SHE3_YEAST
ID SHE3_YEAST Reviewed; 425 AA.
AC P38272; D6VQC7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=SWI5-dependent HO expression protein 3;
GN Name=SHE3; OrderedLocusNames=YBR130C; ORFNames=YBR1005;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091856; DOI=10.1002/yea.320100002;
RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
RA Herbert C.J.;
RT "The sequence of 29.7 kb from the right arm of chromosome II reveals 13
RT complete open reading frames, of which ten correspond to new genes.";
RL Yeast 10:S1-S11(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=9809065; DOI=10.1016/s1097-2765(00)80143-4;
RA Bertrand E., Chartrand P., Schaefer M., Shenoy S.M., Singer R.H.,
RA Long R.M.;
RT "Localization of ASH1 mRNA particles in living yeast.";
RL Mol. Cell 2:437-445(1998).
RN [5]
RP FUNCTION.
RX PubMed=10359695; DOI=10.1016/s0960-9822(99)80260-7;
RA Beach D.L., Salmon E.D., Bloom K.;
RT "Localization and anchoring of mRNA in budding yeast.";
RL Curr. Biol. 9:569-578(1999).
RN [6]
RP FUNCTION.
RX PubMed=10212145; DOI=10.1242/jcs.112.10.1511;
RA Munchow S., Sauter C., Jansen R.P.;
RT "Association of the class V myosin Myo4p with a localised messenger RNA in
RT budding yeast depends on She proteins.";
RL J. Cell Sci. 112:1511-1518(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH SHE2 AND MYO4.
RX PubMed=11032818; DOI=10.1093/emboj/19.20.5514;
RA Bohl F., Kruse C., Frank A., Ferring D., Jansen R.P.;
RT "She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin
RT motor via She3p.";
RL EMBO J. 19:5514-5524(2000).
RN [8]
RP FUNCTION, RNA-BINDING, AND INTERACTION WITH SHE2.
RX PubMed=11101531; DOI=10.1093/emboj/19.23.6592;
RA Long R.M., Gu W., Lorimer E., Singer R.H., Chartrand P.;
RT "She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex
RT to ASH1 mRNA.";
RL EMBO J. 19:6592-6601(2000).
RN [9]
RP RNA-BINDING, AND INTERACTION WITH MYO4.
RX PubMed=10792032; DOI=10.1073/pnas.080585897;
RA Takizawa P.A., Vale R.D.;
RT "The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5273-5278(2000).
RN [10]
RP FUNCTION.
RX PubMed=12499354; DOI=10.1083/jcb.200207101;
RA Kruse C., Jaedicke A., Beaudouin J., Bohl F., Ferring D., Guttler T.,
RA Ellenberg J., Jansen R.P.;
RT "Ribonucleoprotein-dependent localization of the yeast class V myosin
RT Myo4p.";
RL J. Cell Biol. 159:971-982(2002).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14691136; DOI=10.1083/jcb.200304030;
RA Estrada P., Kim J., Coleman J., Walker L., Dunn B., Takizawa P., Novick P.,
RA Ferro-Novick S.;
RT "Myo4p and She3p are required for cortical ER inheritance in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 163:1255-1266(2003).
RN [12]
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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SHE2.
RX PubMed=14561888; DOI=10.1261/rna.5120803;
RA Gonsalvez G.B., Lehmann K.A., Ho D.K., Stanitsa E.S., Williamson J.R.,
RA Long R.M.;
RT "RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA
RT ribonucleoprotein complex.";
RL RNA 9:1383-1399(2003).
RN [14]
RP FUNCTION.
RX PubMed=15328357; DOI=10.1074/jbc.m406086200;
RA Gonsalvez G.B., Little J.L., Long R.M.;
RT "ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p
RT transport complex.";
RL J. Biol. Chem. 279:46286-46294(2004).
RN [15]
RP FUNCTION.
RX PubMed=16890529; DOI=10.1016/j.cub.2006.06.025;
RA Schmid M., Jaedicke A., Du T.G., Jansen R.P.;
RT "Coordination of endoplasmic reticulum and mRNA localization to the yeast
RT bud.";
RL Curr. Biol. 16:1538-1543(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [19]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-343; SER-348 AND SER-361.
RX PubMed=19429778; DOI=10.1128/ec.00084-09;
RA Landers S.M., Gallas M.R., Little J., Long R.M.;
RT "She3p possesses a novel activity required for ASH1 mRNA localization in
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 8:1072-1083(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [21]
RP INTERACTION WITH MYO4.
RX PubMed=20439999; DOI=10.1083/jcb.201002076;
RA Heuck A., Fetka I., Brewer D.N., Huls D., Munson M., Jansen R.P.,
RA Niessing D.;
RT "The structure of the Myo4p globular tail and its function in ASH1 mRNA
RT localization.";
RL J. Cell Biol. 189:497-510(2010).
CC -!- FUNCTION: RNA-binding protein that binds specific mRNAs including the
CC ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the
CC mRNA localization machinery that restricts accumulation of certain
CC proteins to the bud and in the daughter cell. Required for the delivery
CC of cortical endoplasmic reticulum into the emerging bud.
CC {ECO:0000269|PubMed:10212145, ECO:0000269|PubMed:10359695,
CC ECO:0000269|PubMed:11032818, ECO:0000269|PubMed:11101531,
CC ECO:0000269|PubMed:12499354, ECO:0000269|PubMed:14561888,
CC ECO:0000269|PubMed:14691136, ECO:0000269|PubMed:15328357,
CC ECO:0000269|PubMed:16890529, ECO:0000269|PubMed:19429778,
CC ECO:0000269|PubMed:9809065}.
