ID H2ASI6_KAZAF Unreviewed; 1028 AA.
AC H2ASI6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 22-FEB-2023, entry version 45.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN Name=KAFR0C03440 {ECO:0000313|EMBL:CCF57336.1};
GN ORFNames=KAFR_0C03440 {ECO:0000313|EMBL:CCF57336.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57336.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF57336.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650823; CCF57336.1; -; Genomic_DNA.
DR RefSeq; XP_003956471.1; XM_003956422.1.
DR AlphaFoldDB; H2ASI6; -.
DR STRING; 1071382.H2ASI6; -.
DR GeneID; 13885255; -.
DR KEGG; kaf:KAFR_0C03440; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; H2ASI6; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000005220; Chromosome 3.
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:UP000005220};
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 70..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 716..738
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 758..782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 828..847
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 859..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 884..902
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 914..936
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 980..999
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 1028 AA; 117263 MW; D2FE71A130C18D40 CRC64;
MGLSRTLGGI YRRGTFELKK WKYDDVATTT KQIDSAQLLG AVNTNHENKT NKVHDSDLPV
GQRYSKNFKL SSYFGILCIL LLSCICYFRI LDGADSSQCR PIYMYPSYAR IDGFDTRFNT
LAKKYHLYLY REQGLDTEPL ADQEIQLDGI PVLFIPGNAG SFKQSRSIAS ECANIFFKSR
DDIEHANTRN LDFFTADFNE DFTAFHGRTM LDQAEYLNDA IRYILALYQE SASYKNSDMP
LPQSVLIVAH SMGGIVARLM PTLENHIAGS VNSILSLSTP HAASPVTFDG DILKIYKKIN
DYWRTQLDDE SSFFSQNMSL VSVTGGISDD VLPADYAAVH DLLPQTNGFT TFTTTVPQVW
TPIDHLAIVW CKQLRTIIAK LLLEMVDLRT HSKTRPLNER IQLSKNFLLS GFESYFIEDS
PIRNPKTMAM NIDTTFSSGT TELQANQTLT LKKNTLTEEH KFYKVVLPKN KNHPYSFSLI
TSLDSVKVLF CFTNPRTSTL SSIRCVDGNN NMRIVPNSSE ETKYPADSSI GESMRHFKLL
TVGGQDLESY DFIIIEKPDE GAFQTDDDFV EASLAANEEV IVDKVSPLHL FFKGRTIRLY
SDNTLLTKDL QFTNLWDSLF SYRLRIKGQT GKNSAFQPFI RQWINEPFET KWHLNILHNN
KVDINFHNVA PFIPVNISAP KPLHLSTTLP HDTKIEITLN INWSLTMKML FIRYRLAIAS
FPTSILALII ACQFYTYYKS SKFVSFPSML SHTLEKYGIS LLFIYMSLSP LVNLECIQRL
LYFFDPIKLN KPFLLENKRM LTNFYFLGIR SWLMSWIGPL FATMAVGALY AICKIIDLLT
ILARNFVSGR SVKRSTTRVF IDRYRILSCC LLAAGVVFYI PYQLAYVICV VIQLGTCLRV
MLGTEDKNLL NYNVSLLLLM LFTMAIEIPT IIVFLHNVSI GWEATFNSHH NSMSILPIVM
LVSSNSNFNM PHFGKSSIDW HAISALLGYM SIFSLIYGIR NLYWIHYILN IVFCWLFYGS
IMNYVNAI
//
