SHE2_YEAST
ID SHE2_YEAST Reviewed; 246 AA.
AC P36068; D6VX65;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=SWI5-dependent HO expression protein 2;
GN Name=SHE2; OrderedLocusNames=YKL130C;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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=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, RNA-BINDING, AND INTERACTION WITH SHE3 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 SHE3.
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, AND SUBCELLULAR LOCATION.
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.
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.
RX PubMed=13679573; DOI=10.1073/pnas.2033246100;
RA Shepard K.A., Gerber A.P., Jambhekar A., Takizawa P.A., Brown P.O.,
RA Herschlag D., DeRisi J.L., Vale R.D.;
RT "Widespread cytoplasmic mRNA transport in yeast: identification of 22 bud-
RT localized transcripts using DNA microarray analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11429-11434(2003).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH SHE3, AND
RP MUTAGENESIS OF ASN-36; ARG-43; ARG-44; ARG-49; ARG-52 AND ARG-63.
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 [15]
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 [16]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=15899876; DOI=10.1128/mcb.25.11.4752-4766.2005;
RA Olivier C., Poirier G., Gendron P., Boisgontier A., Major F., Chartrand P.;
RT "Identification of a conserved RNA motif essential for She2p recognition
RT and mRNA localization to the yeast bud.";
RL Mol. Cell. Biol. 25:4752-4766(2005).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18566598; DOI=10.1038/embor.2008.112;
RA Du T.G., Jellbauer S., Muller M., Schmid M., Niessing D., Jansen R.P.;
RT "Nuclear transit of the RNA-binding protein She2 is required for
RT translational control of localized ASH1 mRNA.";
RL EMBO Rep. 9:781-787(2008).
RN [19]
RP FUNCTION, INTERACTION WITH LOC1; PUF6 AND SRP1, NUCLEUS LOCALIZATION
RP SIGNAL, AND SUBCELLULAR LOCATION.
RX PubMed=19244342; DOI=10.1091/mbc.e08-11-1151;
RA Shen Z., Paquin N., Forget A., Chartrand P.;
RT "Nuclear shuttling of She2p couples ASH1 mRNA localization to its
RT translational repression by recruiting Loc1p and Puf6p.";
RL Mol. Biol. Cell 20:2265-2275(2009).
RN [20]
RP SUBUNIT, AND MUTAGENESIS OF LEU-130.
RX PubMed=19710186; DOI=10.1261/rna.1753309;
RA Muller M., Richter K., Heuck A., Kremmer E., Buchner J., Jansen R.P.,
RA Niessing D.;
RT "Formation of She2p tetramers is required for mRNA binding, mRNP assembly,
RT and localization.";
RL RNA 15:2002-2012(2009).
RN [21]
RP FUNCTION, AND INTERACTION WITH RPO21; SPT4 AND SPT5.
RX PubMed=20713510; DOI=10.1101/gad.1937510;
RA Shen Z., St-Denis A., Chartrand P.;
RT "Cotranscriptional recruitment of She2p by RNA pol II elongation factor
RT Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud.";
RL Genes Dev. 24:1914-1926(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 6-239, SUBUNIT, FUNCTION,
RP RNA-BINDING, AND MUTAGENESIS OF CYS-68 AND SER-120.
RX PubMed=15537539; DOI=10.1016/j.cell.2004.10.018;
RA Niessing D., Huttelmaier S., Zenklusen D., Singer R.H., Burley S.K.;
RT "She2p is a novel RNA binding protein with a basic helical hairpin motif.";
RL Cell 119:491-502(2004).
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. Recruits the MYO4-SHE3
CC complex to the ASH1 mRNA. Recruits also LOC1 and PUF6 to ASH1 mRNA,
CC which are required for translational repression of this mRNA.
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:13679573,
CC ECO:0000269|PubMed:14561888, ECO:0000269|PubMed:14691136,
CC ECO:0000269|PubMed:15328357, ECO:0000269|PubMed:15537539,
CC ECO:0000269|PubMed:15899876, ECO:0000269|PubMed:16890529,
CC ECO:0000269|PubMed:18566598, ECO:0000269|PubMed:19244342,
CC ECO:0000269|PubMed:20713510, ECO:0000269|PubMed:9809065}.
CC -!- SUBUNIT: Homodimer and homotetramer. Interacts with LOC1, MYO4, PUF6,
CC SHE3 and with RNA pol II subunits RPO21, SPT4 and SPT5.
CC {ECO:0000269|PubMed:10792032, ECO:0000269|PubMed:11032818,
CC ECO:0000269|PubMed:11101531, ECO:0000269|PubMed:14561888,
CC ECO:0000269|PubMed:15537539, ECO:0000269|PubMed:19244342,
CC ECO:0000269|PubMed:19710186, ECO:0000269|PubMed:20713510}.
CC -!- INTERACTION:
CC P36068; P32492: MYO4; NbExp=4; IntAct=EBI-26866, EBI-11681;
CC P36068; Q04373: PUF6; NbExp=2; IntAct=EBI-26866, EBI-33208;
CC P36068; P38272: SHE3; NbExp=11; IntAct=EBI-26866, EBI-21600;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12499354,
CC ECO:0000269|PubMed:14561888, ECO:0000269|PubMed:18566598}. Nucleus
CC {ECO:0000269|PubMed:12499354, ECO:0000269|PubMed:14561888,
CC ECO:0000269|PubMed:18566598, ECO:0000269|PubMed:19244342}.
