PBN1_GIBZE
ID PBN1_GIBZE Reviewed; 493 AA.
AC Q4IBD0; A0A098DZ47; A0A0E0SJN1; I1RNB0; V6RB05;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Protein PBN1;
GN Name=PBN1; ORFNames=FGRRES_05478, FGSG_05478;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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; DS231665; ESU11444.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF86644.1; -; Genomic_DNA.
DR RefSeq; XP_011324020.1; XM_011325718.1.
DR AlphaFoldDB; Q4IBD0; -.
DR STRING; 5518.FGSG_05478P0; -.
DR EnsemblFungi; ESU11444; ESU11444; FGSG_05478.
DR GeneID; 23552659; -.
DR KEGG; fgr:FGSG_05478; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G18013; -.
DR eggNOG; ENOG502QS8N; Eukaryota.
DR HOGENOM; CLU_030047_0_0_1; -.
DR InParanoid; Q4IBD0; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniPathway.
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..493
FT /note="Protein PBN1"
FT /id="PRO_0000246305"
FT TOPO_DOM 1..453
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 493 AA; 54512 MW; 2333AD783CBC8CED CRC64;
MRERVTFIHN DYSLDPEALD NQDAGLLGPQ IETVRQDKLT IPFGELPSEL TDILQEYEAL
HIRWASPVKS ETMDPFTSRI SPGLHVYATP VLPSSCNPTK LCSWLQRFGP LDCSKPEAFT
EFQQSTSTSP SFSFYEALED LHSFITTSSQ EFCPELDSVC NARLRSLLTA SGLDLSFDKA
ANALVVSALW PLRPQTVAVP ASSARRVEVG IFINDRSQPN MKENELGVAG VLSVLGDQKK
PSPTIFTFPA RHRRDGSVFT SKFLTPTGLH PTLQLSFNSN KLPSADGECA PYAFLTLPKT
IFADRYQLGD ELFLASKNLT ALRYTTLPVD LEAPAYTTET WGSSILLGLA PPDPGTEKPW
SVEIPLHLRY LKPSATGQVE IEIPYPAVFW ACSSEEGTLE SPFDRLHVGY DYLFPRDTVF
WHANPQPENG SRLMNRVTVP VLDDDGVGSI RSGTAIAVAI GFAWVMWKLV SVMLKSDRAP
AGVTKETKQK KSH
