PBN1_ASPFU
ID PBN1_ASPFU Reviewed; 489 AA.
AC Q4WU12;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Protein pbn1;
GN Name=pbn1; ORFNames=AFUA_5G06810;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL91914.1; Type=Erroneous gene model prediction; Evidence={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; AAHF01000003; EAL91914.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_753952.1; XM_748859.1.
DR AlphaFoldDB; Q4WU12; -.
DR STRING; 746128.CADAFUBP00005324; -.
DR GeneID; 3510875; -.
DR KEGG; afm:AFUA_5G06810; -.
DR eggNOG; ENOG502QS8N; Eukaryota.
DR HOGENOM; CLU_030047_0_0_1; -.
DR InParanoid; Q4WU12; -.
DR OrthoDB; 1537024at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002530; Chromosome 5.
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..489
FT /note="Protein pbn1"
FT /id="PRO_0000246299"
FT TOPO_DOM 1..448
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 489 AA; 54773 MW; 3A5ED84523BA45BC CRC64;
MRRRITFVQR PESPFHVDQA VLTSDALSIT HLDAAREERA TFGFDELPAE IWQVLKSSHE
LHIRWATERP YEIGAPFSSR ISPGLHVYYT PGTARETGVG LCSLLKTVFD ESLECQSLRY
YSRLPSLQNL VAFIQHKFCD RSDEKCVHHA ESILSADSVD VNYDSISHAL TVSGYWSTSP
GQGWTEQIRK HAADTHQVEV GLLGVESATE PEELKMEPTL FSFPSRHHPL PADATYTVSF
PAPTGLHPTL TISMPRASLR RPPAPPDATC ALHTYLTLPS WIFGDKYQLS TTDRLFLSSH
NLAALRAVAG ETDLEAPDWV VSRWGSNWLL ELATPLRPDT SPEEWNASIP LHLRYLTPSE
SGYRSAAVPW PIVFWACTAE DGTKMGVNPF DRVNLGWEGL FGARTMFYQL HPAPAEGKDR
LVEELDVPVL RLREDAGFFQ SKTIELGTVV VVGLGLLWVL WKLGLVLWIA GTGRSTRAQK
RTDKHRKAE