SHE10_YEAST
ID SHE10_YEAST Reviewed; 577 AA.
AC P53075; D6VVA6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Outer spore wall assembly protein SHE10 {ECO:0000305|PubMed:23966878};
DE AltName: Full=Sensitivity to high expression protein 10 {ECO:0000303|PubMed:7762298};
DE Flags: Precursor;
GN Name=SHE10 {ECO:0000303|PubMed:7762298};
GN OrderedLocusNames=YGL228W {ECO:0000312|SGD:S000003197};
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 FUNCTION.
RX PubMed=7762298; DOI=10.1002/yea.320110104;
RA Espinet C., de la Torre M.A., Aldea M., Herrero E.;
RT "An efficient method to isolate yeast genes causing overexpression-mediated
RT growth arrest.";
RL Yeast 11:25-32(1995).
RN [4]
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 [5]
RP IDENTIFICATION IN MITOCHONDRIAL RNASE MRP, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20086051; DOI=10.1261/rna.1893710;
RA Lu Q., Wierzbicki S., Krasilnikov A.S., Schmitt M.E.;
RT "Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA
RT components with distinct enzymatic activities and protein components.";
RL RNA 16:529-537(2010).
RN [6]
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 a
CC component of the mitochondrial RNase MRP (MtMRP), a ribonucleoprotein
CC endoribonuclease involved in the cleaving RNA transcripts to generate
CC primers for DNA replication in mitochondria (PubMed:20086051). Causes
CC growth arrest when highly overexpressed (PubMed:7762298).
CC {ECO:0000269|PubMed:20086051, ECO:0000269|PubMed:23966878,
CC ECO:0000269|PubMed:7762298}.
CC -!- SUBUNIT: Component of the mitochondria-localized RNase mitochondrial
CC RNA-processing (RNase MRP) composed of one single RNA encoded by the
CC NME1 gene and at least 31 proteins. Absent in the nucleus-localized
CC RNase MRP (NuMRP). {ECO:0000269|PubMed:20086051}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20086051}.
CC -!- DISRUPTION PHENOTYPE: A combined deletion of the OSW7 and SHE10 has
CC reduced dityrosine incorporation in the outer spore wall.
CC {ECO:0000269|PubMed:23966878}.
CC -!- MISCELLANEOUS: Present with 8640 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OSW/SHE family. {ECO:0000305}.
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DR EMBL; Z72750; CAA96945.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07890.1; -; Genomic_DNA.
DR PIR; S64250; S64250.
DR RefSeq; NP_011286.1; NM_001181094.1.
DR AlphaFoldDB; P53075; -.
DR BioGRID; 33011; 91.
DR IntAct; P53075; 2.
DR STRING; 4932.YGL228W; -.
DR MaxQB; P53075; -.
DR PaxDb; P53075; -.
DR PRIDE; P53075; -.
DR EnsemblFungi; YGL228W_mRNA; YGL228W; YGL228W.
DR GeneID; 852623; -.
DR KEGG; sce:YGL228W; -.
DR SGD; S000003197; SHE10.
DR VEuPathDB; FungiDB:YGL228W; -.
DR eggNOG; ENOG502QT2T; Eukaryota.
DR GeneTree; ENSGT00940000176455; -.
DR HOGENOM; CLU_023952_1_0_1; -.
DR InParanoid; P53075; -.
DR OMA; MINEWSK; -.
DR BioCyc; YEAST:G3O-30702-MON; -.
DR PRO; PR:P53075; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53075; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0030476; P:ascospore wall assembly; IGI:SGD.
PE 1: Evidence at protein level;
KW Coiled coil; Mitochondrion; Reference proteome; Ribonucleoprotein; Signal;
KW Sporulation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..577
FT /note="Outer spore wall assembly protein SHE10"
FT /id="PRO_0000202713"
FT REGION 525..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..416
FT /evidence="ECO:0000255"
FT COILED 513..562
FT /evidence="ECO:0000255"
FT COMPBIAS 525..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 66862 MW; EF4CA95FA3157660 CRC64;
MGKLIKLITT LTVLVSLLQY CCEFNSGSIS CERTQTLCHY TNPRVWNTYF SRNCELYKNK
VSPGFDIVAR KYDTAVKPVI DDATVKVNKV AIQPAFKVIH SQCKKWNCGK YYQLVRSPMV
KTRRFFFAKY NAFVKPNLDK FFTAEFRSHL KERILKYKNI GHYYFTITSR CIKSKYDFIV
GNTEEKLMGK FKNKDTHGIH GSVTREPSSE DMVLTVSTME SDEEELTTTS TQTVVETITL
DQEEASAVAN HAHDDEASTD VEGSTDVNVN EQALLQEDFD MWSETILQKT QDVIQLFEKD
VSKYINGKLV EEANHFKAKF QSLDDKSKKF FSKISLAIND IECVEGIDSE TGKKIFFDKS
GSTEISQYIT RELVREYFNE TRSTLDELTN AMEKDLSEIT DEIEKKVNAI REENVEVFEE
WGDIIVNEWS KRMAYVDVIN AHMGADDDTT LDEEKAKSSV NWKKFLKGKK QIIESRDKLA
HHSADLSRVN AFRQKVQKKI LSFTQESGEF LYILRSKANL QFQERERKER ERKEREKAAA
EEFQRQQELL RQQEEEDEED VSYTSTSTIT TTITMTL
