ID   A0A1J1HJN1_9DIPT        Unreviewed;      1041 AA.
AC   A0A1J1HJN1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   ORFNames=CLUMA_CG001416 {ECO:0000313|EMBL:CRK87620.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK87620.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRK87620.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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}.
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DR   EMBL; CVRI01000004; CRK87620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1HJN1; -.
DR   STRING; 568069.A0A1J1HJN1; -.
DR   OrthoDB; 5477082at2759; -.
DR   Proteomes; UP000183832; 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   Reference proteome {ECO:0000313|Proteomes:UP000183832};
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..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        707..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        765..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        905..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        938..956
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        962..982
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        989..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   REGION          828..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..848
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  119310 MW;  1D863A545621E3C8 CRC64;
     MIANSIFILF SFVCITLYLY GVLLTFSSVN HGNNDCKMTF MFEHPNYVKI DFEENESFPK
     YNLYAYSEGQ LTENARNLIF NGAPVLFIPG NSGSYKQARS LASVALRKGI DNDWFRHLDY
     FTVDLNEEYA ALYGGVLHDQ TQFIEHSISA ILKLYNRLPF PPKKIVIVAH SIAGKIAQKL
     LSSPDTAELI NTVITLASPM DKPVLNLDHH IDSFYKSVEG YWIKNRFIDE PLNSTCGVKR
     RKKLSNDQEK RKLDEKLLIT IGGGNKDLLV HSGLTDSKFS DIHAMTTAIS KVWVESDHLC
     IVWCLQLVLV VNRFLYSIIA PTQYKGPISK GLSFIEEKEA RLRKAEQYFL GLPPIPTNKE
     KTRKIDSPEK AEWLEDNRRI FTHQFKNGIN RTRIQMIRLV DNFLYHSVRV DVINRETNEW
     IYGCEAIETT SSSRFCSYAT LLPTNIVRKI PPQYPDHENF LLNLHELKAK NPKWTHVLLR
     FAPTREPFQY TVDIHNPSDR QIMFTMPKWY SFSTYKILDD TLLGASYYQF NVTDLDEQHQ
     ALEIIVTPKH CSKHITVGKV CIPWISGFDR YHQFEDNKNM ILWTPKTRPL NYNTTNYPIQ
     LELFLDPTCR YTIEIKQSFG QLLSKIVQQF SHWLPAHLVA LICLSIKHQI GLTPSGEKFK
     CGSLYKALGT CTPFFVMTVS RLFLKIIVLM KILPKPEVLP TSLTVSIIIH GTALALLTIL
     TGLIWTGITF CASIAHKILF KIVHLPIPIL SDTCISIIEK FPASVAALLI ALAFSSCGGI
     ALIVGCFVYF ILLSKMYEDY LENFVFNTAK LIAMKLFGRV RKSQNSEVIE EPKKSEEVEK
     PIVTSEVESE AEDKEEEEKI SQLLEEAMKK QREEKAKRDK ELASSRIEYD SLTEGLSDIN
     FHLPIFYLLL MSAMFSLPSV VTWARNYHYS KQLSPDPMLI PATCILTALG FIWQMPTPRN
     LYYYKAVGHF LYVTAVVSVL YCQDAIFKLN YVITAVIVVI AIHQFLAPKK QNDDEEAPPD
     FFDNLKTNFE KLREVKGFVQ K
//