ID   PBN1_ASPOR              Reviewed;         543 AA.
AC   Q2U910;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Protein pbn1;
GN   Name=pbn1; ORFNames=AO090701000218;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Required for proper folding and/or the stability of a subset
CC       of proteins in the endoplasmic reticulum. Component of
CC       glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the
CC       first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor
CC       biosynthesis. Probably acts by stabilizing the mannosyltransferase
CC       gpi14 (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type III membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGX family. {ECO:0000305}.
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DR   EMBL; AP007164; BAE61955.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2U910; -.
DR   STRING; 510516.Q2U910; -.
DR   EnsemblFungi; BAE61955; BAE61955; AO090701000218.
DR   HOGENOM; CLU_030047_0_0_1; -.
DR   OMA; HELHIRW; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000006564; Chromosome 5.
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:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR042322; Pbn1.
DR   InterPro; IPR013233; PIG-X/PBN1.
DR   PANTHER; PTHR28533; PTHR28533; 1.
DR   Pfam; PF08320; PIG-X; 1.
DR   SMART; SM00780; PIG-X; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..543
FT                   /note="Protein pbn1"
FT                   /id="PRO_0000246300"
FT   TOPO_DOM        1..503
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        525..543
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   543 AA;  60188 MW;  0A942C8DBF8D2B5E CRC64;
     MRRRITFVQR PETPFSLDQA VLTPDALALH GIDGAREERA TFSVDELPEE LSDVLKQCHQ
     LHVRWASERR YDAVAPFSSR VSPGLHVFYT PVDGSSEENK LKSLCALLKR AFDYGLKCKS
     PETLEESFIT PPILSTRFAS TAAFQYHSLL PTLDNLVAYI ENKICSSSDE QCLRYAASIR
     SADSVDINYD SISHSLTVLG YWSQSPKNGW TDEIRRHAAG TDQVEVGLLG TEAATEPEDI
     KMGGLLAVVG KDDQLSMLSS GLPSEFGVAY GYGTDDSWAE PTLFSFPSRH QPLPEDATYS
     ISFTSPTGLH PTMTISMPPS SLNSPPAPPD ATCALHTYLT LPSTIFGDKY QLSTTDPLFL
     DSHNLVALHA VAGETDLEAP DWFVSRWGSN WLLELATPSE SDQVPEEWNV TIPLHLRYLR
     PSESGYRSAS VPWPVVFWAC TAEDGTKMGV NPFDRVNLGW EGLFGTRTMF YQLHPSSDRL
     VEELEVPVLQ LDDKGFFQSK AIELGTMIVI GLGSLWVLWK LGAIAWSSGT RPQRKSTKQK
     KSE