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LOH1_YEAST
ID   LOH1_YEAST              Reviewed;         219 AA.
AC   P47055; D6VWE5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Outer spore wall protein 4 {ECO:0000303|PubMed:19779569};
DE   AltName: Full=Loss of heterozygosity protein 1 {ECO:0000303|PubMed:18562670};
DE   Flags: Precursor;
GN   Name=LOH1 {ECO:0000303|PubMed:18562670};
GN   Synonyms=OSW4 {ECO:0000303|PubMed:19779569};
GN   OrderedLocusNames=YJL038C {ECO:0000312|SGD:S000003575}; ORFNames=J1232;
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.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   INDUCTION.
RX   PubMed=9784122; DOI=10.1126/science.282.5389.699;
RA   Chu S., DeRisi J., Eisen M., Mulholland J., Botstein D., Brown P.O.,
RA   Herskowitz I.;
RT   "The transcriptional program of sporulation in budding yeast.";
RL   Science 282:699-705(1998).
RN   [5]
RP   INDUCTION.
RX   PubMed=12612074; DOI=10.1128/mcb.23.6.2009-2016.2003;
RA   McCord R., Pierce M., Xie J., Wonkatal S., Mickel C., Vershon A.K.;
RT   "Rfm1, a novel tethering factor required to recruit the hst1 histone
RT   deacetylase for repression of middle sporulation genes.";
RL   Mol. Cell. Biol. 23:2009-2016(2003).
RN   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [7]
RP   GENE NAME, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18562670; DOI=10.1534/genetics.108.089250;
RA   Andersen M.P., Nelson Z.W., Hetrick E.D., Gottschling D.E.;
RT   "A genetic screen for increased loss of heterozygosity in Saccharomyces
RT   cerevisiae.";
RL   Genetics 179:1179-1195(2008).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX   PubMed=19756047; DOI=10.1038/msb.2009.64;
RA   Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT   "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT   new roles for protein glycosylation in eukaryotes.";
RL   Mol. Syst. Biol. 5:308-308(2009).
RN   [9]
RP   FUNCTION.
RX   PubMed=19779569; DOI=10.1371/journal.pone.0007184;
RA   Suda Y., Rodriguez R.K., Coluccio A.E., Neiman A.M.;
RT   "A screen for spore wall permeability mutants identifies a secreted
RT   protease required for proper spore wall assembly.";
RL   PLoS ONE 4:E7184-E7184(2009).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23966878; DOI=10.1371/journal.pgen.1003700;
RA   Lin C.P., Kim C., Smith S.O., Neiman A.M.;
RT   "A highly redundant gene network controls assembly of the outer spore wall
RT   in S. cerevisiae.";
RL   PLoS Genet. 9:E1003700-E1003700(2013).
CC   -!- FUNCTION: Involved in spore wall assembly (PubMed:23966878). May be
CC       involved in maintaining genome integrity (PubMed:18562670).
CC       {ECO:0000269|PubMed:18562670, ECO:0000269|PubMed:23966878}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: During sporulation. Repressed during vegetative growth by
CC       HST1 and RFM1. {ECO:0000269|PubMed:12612074,
CC       ECO:0000269|PubMed:9784122}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC   -!- DISRUPTION PHENOTYPE: Displays elevated rates of loss of heterozygosity
CC       (LOH) (PubMed:18562670). A combined deletion of the LOH1/OSW4 and
CC       IRC18/OSW6 has reduced dityrosine incorporation in the outer spore wall
CC       (PubMed:23966878). {ECO:0000269|PubMed:18562670,
CC       ECO:0000269|PubMed:23966878}.
CC   -!- SIMILARITY: Belongs to the OSW4/6 family. {ECO:0000305}.
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DR   EMBL; Z49313; CAA89329.1; -; Genomic_DNA.
DR   EMBL; AY558245; AAS56571.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08761.1; -; Genomic_DNA.
DR   PIR; S56810; S56810.
DR   RefSeq; NP_012496.1; NM_001181472.1.
DR   AlphaFoldDB; P47055; -.
DR   BioGRID; 33721; 15.
DR   STRING; 4932.YJL038C; -.
DR   PaxDb; P47055; -.
DR   EnsemblFungi; YJL038C_mRNA; YJL038C; YJL038C.
DR   GeneID; 853413; -.
DR   KEGG; sce:YJL038C; -.
DR   SGD; S000003575; LOH1.
DR   VEuPathDB; FungiDB:YJL038C; -.
DR   GeneTree; ENSGT00940000182578; -.
DR   HOGENOM; CLU_107727_0_0_1; -.
DR   InParanoid; P47055; -.
DR   BioCyc; YEAST:G3O-31504-MON; -.
DR   PRO; PR:P47055; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47055; protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030476; P:ascospore wall assembly; IGI:SGD.
DR   GO; GO:0051276; P:chromosome organization; IMP:SGD.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Sporulation;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..219
FT                   /note="Outer spore wall protein 4"
FT                   /id="PRO_0000203068"
FT   TOPO_DOM        20..170
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:16847258"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   219 AA;  24843 MW;  9E6872658E4CA7AA CRC64;
     MRFQLFIYFY FTIVVIAGTN TIQQFSDAGD RLITSLRNLD NNGTYETLTA EKVPIIEGQI
     QNISAKYEQH TFILKGLEAV LNYKVKSLDN NERESLEIEY EKVEKALDAA LNVSPFEYIK
     KFKEVSRGKV VNALENLSRE QNRITINGGR EDEKEKEARE KKKRLDRIKR ILTVSLLELG
     LAQGVADLCA VAPFACLLGV TVGSIGFIFW LALIYNAIQ
 
 
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