ID   PBN1_DEBHA              Reviewed;         450 AA.
AC   Q6BKZ8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Protein PBN1;
GN   Name=PBN1; OrderedLocusNames=DEHA2F17512g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89505.2; -; Genomic_DNA.
DR   RefSeq; XP_461123.2; XM_461123.1.
DR   AlphaFoldDB; Q6BKZ8; -.
DR   STRING; 4959.XP_461123.2; -.
DR   PRIDE; Q6BKZ8; -.
DR   EnsemblFungi; CAG89505; CAG89505; DEHA2F17512g.
DR   GeneID; 2903673; -.
DR   KEGG; dha:DEHA2F17512g; -.
DR   VEuPathDB; FungiDB:DEHA2F17512g; -.
DR   eggNOG; ENOG502QS8N; Eukaryota.
DR   HOGENOM; CLU_044602_0_0_1; -.
DR   InParanoid; Q6BKZ8; -.
DR   OMA; YKINEWG; -.
DR   OrthoDB; 1537024at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000599; Chromosome F.
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..450
FT                   /note="Protein PBN1"
FT                   /id="PRO_0000246303"
FT   TOPO_DOM        1..413
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        435..450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   450 AA;  52197 MW;  E4483590972233E5 CRC64;
     MIRQRTTIFN PTKSNDGIIE AVDSSHLQLS SIDYQCEDKF ILQTPKFKYI DKLRIQLNQF
     HSESILFSKY QAGLNIYCKP KIGDEGFNQE EFFNELNQMM TNLFDIPRDG WINSLDTLFY
     HEPSTGSESF IEYVRKLTGN ESNVNLEVSP NIEYVYDGEK VVLKLNGKSL ANTTITKNSK
     FNKEIGLFLI EKGISSEDDI VLSGLRVILN GDDDKNEEYL QKTLFHVKRR QRQSRGTYSS
     QVKENGMHPF LKTDIHSDIP NDEDLIQCKL YYYLDLNKSF FVDKYQLPKE FTSYVNFGNT
     DLELPEYKIN EWGSEILMEI ENNQQISLPL HSRYQLPNNE SSIRVTGIND PLIFYGCDVK
     DSYLLESSPF DNRLDIGGNY ERFFTDNTVF YHLSSHENQL QINIPRGNES IKKINFVTNL
     IFIAGVVLIF YKIVQGIFKR NPSAGTRKNE