ID A0A099NV62_PICKU Unreviewed; 1103 AA.
AC A0A099NV62;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=JL09_g4113 {ECO:0000313|EMBL:KGK36728.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK36728.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
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:KGK36728.1}.
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DR EMBL; JQFK01000055; KGK36728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099NV62; -.
DR VEuPathDB; FungiDB:C5L36_0D06470; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR Proteomes; UP000029867; 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 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 767..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 830..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 887..913
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 972..994
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1006..1024
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1036..1054
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1061..1079
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 125228 MW; 96C97B950000CD19 CRC64;
MTPAKPSMST DTDNSTNSDG TDTKDFFNDI LPSTTNYLIL IGSSIVGFVL LIAITLSFFK
PFDGPDVPNC KGVYMSPAYA KVHAFDSTHT RFASKYSLYL YREQGKDSMP GESSEFYLSG
TPVLFIPGNA GSYKQVRSIA AEAATQFFDK SSYVTSQNSN ANNVDFFTAD FNEDFTAFHG
RTMLDQSEYL NDAVKFILSL YDSNSSNTSP TSVILLGHSM GGIVARVMLS LPNYLEGSVN
TIITLSTPHN AAPTTFDGDL LNVYKLTDDF WRNGFSHDVS TLSTKMATIA RRRLENVSLI
SITGGVLDTT LPTDYTSLTG LVPSNHGFSV STTGIPGVWT PIDHLAIVWC DQLRKVLAKT
ILQIIDVNSP SQTYPLEKRM EIFKSNLLPG FDKFLDIMKY TNIQHNLPFK LKIDLKQLKD
SINERFFQLP RKNAKRDIAG FPPIHLFNIP RKESSKFNFI SSIKPTMIDK ITSSVELSLL
LCRSILSDVG KASAKRNFRK VFDYTTDITQ QYAELECIDV SEYIYVVPKS YSSNNEHSNE
PTDVYYSLEI PSNILSYFSS IVIVEPKTIL TESSENFVLA DLHSESSSAL TLGDSSLWKL
ITRGNDLTIP AHRPIIIDIN VPSMKSSLLA YRLDVRYAKS SNEKFSPLIS QTIKGETKWH
INIDDDKIIT SIINGDSPYT PFIVDDPESH TRFKVFSDSF SSDQLMDIYI TVDWFQSLKL
LVLKYRLSVV GFPLFFTLLV ITLQFRYYSK TNLYPSFGET MLSVCDYRVV TGLVIFFSFL
SKLTSSNSLF NKFIEFMDPV ERNELHLMEK IENAEVRLNV SFMSIEEPSL WFYGVFVLFI
SIGLNFLLYN LILLVIKCLI YLSELGLLQG ITSNIHSFPN QRKTIGIITL LFLVLLYLPY
QFAFVVCVLT QLFSTLKLFL SNTKLNSYHT SYKNFDDYKG KKDSVPDNES NEKAVVSNKA
LYFVDNFKNF NLSLLILMLW LVPINVPVLV VWLHDISLKW RTPFSSHHNI LAILPIIYLV
QALNQGFMVP RPTKRFNVFF TKVILFYFAF YCLFFGTRHL YLLHSLFDAI CTWFLILYIQ
GWGNGSLENI RTITIIKNET KIH
//