CC -!- SUBUNIT: Interacts with SHE2 and MYO4. {ECO:0000269|PubMed:10792032,
CC ECO:0000269|PubMed:11032818, ECO:0000269|PubMed:11101531,
CC ECO:0000269|PubMed:14561888, ECO:0000269|PubMed:20439999}.
CC -!- INTERACTION:
CC P38272; P32492: MYO4; NbExp=10; IntAct=EBI-21600, EBI-11681;
CC P38272; P36068: SHE2; NbExp=11; IntAct=EBI-21600, EBI-26866;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14561888, ECO:0000269|PubMed:14691136}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14561888,
CC ECO:0000269|PubMed:14691136}.
CC -!- MISCELLANEOUS: Present with 1010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHE3 family. {ECO:0000305}.
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DR EMBL; X75891; CAA53489.1; -; Genomic_DNA.
DR EMBL; Z35999; CAA85087.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07247.1; -; Genomic_DNA.
DR PIR; S45999; S45999.
DR RefSeq; NP_009688.3; NM_001178478.3.
DR PDB; 4LL7; X-ray; 2.31 A; A/B/C/D/E/F/G/H=42-137.
DR PDB; 4LL8; X-ray; 3.58 A; B/E=81-311.
DR PDB; 4WNL; X-ray; 2.80 A; E/F/G/H=342-374.
DR PDB; 5M0I; X-ray; 2.41 A; H/I/J=382-405.
DR PDB; 5M0J; X-ray; 2.80 A; A/B/C/D/G/H/I/J=331-405.
DR PDBsum; 4LL7; -.
DR PDBsum; 4LL8; -.
DR PDBsum; 4WNL; -.
DR PDBsum; 5M0I; -.
DR PDBsum; 5M0J; -.
DR AlphaFoldDB; P38272; -.
DR SMR; P38272; -.
DR BioGRID; 32831; 106.
DR DIP; DIP-2037N; -.
DR IntAct; P38272; 27.
DR MINT; P38272; -.
DR STRING; 4932.YBR130C; -.
DR iPTMnet; P38272; -.
DR MaxQB; P38272; -.
DR PaxDb; P38272; -.
DR PRIDE; P38272; -.
DR EnsemblFungi; YBR130C_mRNA; YBR130C; YBR130C.
DR GeneID; 852427; -.
DR KEGG; sce:YBR130C; -.
DR SGD; S000000334; SHE3.
DR VEuPathDB; FungiDB:YBR130C; -.
DR eggNOG; ENOG502QSQX; Eukaryota.
DR HOGENOM; CLU_038734_0_0_1; -.
DR InParanoid; P38272; -.
DR OMA; HFMANIN; -.
DR BioCyc; YEAST:G3O-29085-MON; -.
DR PRO; PR:P38272; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38272; protein.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:SGD.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IMP:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:0007533; P:mating type switching; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR InterPro; IPR031398; She3.
DR Pfam; PF17078; SHE3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endoplasmic reticulum; Membrane; mRNA transport;
KW Phosphoprotein; Reference proteome; RNA-binding; Transport.
FT CHAIN 1..425
FT /note="SWI5-dependent HO expression protein 3"
FT /id="PRO_0000202490"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..197
FT /evidence="ECO:0000255"
FT COMPBIAS 323..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 343
FT /note="S->E: Prevents correct localization of ASH1 mRNA;
FT when associated with E-361."
FT /evidence="ECO:0000269|PubMed:19429778"
FT MUTAGEN 348
FT /note="S->E: Prevents correct localization of ASH1 mRNA."
FT /evidence="ECO:0000269|PubMed:19429778"
FT MUTAGEN 361
FT /note="S->E: Prevents correct localization of ASH1 mRNA;
FT when associated with E-343."
FT /evidence="ECO:0000269|PubMed:19429778"
FT HELIX 44..71
FT /evidence="ECO:0007829|PDB:4LL7"
FT HELIX 74..134
FT /evidence="ECO:0007829|PDB:4LL7"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:5M0J"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:5M0J"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5M0J"
SQ SEQUENCE 425 AA; 47417 MW; 590404D2E140BB7A CRC64;
MSDQDNTQTS SSKLAPHHNI FMANLESSPT KDRNTSSQNA SSSRVIESLH DQIDMLTKTN
LQLTTQSQNL LSKLELAQSK ESKLLENLNL LKNENENLNS IFERKNKKLK ELEKDYSELS
NRYNEQKEKM DQLSKLAKNS SAIEQSCSEK LQNMEVNYNS LLESQNLYRD HYSDEISKLN
EKIGLLELEL SNQNLNYGSD TSSNSDIELN LNKFNDSVKD LKSLETEKDS KLSKIITHSL
DELNLQSWLN LYQTNENLIS TFAEKMDLKD VLKRNDEKIS NKGAVVQTLK KNVQTQVESN
NADALSSNNA QDMLPIKMVK LRKTPNTNDS SSNGNSSNNK RRSFYTASPL LSSGSIPKSA
SPVLPGVKRT ASVRKPSSSS SKTNVTHNND PSTSPTISVP PGVTRTVSST HKKKGNSMVV
HGAQS
