ID   PBN1_CANGA              Reviewed;         416 AA.
AC   Q6FX62;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Protein PBN1;
GN   Name=PBN1; OrderedLocusNames=CAGL0B00506g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380948; CAG57892.1; -; Genomic_DNA.
DR   RefSeq; XP_444992.1; XM_444992.1.
DR   AlphaFoldDB; Q6FX62; -.
DR   STRING; 5478.XP_444992.1; -.
DR   EnsemblFungi; CAG57892; CAG57892; CAGL0B00506g.
DR   GeneID; 2886555; -.
DR   KEGG; cgr:CAGL0B00506g; -.
DR   CGD; CAL0127126; CAGL0B00506g.
DR   VEuPathDB; FungiDB:CAGL0B00506g; -.
DR   eggNOG; ENOG502QS8N; Eukaryota.
DR   HOGENOM; CLU_055666_0_0_1; -.
DR   InParanoid; Q6FX62; -.
DR   OMA; DKAWGSE; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000030; F:mannosyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016485; P:protein processing; IEA:EnsemblFungi.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR   InterPro; IPR042322; Pbn1.
DR   InterPro; IPR013233; PIG-X/PBN1.
DR   PANTHER; PTHR28533; PTHR28533; 2.
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..416
FT                   /note="Protein PBN1"
FT                   /id="PRO_0000246302"
FT   TOPO_DOM        1..381
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..416
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   416 AA;  47746 MW;  C48517B26EE03229 CRC64;
     MESVRHRIAL LFANEADIQD VETVEDGVIV FPNSNITIQD RWTYAIDYEL DSIRRISWRN
     PSSTRQFSVI ESRLAPGFNI YSNDKEARLN LFGIQPVYSP MYKSLHSETW KSINEILPGG
     KNLNIPWNPE LCDYDILITA NTVQVFSYCS LVEKKKFVKD AGKVEIGLFH VDTEDEEDIN
     LSGLRCTWED TSNNIGKCEK TTLFYKPFHL YVDDSSDIAP ITIENTNGLH PKMKIDLSGI
     RKDKDCRHFV FSQLPSEIFV DKFQSPGSIV FGLDDLELPD YKVNSLSWGS ESIVTLKEGQ
     INEITYFSRY LEPKERASNK TVGFEPILFK ACQVGKEEDL SNPFYSRSLG YEAYFSENTK
     FYHINSTSVH VNIPYPNKND IGNIEYTTFG IVVLAICYLI YKLLRPSRKL STVKRD