CC Note=Shuttles between the nucleus and cytoplasm and is exported in an
CC mRNA-dependent manner (PubMed:12499354, PubMed:14561888)
CC (PubMed:18566598). The presence in the nucleus is essential for PUF6
CC and LOC1 to bind the ASH1 mRNA. {ECO:0000269|PubMed:12499354,
CC ECO:0000269|PubMed:14561888, ECO:0000269|PubMed:19244342}.
CC -!- MISCELLANEOUS: Present with 4070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHE2 family. {ECO:0000305}.
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DR EMBL; Z28130; CAA81971.1; -; Genomic_DNA.
DR EMBL; AY557902; AAS56228.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09031.1; -; Genomic_DNA.
DR PIR; S37959; S37959.
DR RefSeq; NP_012792.1; NM_001179696.1.
DR PDB; 1XLY; X-ray; 1.95 A; A/B=6-239.
DR PDB; 4WNL; X-ray; 2.80 A; A/B/C/D=6-239.
DR PDB; 5M0I; X-ray; 2.41 A; A/B/C/D=6-246.
DR PDB; 5M0J; X-ray; 2.80 A; A/B/C/D/G/H/I/J=6-246.
DR PDBsum; 1XLY; -.
DR PDBsum; 4WNL; -.
DR PDBsum; 5M0I; -.
DR PDBsum; 5M0J; -.
DR AlphaFoldDB; P36068; -.
DR SMR; P36068; -.
DR BioGRID; 34005; 113.
DR DIP; DIP-1206N; -.
DR IntAct; P36068; 26.
DR MINT; P36068; -.
DR STRING; 4932.YKL130C; -.
DR iPTMnet; P36068; -.
DR MaxQB; P36068; -.
DR PaxDb; P36068; -.
DR PRIDE; P36068; -.
DR EnsemblFungi; YKL130C_mRNA; YKL130C; YKL130C.
DR GeneID; 853728; -.
DR KEGG; sce:YKL130C; -.
DR SGD; S000001613; SHE2.
DR VEuPathDB; FungiDB:YKL130C; -.
DR eggNOG; ENOG502RXWH; Eukaryota.
DR HOGENOM; CLU_1129832_0_0_1; -.
DR InParanoid; P36068; -.
DR OMA; HFVKFTQ; -.
DR BioCyc; YEAST:G3O-31911-MON; -.
DR EvolutionaryTrace; P36068; -.
DR PRO; PR:P36068; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36068; protein.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; IDA:SGD.
DR GO; GO:0007533; P:mating type switching; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.200.20; -; 1.
DR InterPro; IPR024261; RNA-bd_She2.
DR InterPro; IPR036827; She2_dom_sf.
DR Pfam; PF11435; She2p; 1.
DR SUPFAM; SSF116942; SSF116942; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA transport; Nucleus; Reference proteome;
KW RNA-binding; Transport.
FT CHAIN 1..246
FT /note="SWI5-dependent HO expression protein 2"
FT /id="PRO_0000203151"
FT MOTIF 15..23
FT /note="Nuclear localization signal"
FT MUTAGEN 36
FT /note="N->S: Prevents association with ASH1 and IST2 mRNAs
FT and leads to their mislocalization."
FT /evidence="ECO:0000269|PubMed:14561888"
FT MUTAGEN 43
FT /note="R->A: Prevents association with ASH1 and mRNA and
FT leads to its mislocalization."
FT /evidence="ECO:0000269|PubMed:14561888"
FT MUTAGEN 44
FT /note="R->A: Prevents association with ASH1 and mRNA and
FT leads to its mislocalization."
FT /evidence="ECO:0000269|PubMed:14561888"
FT MUTAGEN 49
FT /note="R->K: Prevents association with ASH1 and mRNA and
FT leads to its mislocalization."
FT /evidence="ECO:0000269|PubMed:14561888"
FT MUTAGEN 52
FT /note="R->A,K: Prevents association with ASH1 and mRNA and
FT leads to its mislocalization."
FT /evidence="ECO:0000269|PubMed:14561888"
FT MUTAGEN 63
FT /note="R->A,K: Prevents association with ASH1 and IST2
FT mRNAs and leads to their mislocalization."
FT /evidence="ECO:0000269|PubMed:14561888"
FT MUTAGEN 68
FT /note="C->Y: Prevents dimerization and RNA-binding."
FT /evidence="ECO:0000269|PubMed:15537539"
FT MUTAGEN 120
FT /note="S->Y: Prevents dimerization and RNA-binding."
FT /evidence="ECO:0000269|PubMed:15537539"
FT MUTAGEN 130
FT /note="L->Y: Prevents tetramerization."
FT /evidence="ECO:0000269|PubMed:19710186"
FT HELIX 13..42
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 49..71
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1XLY"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5M0I"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 92..118
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 138..161
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1XLY"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:1XLY"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5M0J"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5M0I"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4WNL"
FT HELIX 205..235
FT /evidence="ECO:0007829|PDB:1XLY"
SQ SEQUENCE 246 AA; 28251 MW; 5514B374655EFDBB CRC64;
MSKDKDIKVT PGTCELVEQI LALLSRYLSS YIHVLNKFIS HLRRVATLRF ERTTLIKFVK
KLRFYNDCVL SYNASEFINE GKNELDPEAD SFDKVILPIA SMFVKCVETF DLLNYYLTQS
LQKEILSKTL NEDLTLTAES ILAIDDTYNH FVKFSQWMIE SLRIGSNLLD LEVVQFAIKC
ADEDGTNIGE TDNIFLQEIL PVNSEEEFQT LSAAWHSILD GKLSALDEEF DVVATKWHDK
FGKLKN
