PBN1_CANAL
ID PBN1_CANAL Reviewed; 481 AA.
AC Q5A4J4; A0A1D8PPL2; Q5A4Q8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein PBN1;
GN Name=PBN1; OrderedLocusNames=CAALFM_C601370WA;
GN ORFNames=CaO19.10951, CaO19.3447;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017628; AOW30078.1; -; Genomic_DNA.
DR RefSeq; XP_716754.1; XM_711661.1.
DR AlphaFoldDB; Q5A4J4; -.
DR STRING; 237561.Q5A4J4; -.
DR GeneID; 3641607; -.
DR KEGG; cal:CAALFM_C601370WA; -.
DR CGD; CAL0000174087; orf19.10951.
DR VEuPathDB; FungiDB:C6_01370W_A; -.
DR HOGENOM; CLU_044602_0_0_1; -.
DR InParanoid; Q5A4J4; -.
DR OrthoDB; 1537024at2759; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q5A4J4; -.
DR Proteomes; UP000000559; Chromosome 6.
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..481
FT /note="Protein PBN1"
FT /id="PRO_0000246301"
FT TOPO_DOM 1..451
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 481 AA; 55568 MW; D6651B7327A4E7B7 CRC64;
MRQRTTIYNP YSSHDGIITN LNRTNFQLSS IPNHLFTIEN KYTITTTTTQ PNKSSLYSAI
KELRIQTKFN NNESGIPIFS FHYEPGLNIY AVPQSNVDKL EFWQQVEQLI MELLGIKLSS
QQWIANVNSF YYHDIQPQPL LNLKEGWKFN LHPKSNYDYI YNQDKIIIRE LLTNVSEIEF
NLESGIYKEI GLFLIDEKIS TNDDLNLSGI RVILDEDSNT NNKEESIHKT MFHIKPRHRS
FDDSTTITTT KIIPQGLHPI LSTELNTTTI VIPTDFDVEE CKFYYYLNLN KSLIFDQFQN
IPIGSQLIIN NGNKNLELPE YKINQWGNEL LFEFEFDNDN DIPHHINLTV HSRYQLPQNN
HSHSQISNVL NSLPNIFIGC NVKEGNLLDK SPFDTKRDVK IGGNYEIYFT EDTVFYHLQN
SDNSGNSGSS TLLEINIPHG KTTFDRVNNI TSLGLLIGVL MILYAISIRV FMSTTSKTKR
D
