ID   PBN1_YEAST              Reviewed;         416 AA.
AC   P25580; D6VQW4;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   04-NOV-2026, entry version 163.
DE   RecName: Full=Protein PBN1;
DE   AltName: Full=Protease B non-derepressible protein 1;
GN   Name=PBN1; OrderedLocusNames=YCL052C; ORFNames=YCL52C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=9090049;
RX   DOI=10.1002/(sici)1097-0061(19970315)13:3<199::aid-yea76>3.0.co;2-z;
RA   Lai M.H., Silverman S.J., Gaughran J.P., Kirsch D.R.;
RT   "Multiple copies of PBS2, MHP1 or LRE1 produce glucanase resistance and
RT   other cell wall effects in Saccharomyces cerevisiae.";
RL   Yeast 13:199-213(1997).
RN   [5]
RP   SUBCELLULAR LOCATION, GLYCOSYLATION, AND FUNCTION.
RX   PubMed=9649520; DOI=10.1093/genetics/149.3.1277;
RA   Naik R.R., Jones E.W.;
RT   "The PBN1 gene of Saccharomyces cerevisiae: an essential gene that is
RT   required for the post-translational processing of the protease B
RT   precursor.";
RL   Genetics 149:1277-1292(1998).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=15635094; DOI=10.1091/mbc.e04-09-0802;
RA   Ashida H., Hong Y., Murakami Y., Shishioh N., Sugimoto N., Kim Y.U.,
RA   Maeda Y., Kinoshita T.;
RT   "Mammalian PIG-X and yeast Pbn1p are the essential components of
RT   glycosylphosphatidylinositol-mannosyltransferase I.";
RL   Mol. Biol. Cell 16:1439-1448(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=16418276; DOI=10.1073/pnas.0505570103;
RA   Subramanian S., Woolford C.A., Drill E., Lu M., Jones E.W.;
RT   "Pbn1p: an essential endoplasmic reticulum membrane protein required for
RT   protein processing in the endoplasmic reticulum of budding yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:939-944(2006).
CC   -!- FUNCTION: Required for proper folding and/or the stability of a subset
CC       of proteins in the endoplasmic reticulum. Aids the autocatalytic
CC       processing of PRB1. Component of glycosylphosphatidylinositol-
CC       mannosyltransferase 1 which transfers the first of the 4 mannoses in
CC       the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts
CC       by stabilizing the mannosyltransferase GPI14.
CC       {ECO:0000269|PubMed:15635094, ECO:0000269|PubMed:16418276,
CC       ECO:0000269|PubMed:9649520}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9649520}; Single-pass type III membrane protein
CC       {ECO:0000269|PubMed:9649520}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9649520}.
CC   -!- MISCELLANEOUS: Present with 4930 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; X59720; CAA42392.1; -; Genomic_DNA.
DR   EMBL; AY692756; AAT92775.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07433.1; -; Genomic_DNA.
DR   PIR; S19382; S19382.
DR   RefSeq; NP_009878.1; NM_001178697.1.
DR   AlphaFoldDB; P25580; -.
DR   BioGRID; 30933; 256.
DR   ComplexPortal; CPX-1270; Glycosylphosphatidylinositol-mannosyltransferase I complex.
DR   DIP; DIP-8257N; -.
DR   FunCoup; P25580; 64.
DR   IntAct; P25580; 6.
DR   MINT; P25580; -.
DR   STRING; 4932.YCL052C; -.
DR   GlyCosmos; P25580; 5 sites, No reported glycans.
DR   GlyGen; P25580; 5 sites.
DR   PaxDb; 4932-YCL052C; -.
DR   PeptideAtlas; P25580; -.
DR   EnsemblFungi; YCL052C_mRNA; YCL052C; YCL052C.
DR   GeneID; 850305; -.
DR   KEGG; sce:YCL052C; -.
DR   AGR; SGD:S000000557; -.
DR   SGD; S000000557; PBN1.
DR   VEuPathDB; FungiDB:YCL052C; -.
DR   eggNOG; ENOG502QS8N; Eukaryota.
DR   HOGENOM; CLU_055666_0_0_1; -.
DR   InParanoid; P25580; -.
DR   OMA; ACDTEIS; -.
DR   OrthoDB; 5546453at2759; -.
DR   BioCyc; YEAST:G3O-29306-MONOMER; -.
DR   BRENDA; 3.4.21.48; 984.
DR   UniPathway; UPA00196; -.
DR   BioGRID-ORCS; 850305; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P25580; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25580; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:ComplexPortal.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IPI:SGD.
DR   GO; GO:0036503; P:ERAD pathway; IMP:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; NAS:ComplexPortal.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR   GO; GO:0016485; P:protein processing; IMP:SGD.
DR   InterPro; IPR042322; Pbn1.
DR   InterPro; IPR013233; PIG-X/PBN1.
DR   PANTHER; PTHR28533; PROTEIN PBN1; 1.
DR   PANTHER; PTHR28533:SF1; PROTEIN PBN1; 1.
DR   Pfam; PF08320; PIG-X; 1.
DR   SMART; SM00780; PIG-X; 1.
PE   1: Evidence at protein level;
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_0000058243"
FT   TOPO_DOM        1..385
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..405
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..416
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
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;  47923 MW;  65F7B920F0C2BBF0 CRC64;
     MVTRHRVTVL YNAPEDIGNH MRQNDTHLTV RGGSGVVLQQ RWLLERTGSL DKSFTRITWR
     PRADLARSLS VIENELSAGF SVYSNSSDVP ERFITNPVYN SFHSEKFDIE QYLPPEVDLN
     LSWNPEDFTY DISVEPTQIQ IVEYRLLKQG EEFTIARVKD EKLEVGVFFV DASDESDVDI
     GGIRCNWRMD DGKMERCQKT SLLYKQGHIA YNHSTTTTSL YLNEPIGLHP KIMIDLTDFE
     ERPKCMYLMH LQLPLELFID KFQSSPLLLF GEDDLELPEY SLRDKAWGSE SIFELKAGTM
     NEVTLHTRYI EPSNNKGDKL EVSFDPEVIL ACDTGDNKVS RNPFYKKGLG YESLFTDDTT
     FRHLNSTTLL VPIPRPDTKD YSKIKNGTLL CLLISIIYIF SKVFGNNKKK RSVKRE
//