ID M7X9I5_RHOT1 Unreviewed; 1155 AA.
AC M7X9I5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=RHTO_03610 {ECO:0000313|EMBL:EMS20374.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS20374.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS20374.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS20374.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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; KB722662; EMS20374.1; -; Genomic_DNA.
DR RefSeq; XP_016271493.1; XM_016417280.1.
DR AlphaFoldDB; M7X9I5; -.
DR GeneID; 27367623; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000016926; 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 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 735..762
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 792..813
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 850..883
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 985..1006
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1012..1033
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1054..1071
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 506..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1155 AA; 124426 MW; 6D67104E6FF6CA44 CRC64;
MARSRPPAPT AASQHRTAFP RLSAFLVGLS LTSLAICLAI YRSYVATQPY YPPGSLPEDA
RGGGAGSCRM SFMSPAYMHL SGFGREFTRL GNGPWGLYLY REAGWDDNPF VEDGRGGQKL
QLSGTPVLFV PGNAGSFRQV RSLASAASRA WFEVPGVPRK GVGTREGGAS LDFFTLDFND
DFSAFHGQTL LDQAEYTADC IRYILSLYAH HEDEATGRNR RPDPTAVIVV GHSMGGVVAR
AAFLNPNYQS HSISTLITFA TPHVVPPVTV DAGVDRVYEA INSYWRDAYE LSTSPTSSFT
AIEPPSPALA SFRAPPHEEL RDLVLISIAG GLSDVTIASE SVSLASLLPV DGSNGFTVFT
TAIPGVQTPI DHLAILWCQQ LMQTVAQGLL AIVDVRRASG VSSREERVAE LGRRWLGSLE
LPPKEDSSAR RVALDAVVRG QSSTQLKVGE RLVVRPDDVI AGRRTYILPV PPTRTYTGPR
VFRLLTSASI GRRKDDFVEV WACEASGSTR QQPDNDKGRS ALDETEGSPC TALYPRHVTT
LPSSPHSSVS PILPAPVEHG SISLVSLDAQ QLEGKEAIAV VVKEGGSPWV LAEFADAEKS
IHVVEKGALH LLLNGYKLEA LPATPAMVSE VWLPALDTSL LTLKLRVYRS ECQEHTSLFA
PLLRQYSSTV HESKYFPNVR LASLYTHSSG PYLPPASSPF SASGTRLQFF LDPTCARPAG
PGETADLALE ISVDVWATLG ALVVRYRMAM VTVPFAFAMF VLGRQIREYN GGAPFPTFGA
ALSNVSRRTF PLLLAGLLVL SYIQSIALSG HMASRDHLAS VEPAHHRHSH LSLPPSWLAN
LMLGNSGSFW APLVPILAFA ILSVVVFEYV ALSAIVGGVA WSIRQLQARG PARLRPFVTL
ADTPDTLPLQ RVLTMIVLLL LVLFFAPYQF AYLVIVLVHL FSTIRCLVLA QEAAPASTPS
ASAGPSSAVT AAAARRLWDR YHYTFSILFV LVTLLPINAL ILVVWVRNLA VGWLAPFSSD
HNVLMVVGFL ANVEALHSGK MLQRSAGGRY SPTVTLLAFV IPATYSLLYG IRAAHRLYSL
ANLCFLWLAL GTSDGFVGST GASPTAGDAG LVDVPPRDVK RRCSSPPEPT DDLVGEGGVA
RKVATLGTAG GPSRR
//
