ID W1QFK6_OGAPD Unreviewed; 1040 AA.
AC W1QFK6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=HPODL_03632 {ECO:0000313|EMBL:ESW99761.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW99761.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESW99761.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) 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|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:ESW99761.1}.
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DR EMBL; AEOI02000007; ESW99761.1; -; Genomic_DNA.
DR RefSeq; XP_013935433.1; XM_014079958.1.
DR AlphaFoldDB; W1QFK6; -.
DR STRING; 871575.W1QFK6; -.
DR GeneID; 25773068; -.
DR KEGG; opa:HPODL_03632; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR OMA; WVRNLAV; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000008673; Chromosome IV.
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 Reference proteome {ECO:0000313|Proteomes:UP000008673};
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 698..720
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 799..832
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 853..869
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 943..961
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 973..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 998..1016
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 1040 AA; 117842 MW; 76C1F06E6621F9D2 CRC64;
MPPTLVTPRY VLLILTLCGL SLLSLIAFSF LEQLDGPDSA KCRSVYMSPA YARVHGFDES
HTRFASKYSL YLYREQGRDT LPNNDGQSLR LTGTPVLFIP GNAGSYKQVR SLASQSANSY
YTELEKFKEL NPHVNSLDFF AADFNEDFTA FHGRTMLDQA EYLNDAIGFI LSLYRHNPTP
ARSVILVGHS MGGIVARVML SLPNYVEDSV NTIITLAAPH AAAPATFDAE LLHVFAATDD
FWRHGFVSLD SDDSGFSKIA RRRLENVSLV SITGGLLDNM LPADYTSLTG LVPETNGFTI
ATTGIPGVWT PIDHLAIVWC DQLRKVIASS LLQLVDKTSV SQTYPLQKRM EILRKNLFTG
FEADATQDFD SYKAGAGKLD LPYKLKIDTK QFKDTSRQRN LQLPNSKLKR DLLSSPDMHL
FYIPKDGLKF KFNFLSSLKP VDISRLGEGL ASPSILLCRT LNPDGRSFKE EFDYTTGTTS
KAVQLECIDI HRDAHEIPRS YNDSISSSES SLGGEKRPFY SIQLDSRVLS MFDAVVIAES
PVPVESPEFV LADLELTQST DLVLGDYSLW TLLSRGYDIT LPAHRPLSIS IKIPSAWSSL
LAYNFDIRYQ QSQMERFSPM ISQRIRDETK WHINLHQDKS ITALIQGISP YCPFTRDDTS
SLELQLFSDS LASDQIMDIY LTVNWFKSLK LLVLKYRLSI FSFPVFITTL VFFLQFRKYI
KEDVFPSFGE GLLMLCDPHM LFPLALVLSV LSSFASHRFF QKLLSYIDPV DFGNKTLMHE
IAKSDVFVNL YFLGLEEKAL WFFGPVVLVI SLSLVCAFYN LLQVLLWTIV MVMRKLHFPC
LLKPGMSGNY NKRRALGTAL ILTLVPLYIP YQFPYVVSCL VQCTVVIRAF VTSSGQKHVS
VENFRNFNFS LLILMLWILP VNIPVLIVWI HNFSLRWATP FSSHHNFLAI ISIVFLVQNN
VAGNIIPRPT SAVTIFVTKF VIIYFSLCSL IYGTRHLFWL HYLFNFLCAW LLCLLLEDVW
KKQVKNVTMF KKEDTPSKLN
//
