YJR1_YEAST
ID YJR1_YEAST Reviewed; 396 AA.
AC P46992; D6VW17;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cell wall protein YJL171C;
DE Flags: Precursor;
GN OrderedLocusNames=YJL171C; ORFNames=J0512;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 366; 371 AND 374.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 28-44 AND 191-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9613572; DOI=10.1007/s004380050706;
RA Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:53-59(1998).
RN [5]
RP GPI-ANCHOR, AND SUBCELLULAR LOCATION.
RX PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT "Amino acid residues in the omega-minus region participate in cellular
RT localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL J. Bacteriol. 181:3886-3889(1999).
RN [6]
RP INDUCTION.
RX PubMed=12644457; DOI=10.1074/jbc.m211604200;
RA Lagorce A., Hauser N.C., Labourdette D., Rodriguez C., Martin-Yken H.,
RA Arroyo J., Hoheisel J.D., Francois J.;
RT "Genome-wide analysis of the response to cell wall mutations in the yeast
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:20345-20357(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18434410; DOI=10.1128/jvi.00412-08;
RA Luallen R.J., Lin J., Fu H., Cai K.K., Agrawal C., Mboudjeka I., Lee F.-H.,
RA Montefiori D., Smith D.F., Doms R.W., Geng Y.;
RT "An engineered Saccharomyces cerevisiae strain binds the broadly
RT neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits
RT mannose-specific gp120-binding antibodies.";
RL J. Virol. 82:6447-6457(2008).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10383953,
CC ECO:0000269|PubMed:18434410, ECO:0000269|PubMed:9613572}; Lipid-anchor,
CC GPI-anchor {ECO:0000305|PubMed:10383953, ECO:0000305|PubMed:18434410,
CC ECO:0000305|PubMed:9613572}; Extracellular side
CC {ECO:0000269|PubMed:10383953, ECO:0000269|PubMed:18434410,
CC ECO:0000269|PubMed:9613572}. Note=GPI-anchored plasma membrane protein
CC (GPI-PMP).
CC -!- INDUCTION: Induced in response to cell wall damage.
CC {ECO:0000269|PubMed:12644457}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000269|PubMed:18434410}.
CC -!- MISCELLANEOUS: Present with 5525 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PGA52 family. {ECO:0000305}.
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DR EMBL; Z49446; CAA89466.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08633.2; -; Genomic_DNA.
DR PIR; S56954; S56954.
DR RefSeq; NP_012364.2; NM_001181604.2.
DR AlphaFoldDB; P46992; -.
DR BioGRID; 33589; 55.
DR IntAct; P46992; 2.
DR STRING; 4932.YJL171C; -.
DR iPTMnet; P46992; -.
DR MaxQB; P46992; -.
DR PaxDb; P46992; -.
DR PRIDE; P46992; -.
DR EnsemblFungi; YJL171C_mRNA; YJL171C; YJL171C.
DR GeneID; 853268; -.
DR KEGG; sce:YJL171C; -.
DR SGD; S000003707; YJL171C.
DR VEuPathDB; FungiDB:YJL171C; -.
DR eggNOG; ENOG502QSTV; Eukaryota.
DR GeneTree; ENSGT00940000176743; -.
DR HOGENOM; CLU_030276_4_0_1; -.
DR InParanoid; P46992; -.
DR OMA; STIHDYQ; -.
DR BioCyc; YEAST:G3O-31608-MON; -.
DR PRO; PR:P46992; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46992; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR InterPro; IPR018805; YJL171C/Tos1_C.
DR InterPro; IPR018807; YJL171C/Tos1_N.
DR Pfam; PF10287; DUF2401; 1.
DR Pfam; PF10290; DUF2403; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..368
FT /note="Cell wall protein YJL171C"
FT /id="PRO_0000042986"
FT PROPEP 369..396
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000406124"
FT LIPID 368
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 366
FT /note="K -> L (in Ref. 1; CAA89466)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="A -> R (in Ref. 1; CAA89466)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="K -> N (in Ref. 1; CAA89466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42958 MW; 979CB4AD751266CC CRC64;
MLQSIVLSVC MFMLHTVAAS GPQSYQKLDF TNVGFTGSYV DVNKFKDITN NESCTCEVGD
RVWFSGKNAP LADYLSVHFR GPLKLKQFAF YTSPGFTVNN SRSSSDWNRL AYYESSSKTA
DNVTFLNHGG EASPCLGNAL SYASSNGTGS ASEATVLADG TLISSDQEYI IYSNVSCPKS
GYDKGCGVYR SGIPAYYGYG GTTKMFLFEF EMPTETEKNS SSIGYYDLPA IWLLNDHIAR
TSQYPTNANC SCWASGCGEY DIFEAMNGTE KNHLYSTFHT FQGIEDLGTG IQSYGYITRN
TTGTMKGGVV FDSSGNVVSF ISDATPFNGT VSADTVNDLL AAIPENETYS SQLMSISATA
PSTTSKSNGV ALTKMQNGVW YYILAIFTAF TQVVLI
