ID   PBN1_NEUCR              Reviewed;         501 AA.
AC   Q7RYM7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Protein pbn1;
GN   Name=pbn1; ORFNames=NCU00101;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 gim-
CC       1/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; CM002238; EAA27989.1; -; Genomic_DNA.
DR   RefSeq; XP_957225.1; XM_952132.3.
DR   AlphaFoldDB; Q7RYM7; -.
DR   STRING; 5141.EFNCRP00000000076; -.
DR   EnsemblFungi; EAA27989; EAA27989; NCU00101.
DR   GeneID; 3873388; -.
DR   KEGG; ncr:NCU00101; -.
DR   VEuPathDB; FungiDB:NCU00101; -.
DR   HOGENOM; CLU_030047_0_0_1; -.
DR   InParanoid; Q7RYM7; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
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; IBA:GO_Central.
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   Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..501
FT                   /note="Protein pbn1"
FT                   /id="PRO_0000246307"
FT   TOPO_DOM        1..458
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        480..501
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  55527 MW;  96D027A7904009C7 CRC64;
     MRERITFIQK QGDSIEPTTL KIKGGVLNGP EIQAAREDRL TIAIDELPKD LQALLGTAHE
     LHIRYVSSQP YEAITPLLAR LPPGFHLFYT PAGQADATSP ALCLALNQIF GNVQCENPEK
     SFTTLPRDRF SHSAAYQFYQ PSVDLSPFIA LVKEKLCSSS KDQSCAARAD RLANASSLDI
     SYDAISHAVK LTATWPYQKQ EVHATSRPQT RTEVGVLNSD RPGHLEPHEL GISGLLTVLG
     QDKKPSATMF AFASRHRDAE SSFSAEFLEP TGLHPTLKLR LESSKPPIED AYCSPHAYFT
     LPKTIFADRH QLSDDLFLAS KNLTGLRYIS QPVDLEAPEY VEKRWGSSLL LELSPPEHEE
     SKSWTVQVPL HLRYLSPAEG GYTDIQVPYP AVFWACAAEE GTKFPNNPFE KANLGYDGLF
     GPRTVFWHVE PRPTIGSRLS NMIKVPVLDT NKAEWVSGGT GLAVLLGFAW IMWKLFGVLS
     KSGYQNQPSQ AAEVVKAKKN Q