PBN1_YEAST
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 03-AUG-2022, entry version 148.
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}.
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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; 252.
DR ComplexPortal; CPX-1270; Glycosylphosphatidylinositol-mannosyltransferase I complex.
DR DIP; DIP-8257N; -.
DR IntAct; P25580; 5.
DR MINT; P25580; -.
DR STRING; 4932.YCL052C; -.
DR MaxQB; P25580; -.
DR PaxDb; P25580; -.
DR PRIDE; P25580; -.
DR EnsemblFungi; YCL052C_mRNA; YCL052C; YCL052C.
DR GeneID; 850305; -.
DR KEGG; sce:YCL052C; -.
DR SGD; S000000557; PBN1.
DR VEuPathDB; FungiDB:YCL052C; -.
DR eggNOG; ENOG502QS8N; Eukaryota.
DR HOGENOM; CLU_055666_0_0_1; -.
DR InParanoid; P25580; -.
DR OMA; DKAWGSE; -.
DR BioCyc; YEAST:G3O-29306-MON; -.
DR BRENDA; 3.4.21.48; 984.
DR UniPathway; UPA00196; -.
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; IC:ComplexPortal.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IPI:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR GO; GO:0035268; P:protein mannosylation; IC:ComplexPortal.
DR GO; GO:0016485; P:protein processing; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
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 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
