SHE4_YEAST
ID SHE4_YEAST Reviewed; 789 AA.
AC P51534; D6W2A2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=SWI5-dependent HO expression protein 4;
GN Name=SHE4; OrderedLocusNames=YOR035C; ORFNames=OR26.26;
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 200060 / W303;
RX PubMed=8625407; DOI=10.1016/s0092-8674(00)81047-8;
RA Jansen R.P., Dowzer C., Michaelis C., Galova M., Nasmyth K.;
RT "Mother cell-specific HO expression in budding yeast depends on the
RT unconventional myosin myo4p and other cytoplasmic proteins.";
RL Cell 84:687-697(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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).
CC -!- FUNCTION: Required for mother cell-specific ho expression. Might be
CC required for the transport of factors (such as ASH1) that promote HO
CC repression from the mother cell into its bud.
CC -!- INTERACTION:
CC P51534; P19524: MYO2; NbExp=2; IntAct=EBI-17086, EBI-11659;
CC P51534; P32492: MYO4; NbExp=3; IntAct=EBI-17086, EBI-11681;
CC P51534; P51534: SHE4; NbExp=3; IntAct=EBI-17086, EBI-17086;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 3410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X93598; CAA63795.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60752.1; -; Genomic_DNA.
DR EMBL; Z74943; CAA99225.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10818.1; -; Genomic_DNA.
DR PIR; S62172; S62172.
DR RefSeq; NP_014678.1; NM_001183454.1.
DR PDB; 3OPB; X-ray; 2.90 A; A/B=1-789.
DR PDBsum; 3OPB; -.
DR AlphaFoldDB; P51534; -.
DR SMR; P51534; -.
DR BioGRID; 34437; 326.
DR DIP; DIP-4186N; -.
DR IntAct; P51534; 6.
DR MINT; P51534; -.
DR STRING; 4932.YOR035C; -.
DR iPTMnet; P51534; -.
DR MaxQB; P51534; -.
DR PaxDb; P51534; -.
DR PRIDE; P51534; -.
DR EnsemblFungi; YOR035C_mRNA; YOR035C; YOR035C.
DR GeneID; 854200; -.
DR KEGG; sce:YOR035C; -.
DR SGD; S000005561; SHE4.
DR VEuPathDB; FungiDB:YOR035C; -.
DR eggNOG; KOG4151; Eukaryota.
DR HOGENOM; CLU_364165_0_0_1; -.
DR InParanoid; P51534; -.
DR OMA; VLIKTWS; -.
DR BioCyc; YEAST:G3O-33581-MON; -.
DR PRO; PR:P51534; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P51534; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017022; F:myosin binding; IDA:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:SGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:0007533; P:mating type switching; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024660; UCS_central_dom.
DR Pfam; PF11701; UNC45-central; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..789
FT /note="SWI5-dependent HO expression protein 4"
FT /id="PRO_0000097736"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 254
FT /note="L -> LKL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="D -> G (in Ref. 1; CAA63795)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="G -> D (in Ref. 1; CAA63795)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3OPB"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 179..217
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 282..299
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 359..372
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 449..463
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 464..468
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 469..476
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 482..496
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 502..507
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 510..517
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 527..541
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:3OPB"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:3OPB"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 584..599
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 603..614
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 616..624
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 631..645
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 661..672
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 679..695
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 697..703
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 707..719
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 724..738
FT /evidence="ECO:0007829|PDB:3OPB"
FT TURN 744..747
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 751..754
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 757..767
FT /evidence="ECO:0007829|PDB:3OPB"
FT STRAND 768..772
FT /evidence="ECO:0007829|PDB:3OPB"
FT HELIX 779..784
FT /evidence="ECO:0007829|PDB:3OPB"
SQ SEQUENCE 789 AA; 89553 MW; 4A0E1C7D41939B44 CRC64;
MPLCEKGNDP IDSSTIDSLC AAFDKTLKST PDVQKYNDAI NTIFQLRQKS ESGKMPADLT
NSEALKDRQK IEEILTRSYQ DHSESRVHLS KLIQNDIPFA LNLFEILSRS SIHVFVGCFS
NKDATIALLN ELQIRIHYGE DTHVTYLLSI ILQLLNKFKY NFKEVRFLVK ELILRISEDE
VKSMMLIIFA ELQSSFQKDF DKAVVDFMSS LIVEAEIDVG NDPLSIIVKT LSELYPSLTT
LCSEIFLTKG LSKLFKKRVF EEQDLQFTKE LLRLLSSACI DETMRTYITE NYLQLLERSL
NVEDVQIYSA LVLVKTWSFT KLTCINLKQL SEIFINAISR RIMPKIENVN ESAVKLEEVP
KVEMSVEALA YLSLKASVKI MIRSNESFTE ILLTMIKSQK MTHCLYGLLV IMANLSTLPE
ESNGSSQSIN DLKNYADLKG PGADKVGAEK ESKEDILLFN EKYILRTELI SFLKREMHNL
SPNCKQQVVR VIYNITRSKN FIPQCISQGG TTIILEYLAN KQDIGEPIRI LGCRALTRML
IFTNPGLIFK KYSALNAIPF LFELLPRSTP VDDNPLHNDE QIKLTDNYEA LLALTNLASS
ETSDGEEVCK HIVSTKVYWS TIENLMLDEN VPLQRSTLEL ISNMMSHPLT IAAKFFNLEN
PQSLRNFNIL VKLLQLSDVE SQRAVAAIFA NIATTIPLIA KELLTKKELI ENAIQVFADQ
IDDIELRQRL LMLFFGLFEV IPDNGTNEVY PLLQENQKLK DALNMSLKRG DSGPEFSAAI
PVILAKIKV
