PBN1_SCHPO
ID PBN1_SCHPO Reviewed; 332 AA.
AC O94472;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Protein pbn1;
GN Name=pbn1; ORFNames=SPCC1919.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329672; CAA22633.1; -; Genomic_DNA.
DR PIR; T41227; T41227.
DR RefSeq; NP_588484.1; NM_001023475.2.
DR AlphaFoldDB; O94472; -.
DR STRING; 4896.SPCC1919.02.1; -.
DR MaxQB; O94472; -.
DR PaxDb; O94472; -.
DR EnsemblFungi; SPCC1919.02.1; SPCC1919.02.1:pep; SPCC1919.02.
DR GeneID; 2539243; -.
DR KEGG; spo:SPCC1919.02; -.
DR PomBase; SPCC1919.02; pbn1.
DR VEuPathDB; FungiDB:SPCC1919.02; -.
DR eggNOG; ENOG502QS8N; Eukaryota.
DR HOGENOM; CLU_837176_0_0_1; -.
DR InParanoid; O94472; -.
DR OMA; IFACMSE; -.
DR PhylomeDB; O94472; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:O94472; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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 Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..332
FT /note="Protein pbn1"
FT /id="PRO_0000246308"
FT TOPO_DOM 1..301
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 332 AA; 38483 MW; 899DE5FE8A4AA182 CRC64;
MDLQRTNQDT GTTTLFKVVI SNTVNYLPKG VWILRNNTID SLSIAKQFRE IKNNINISHL
SRENYWVETP FGKVFHSEVV SEEFMQIFID KGNKALNNEE MIFACMSEKG WNVSLETVPN
LDIPVGSYET QLGLPVGLHP KLHVHLKNLH KPEDECSLQG FMYIPPTLFI DRYELSNIAE
MHADNLGHVL GIWGETDLEA PSYKLNGTGS FFWFDIYTDD GLLQKDYIDT IIPLHTRYQS
PLKGQTYLKT SLTNPKFFWN CDTEDKVNDF RFLFSSKNKY TLQNDPTTLS ISIPIADLSY
KHVVEWVTNG VAIFSFFYLL LYLWKRFRYA KD
