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SPO73_YEAST
ID   SPO73_YEAST             Reviewed;         143 AA.
AC   P40031; D3DLU7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Sporulation-specific protein 73 {ECO:0000305};
GN   Name=SPO73 {ECO:0000303|PubMed:11470404};
GN   OrderedLocusNames=YER046W {ECO:0000312|SGD:S000000848};
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
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   FUNCTION.
RX   PubMed=11470404; DOI=10.1016/s0960-9822(01)00274-3;
RA   Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G., Aigner E.,
RA   Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M., Esposito R.E.,
RA   Klein F., Knop M., Nasmyth K.;
RT   "A screen for genes required for meiosis and spore formation based on
RT   whole-genome expression.";
RL   Curr. Biol. 11:1001-1009(2001).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15590821; DOI=10.1128/ec.3.6.1464-1475.2004;
RA   Coluccio A., Bogengruber E., Conrad M.N., Dresser M.E., Briza P.,
RA   Neiman A.M.;
RT   "Morphogenetic pathway of spore wall assembly in Saccharomyces
RT   cerevisiae.";
RL   Eukaryot. Cell 3:1464-1475(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPO71.
RX   PubMed=26605945; DOI=10.1371/journal.pone.0143571;
RA   Parodi E.M., Roesner J.M., Huang L.S.;
RT   "SPO73 and SPO71 function cooperatively in prospore membrane elongation
RT   during sporulation in Saccharomyces cerevisiae.";
RL   PLoS ONE 10:e0143571-e0143571(2015).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-119; LYS-121 AND
RP   LYS-123.
RX   PubMed=27303688; DOI=10.1128/msphere.00038-15;
RA   Okumura Y., Nakamura T.S., Tanaka T., Inoue I., Suda Y., Takahashi T.,
RA   Nakanishi H., Nakamura S., Gao X.D., Tachikawa H.;
RT   "The dysferlin domain-only protein, Spo73, is required for prospore
RT   membrane extension in Saccharomyces cerevisiae.";
RL   MSphere 1:0-0(2016).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA   He C., Jia C., Zhang Y., Xu P.;
RT   "Enrichment-based proteogenomics identifies microproteins, missing
RT   proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL   J. Proteome Res. 17:2335-2344(2018).
CC   -!- FUNCTION: Required for spore wall assembly and ascus formation
CC       (PubMed:11470404, PubMed:15590821). Involved in the formation and
CC       elongation of prospore membranes (PubMed:26605945, PubMed:27303688).
CC       {ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:15590821,
CC       ECO:0000269|PubMed:26605945, ECO:0000269|PubMed:27303688}.
CC   -!- SUBUNIT: Inteacts with SPO71. {ECO:0000269|PubMed:26605945}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15590821}. Prospore
CC       membrane {ECO:0000269|PubMed:26605945, ECO:0000269|PubMed:27303688};
CC       Peripheral membrane protein {ECO:0000305|PubMed:26605945,
CC       ECO:0000305|PubMed:27303688}. Note=Punctate location throughout the
CC       cytosol in meiosis II cells and peripheral punctate structures in the
CC       spore. {ECO:0000269|PubMed:15590821}.
CC   -!- SIMILARITY: Belongs to the SPO73 family. {ECO:0000305}.
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DR   EMBL; U18796; AAB64581.1; -; Genomic_DNA.
DR   EMBL; AY558454; AAS56780.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07701.1; -; Genomic_DNA.
DR   PIR; S50549; S50549.
DR   RefSeq; NP_010965.1; NM_001178937.1.
DR   AlphaFoldDB; P40031; -.
DR   BioGRID; 36783; 51.
DR   STRING; 4932.YER046W; -.
DR   TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR   PaxDb; P40031; -.
DR   EnsemblFungi; YER046W_mRNA; YER046W; YER046W.
DR   GeneID; 856770; -.
DR   KEGG; sce:YER046W; -.
DR   SGD; S000000848; SPO73.
DR   VEuPathDB; FungiDB:YER046W; -.
DR   eggNOG; ENOG502S49X; Eukaryota.
DR   HOGENOM; CLU_1778715_0_0_1; -.
DR   InParanoid; P40031; -.
DR   OMA; DQGWFYS; -.
DR   BioCyc; YEAST:G3O-30225-MON; -.
DR   ChiTaRS; SPO73; yeast.
DR   PRO; PR:P40031; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40031; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR   GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR   GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR   GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR   InterPro; IPR006614; Peroxin/Ferlin.
DR   SMART; SM00694; DysFC; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Reference proteome; Sporulation.
FT   CHAIN           1..143
FT                   /note="Sporulation-specific protein 73"
FT                   /id="PRO_0000072141"
FT   MUTAGEN         119
FT                   /note="R->A: In Spo73AAA; disrupts localization to the
FT                   prospore membrane; when associated with A-121 and A-123."
FT                   /evidence="ECO:0000269|PubMed:27303688"
FT   MUTAGEN         121
FT                   /note="K->A: In Spo73AAA; disrupts localization to the
FT                   prospore membrane; when associated with A-119 and A-123."
FT                   /evidence="ECO:0000269|PubMed:27303688"
FT   MUTAGEN         123
FT                   /note="K->A: In Spo73AAA; disrupts localization to the
FT                   prospore membrane; when associated with A-119 and A-121."
FT                   /evidence="ECO:0000269|PubMed:27303688"
SQ   SEQUENCE   143 AA;  16598 MW;  A6B408F87F689351 CRC64;
     MGKNHFLKDF SALPEDVLIE NERGITLLGY PLFSPKILLP HVDPPQFQRL NTENGSLIAL
     SKNTISNFIE LYPIDLSTER TAGSSSSQMT KWFVLMDYKE KYDIDDQGWC YSWNFNNSRW
     KSKNGLVRRR VWVRLPTTSH GLD
 
 
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