PBN1_EMENI
ID PBN1_EMENI Reviewed; 526 AA.
AC Q5BB40; C8VMT3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Protein pbn1;
GN Name=pbn1; ORFNames=AN2240;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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=CBF86444.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA63925.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000036; EAA63925.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF86444.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_659844.1; XM_654752.1.
DR AlphaFoldDB; Q5BB40; -.
DR STRING; 227321.Q5BB40; -.
DR EnsemblFungi; EAA63925; EAA63925; AN2240.2.
DR GeneID; 2874615; -.
DR KEGG; ani:AN2240.2; -.
DR VEuPathDB; FungiDB:AN2240; -.
DR eggNOG; ENOG502QS8N; Eukaryota.
DR HOGENOM; CLU_030047_0_0_1; -.
DR InParanoid; Q5BB40; -.
DR OrthoDB; 1537024at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..526
FT /note="Protein pbn1"
FT /id="PRO_0000246304"
FT TOPO_DOM 1..484
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 526 AA; 58675 MW; EA55F2137BD10936 CRC64;
MRQRITYIQK PSLPFHPSQT TLTRDSLYVE SLDAAREERV TFSFDELPSE LWQVLRQCHQ
LHIRWASERA FEAVSPLSSR ISPGLHVFYS PVEAGRAKRD SEGREPLCTL LKKVFDDELR
CESPEKSFIT PPILSKRFAS TTAYQFYELL PSLGNLVTYI QQKFCGTDDK CHQRAASILS
ADSVDINYDS ISHALTMSGF WSQAPGEQGW TETIGKHEGG TDKVEIGLLG AEPASEPEEI
KVGGLLAVVG QDEELKPTLF SFPSRHHPLH EDATYSVTFP PPTGLHPTMT ISIAPEALKE
PPRRPDATCA LHAYLTLPSK LFGDKYQLST TDPLFLKSHN LASLRAVAGE TDLEAPDWSI
SRWGSNWLLE LASPSESDEV AEEWNITIPL HLRYLPPSES GYQPASVPWP VVFWACSAED
GTKMGVNPFD RINLGWEGLF GPRTMFYQLH PSPSPEGGNL VEELEVPVLT LKENSGIFNS
QVIELGTFAV ISIGFLWVLW KLGLVARSSG IRPQHQRNPG KRDKAE
