GDDANSSAEP GSSHMKKKP
//
