BST1_NEUCR
ID BST1_NEUCR Reviewed; 1256 AA.
AC Q7SAM0; Q6MFS7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=bst-1; ORFNames=B2N18.110, NCU08021;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE85512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX897674; CAE85512.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002239; EAA33455.1; -; Genomic_DNA.
DR RefSeq; XP_962691.1; XM_957598.3.
DR AlphaFoldDB; Q7SAM0; -.
DR STRING; 5141.EFNCRP00000008286; -.
DR ESTHER; neucr-q6mfs7; PGAP1.
DR EnsemblFungi; EAA33455; EAA33455; NCU08021.
DR GeneID; 3878857; -.
DR KEGG; ncr:NCU08021; -.
DR VEuPathDB; FungiDB:NCU08021; -.
DR HOGENOM; CLU_006103_1_0_1; -.
DR InParanoid; Q7SAM0; -.
DR OMA; LLVWAHN; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050185; F:phosphatidylinositol deacylase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495; PTHR15495; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1256
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277640"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1103..1123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1130..1150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 37..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /evidence="ECO:0000250"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1256 AA; 140123 MW; 41B003D0E5EBFFD4 CRC64;
MRTRLAGTSE DGHLCPVEAP FPNVDFLLHQ QLQQEQDVYA NSTTNATASP PIAPTSVLPR
PSRPSQSSAA ERTSPESPSV RQSPTKRDRN PGPSSISGAG PLNLEHQSPS QQSQNQQQQQ
QQQQQQQQQQ QQQQSFYARS RRSGNFNWKL SHSRNGSIEK PPPSFFSSSF SHSPSTPPLS
LGAPANGAAH SKEMEKEEEQ KFVGKRPRIR SPWAITFVTL LISILGIGFL ALVLNSSFTR
HIDPKGCRMS YMRPGYAKFD DFDTEHTRFA SKYSLYLYRE LGIENDAKVR GVPVLFIPGN
AGSYKQVRPI AAEAANYFHD VLQQDESAVK AGARSLDFFT VDFNEDITAF HGQTLLDQAE
YLNEAIRYIL SLYLDRTRSD RDPNLPDPTS VIVLGHSMGG VVARTMLIMP NYQANSINTI
ITMSAPHARP PVSFDSEIVK TYKDINDYWR RAYSQQWANN NPLWHVTLVS IAGGGLDTVV
PSDYASVESL VPDTHGFTVF TTSIPNVWTS MDHAAILWCD QFRKALVKAI FDVVDVNRAA
QTKPRADRMR VFKRWFLTGM EEVAEKTVPS KDPSTLLTLE DNLSSVIAQG ERLVLRSLGA
SGAVRAHLLP IPPSGSPEAK RFTLLTDHKL DVSSESGRLE VLFCSVFPMQ PGQAVAGFAA
QINLAGDSSA STRLACNNAA SDVVTLPASL RSSQYPFSKE GEPPKTHFSY LQYDVEDIAE
HQYVAVIEKT HTPTPGFVIA EFSDVSQSHR TRHISLRRLL AFGMKFRLPS SRPMVSELKV
PTMQSSLLAY NLEISEQNCG KQQELFAPLI RQYLTEPYES KFFVNAREAA VSIHGVAPYV
PPPLKSRSTE DGLSFQFWTD PTCASNINIK MSIDVMGSLG KLYMRYRTVF AAFPLLVVTL
VLRKQFRIYD TTGVFISFSE SLDLCLRQSI PLVLAFLTFL SLFIWNSSSS ATANIWNWAN
VTSGAIDFHQ NDLLIGTQDP FFWFLVPVIG LICVGICTVF NYMTLTLVHI LSTAVSLLSF
RPGWIRNDER RKALPLPAFY PTSPRRRMVT TAILLVLVST LIPYQFAYLV CCLVQLTTTV
RAQRLASDLR SAANSNFYNY VHSILLLMLW ILPINLPILV VWIHNLAVHW LTPFSSHHNV
LSIMPFIILV ETLTTGKMVP RVNSRFKHFT SVLLFGIALY AAIYGVSYAY MLHYLVNLVA
AWLAIVHSTS DNWSVLSGIK HISCTLFDAG NTNNVGGVNG TNNTMLAEDC KMRKEP
