ID   PBN1_YARLI              Reviewed;         523 AA.
AC   Q6C5K1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Protein PBN1;
GN   Name=PBN1; OrderedLocusNames=YALI0E17391g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382131; CAG79654.1; -; Genomic_DNA.
DR   RefSeq; XP_504061.1; XM_504061.1.
DR   AlphaFoldDB; Q6C5K1; -.
DR   STRING; 4952.CAG79654; -.
DR   EnsemblFungi; CAG79654; CAG79654; YALI0_E17391g.
DR   GeneID; 2911668; -.
DR   KEGG; yli:YALI0E17391g; -.
DR   VEuPathDB; FungiDB:YALI0_E17391g; -.
DR   HOGENOM; CLU_030047_0_0_1; -.
DR   InParanoid; Q6C5K1; -.
DR   OMA; FQSISEM; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001300; Chromosome E.
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..523
FT                   /note="Protein PBN1"
FT                   /id="PRO_0000246309"
FT   TOPO_DOM        1..486
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   523 AA;  59010 MW;  9ABC6B2BDAB4E73C CRC64;
     MRRRATILAD LQQHGDKISF KPGDNNKSKL TVSVNAPRQD RFSAPVSNAD LDVLNHVADV
     SVAWGRPSAA QQPVLFAAAY EPGLHVTVVK KQASEPRKWG EEKPSEAAPE LVHVAKFLEE
     QLGLPVDPKT FIESRSDYTY YDPLVGPEAF GHFVDKHSAC SDESEEFVND LDTFNYAQSA
     SFHIDHDKKE LVTEVTIPDL EHYFNQKKQH ISRACKNDRL EVGIFDLNNL ATSYAFRGVA
     ELKGLLHDST KEKPQETFLV IEPRHNIGAG SVSVDFERPV GLHPKSELKL RHIAIPTDHN
     DENDGVKHCR LFAKYSAPSS IFFDKYQLAD LERTTSEHPN GQGRLLALWG EADLEEPRYH
     TEGWGSEALV EIFPITDAPE GTPFNLNFTL PLHLRYEEPK EGETYEPNEA PWPLVFWVCA
     ETDEQLANFK QSPFDVTHNS YMRLFPEGVS YHHIGPREAN GRGFPLLSTS WGTPVADIDR
     FAAVRDYTSI MMVAGFLMVT IAILRKVFRG KAMSEELKEK KEQ