ID A0A0L0GAB7_9EUKA Unreviewed; 799 AA.
AC A0A0L0GAB7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=SARC_02009 {ECO:0000313|EMBL:KNC85826.1};
OS Sphaeroforma arctica JP610.
OC Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC85826.1, ECO:0000313|Proteomes:UP000054560};
RN [1] {ECO:0000313|EMBL:KNC85826.1, ECO:0000313|Proteomes:UP000054560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP610 {ECO:0000313|EMBL:KNC85826.1,
RC ECO:0000313|Proteomes:UP000054560};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Sphaeroforma arctica JP610.";
RL Submitted (FEB-2011) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; KQ241682; KNC85826.1; -; Genomic_DNA.
DR RefSeq; XP_014159728.1; XM_014304253.1.
DR AlphaFoldDB; A0A0L0GAB7; -.
DR STRING; 667725.A0A0L0GAB7; -.
DR EnsemblProtists; KNC85826; KNC85826; SARC_02009.
DR GeneID; 25902513; -.
DR eggNOG; KOG3724; Eukaryota.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000054560; 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:UP000054560};
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 732..763
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 694..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 87399 MW; BCEB6A3C58CEE92D CRC64;
MILALASVIS LCSVLLLGGG LHFLLANRMD PNYCHMTYMY QNPVYTSIQV KNGPANNDRR
YRLLQYTEGI IRGNECKGRH PVLYISGNSG SYKQVRSIAS IAADMDRTNY LIKGSPRRPL
SFFTVDFNEE LSALFGGVLP VQSEYAAHCV RHLQSMCTKP SGTGKLATVT ILGHSMGGLV
ALSLLNSDVL QAGSIETIVT VATPHRPVLA FDYRLGSFYH TMNSAVLRSA TQNVTLVSIE
TGIRDFQVRA DLASLGMTGP NIVHASTSGI PGAWLSCDHL AAVWCKQLVL PILTAMSVLS
LPSPKAADAV GNFQSTSDIA RANERAERYR STLLPAAEFI HTTTCDSADS TTSTIGTTDE
KMWPSPAQTL QDRTGVARTI KIALGGSPET TSSTETLAIS TTETISSLSL CSVRQCYACG
NGSCVSNADE LELRLETQRL PYWRDTFKGA NVRPPQHFDN LRRPVTAVLI HRMNHLRSPQ
SWEDIHLEMV LNAAGSEQAK APVYSSEKGF VSIGWSSGVS NVFATPFYGQ TLAIESSDQH
HRVRVAQPLE SCLITSILRF KLMHSETGED CPTNSAGYIA THVSNRRATT AQHYSANTHT
RGGVQFEHVL RPCDATFDKI QSYVAMDIDV WDTRYQLDDR LNCVVFVDRN FNNYKPSRTN
FVPAEYYTIF TVMGCLQMCR LKVALTFSPT NAATDPCLSP RSKQSPAPDV GNKARLPENP
SDAFYFELDS KFVAFGVGLC AVAILVTGCS GIGVAIAAVI SVVQSIRERA DIQCEATAQN
NRAKDNSWID SQVRLYSTQ
//