ID   PBN1_ASHGO              Reviewed;         413 AA.
AC   Q751U2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Protein PBN1;
GN   Name=PBN1; OrderedLocusNames=AFR733W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 23-24.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS54105.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016819; AAS54105.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_986281.2; NM_212417.2.
DR   AlphaFoldDB; Q751U2; -.
DR   STRING; 33169.AAS54105; -.
DR   PRIDE; Q751U2; -.
DR   GeneID; 4622572; -.
DR   KEGG; ago:AGOS_AFR733W; -.
DR   eggNOG; ENOG502QS8N; Eukaryota.
DR   InParanoid; Q751U2; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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..413
FT                   /note="Protein PBN1"
FT                   /id="PRO_0000246298"
FT   TOPO_DOM        1..378
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        402..413
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  45418 MW;  AFEA0C011A5A5CEA CRC64;
     MQSVRQTVLF ESEEAWRAGA EQNATAITVH ARGGEVVQTR RTWAAAGGPR VRVTWSGGRT
     VSEVSPQLAA GLSVYVEGGA HVSRDFVQAR GQAVFHSAQL ELDAVRAWWP RELAVQPEAL
     RWAECAYDIE LGRQVRVDEY CALRAGETVA LTAAAGGTDE AKVETGVFYP EISDGADVSL
     SGFRCTWLRD GSGRTDTCQK TLLMYKPAHV HMPEPAVGIE LVQPVTLHPV IEVDLSSVSA
     SGPACAHHVF LQLPAQLFVD KFQQPPELLF GEDDLELPEY KVEAWGSEVI YALEPGRVNR
     VQLHSRYARP GPGRRYEVVP LRPYVFEACD TGSADIAENP FYSKGMGFEA YFTADTVFKH
     RNSTRLNIPV PRGNSNDFPS IQYVTVLSIL FSVLYISYCL FRRPVAASAR ASG