ID   PBN1_KLULA              Reviewed;         414 AA.
AC   Q6CV11;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Protein PBN1;
GN   Name=PBN1; OrderedLocusNames=KLLA0C00759g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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; CR382123; CAH01079.1; -; Genomic_DNA.
DR   RefSeq; XP_452228.1; XM_452228.1.
DR   AlphaFoldDB; Q6CV11; -.
DR   STRING; 28985.XP_452228.1; -.
DR   PRIDE; Q6CV11; -.
DR   EnsemblFungi; CAH01079; CAH01079; KLLA0_C00759g.
DR   GeneID; 2892115; -.
DR   KEGG; kla:KLLA0_C00759g; -.
DR   eggNOG; ENOG502QS8N; Eukaryota.
DR   HOGENOM; CLU_055666_0_0_1; -.
DR   InParanoid; Q6CV11; -.
DR   OMA; DKAWGSE; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000598; Chromosome C.
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; 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..414
FT                   /note="Protein PBN1"
FT                   /id="PRO_0000246306"
FT   TOPO_DOM        1..390
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        411..414
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  47378 MW;  CB87E43CFCC60416 CRC64;
     MSVQTIQSES FIEEKRRITV LLDRDGRSVE EKVVNRDGVI TIPNQSGHVQ DRAVLFVPQL
     ASRPDFIHIS WKRNAEADIT PIKSYIPYGF NIFTNSSGSI AKFIDTPVGK VYYSDTFEDN
     ALSKWFPPEF VDQLLRYSED NDLDITVTRG RVEVNRYYEL TDDNLFPLNG TESVKTEAGI
     FQVDTEDDTD TSLSGLRCTW HTGSGALNKC QRTLFFYNQI YADKSSLSEV SLTLSEPVNL
     HPVVQIDLTS KRPIHNCEYY AYFNLPKYFF IDQFQSIPTL LFGEHDLELP EYKLSGFGSI
     SLFTLQPGSI NEVTLHSRYI KPTNDGSAFF EAAFTPQVFY ACDTSIELTK RSPFYTGKIG
     YEHFFTDNTK FYYLNSTKMT INLPKLDSSD NLCIQLFTLG LVLFSVLYLI RKLF