ID   MYO4_YEAST              Reviewed;        1471 AA.
AC   P32492; D6VPI9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 208.
DE   RecName: Full=Myosin-4;
DE   AltName: Full=SWI5-dependent HO expression protein 1;
GN   Name=MYO4; Synonyms=SHE1; OrderedLocusNames=YAL029C; ORFNames=FUN22;
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.
RX   PubMed=8056830; DOI=10.1242/jcs.107.4.1055;
RA   Haarer B.K., Petzold A., Lillie S.H., Brown S.S.;
RT   "Identification of MYO4, a second class V myosin gene in yeast.";
RL   J. Cell Sci. 107:1055-1064(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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=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   [5]
RP   FUNCTION, AND INTERACTION WITH SHE2 AND SHE3.
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   [6]
RP   FUNCTION, 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   [7]
RP   INTERACTION WITH SHE2 AND SHE3.
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   [8]
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   [9]
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   [10]
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   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15082763; DOI=10.1128/mcb.24.9.3670-3681.2004;
RA   Tadauchi T., Inada T., Matsumoto K., Irie K.;
RT   "Posttranscriptional regulation of HO expression by the Mkt1-Pbp1
RT   complex.";
RL   Mol. Cell. Biol. 24:3670-3681(2004).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1091-1471, FUNCTION, AND
RP   INTERACTION WITH SHE3.
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: Part of the mRNA localization machinery that restricts
CC       accumulation of certain proteins to the bud and in the daughter cell.
CC       Recruited to specific mRNAs including the ASH1 mRNA, coding for a
CC       repressor of the HO endonuclease, via its interaction with SHE3.
CC       {ECO:0000269|PubMed:10212145, ECO:0000269|PubMed:11032818,
CC       ECO:0000269|PubMed:11101531, ECO:0000269|PubMed:12499354,
CC       ECO:0000269|PubMed:15082763, ECO:0000269|PubMed:15328357,
CC       ECO:0000269|PubMed:20439999}.
CC   -!- SUBUNIT: Interacts with SHE2 and SHE3. {ECO:0000269|PubMed:10792032,
CC       ECO:0000269|PubMed:11032818, ECO:0000269|PubMed:11101531,
CC       ECO:0000269|PubMed:20439999}.
CC   -!- INTERACTION:
CC       P32492; P36068: SHE2; NbExp=4; IntAct=EBI-11681, EBI-26866;
CC       P32492; P38272: SHE3; NbExp=11; IntAct=EBI-11681, EBI-21600;
CC       P32492; P51534: SHE4; NbExp=4; IntAct=EBI-11681, EBI-17086;
CC   -!- SUBCELLULAR LOCATION: Bud {ECO:0000269|PubMed:12499354}.
CC       Note=Accumulates preferentially in growing buds.
CC   -!- DISRUPTION PHENOTYPE: Abnormal localization of ASH1 protein to daughter
CC       cell, with protein mislocalized to mother and daughter
CC       (PubMed:15082763). Decreases HO mRNA level (PubMed:15082763).
CC       {ECO:0000269|PubMed:15082763}.
CC   -!- MISCELLANEOUS: Present with 2210 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
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DR   EMBL; M90057; AAC37409.1; -; Unassigned_DNA.
DR   EMBL; U12980; AAC05003.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06959.1; -; Genomic_DNA.
DR   PIR; S30790; S30790.
DR   RefSeq; NP_009373.1; NM_001178174.1.
DR   PDB; 3MMI; X-ray; 2.30 A; A/B=1091-1471.
DR   PDB; 4LL6; X-ray; 2.30 A; A=1098-1471.
DR   PDB; 4LL8; X-ray; 3.58 A; A=918-1471.
DR   AlphaFoldDB; P32492; -.
DR   SMR; P32492; -.
DR   BioGRID; 31737; 140.
DR   ComplexPortal; CPX-1501; Myosin class V complex, MYO4 variant.
DR   DIP; DIP-5761N; -.
DR   FunCoup; P32492; 491.
DR   IntAct; P32492; 35.
DR   MINT; P32492; -.
DR   STRING; 4932.YAL029C; -.
DR   iPTMnet; P32492; -.
DR   PaxDb; 4932-YAL029C; -.
DR   PeptideAtlas; P32492; -.
DR   EnsemblFungi; YAL029C_mRNA; YAL029C; YAL029C.
DR   GeneID; 851204; -.
DR   KEGG; sce:YAL029C; -.
DR   AGR; SGD:S000000027; -.
DR   SGD; S000000027; MYO4.
DR   VEuPathDB; FungiDB:YAL029C; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   HOGENOM; CLU_000192_9_0_1; -.
DR   InParanoid; P32492; -.
DR   OMA; DESWASK; -.
DR   OrthoDB; 6108017at2759; -.
DR   BioCyc; YEAST:G3O-28840-MONOMER; -.
DR   Reactome; R-SCE-190873; Gap junction degradation.
DR   Reactome; R-SCE-9013419; RHOT2 GTPase cycle.
DR   Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR   Reactome; R-SCE-9013425; RHOT1 GTPase cycle.
DR   BioGRID-ORCS; 851204; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P32492; -.
DR   PRO; PR:P32492; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P32492; protein.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005933; C:cellular bud; IDA:SGD.
DR   GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR   GO; GO:0031941; C:filamentous actin; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0031475; C:myosin V complex; NAS:ComplexPortal.
DR   GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0000146; F:microfilament motor activity; IDA:SGD.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
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:0030050; P:vesicle transport along actin filament; NAS:ComplexPortal.
DR   CDD; cd15479; fMyo4p_CBD; 1.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   FunFam; 1.20.58.530:FF:000002; Class V myosin; 1.
DR   FunFam; 1.10.10.820:FF:000001; Myosin heavy chain; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom-like.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004009; SH3_Myosin.
DR   PANTHER; PTHR13140:SF706; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   PDBsum; 3MMI; -.
DR   PDBsum; 4LL6; -.
DR   PDBsum; 4LL8; -.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW   Motor protein; mRNA transport; Myosin; Nucleotide-binding;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..1471
FT                   /note="Myosin-4"
FT                   /id="PRO_0000123491"
FT   DOMAIN          4..57
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          71..777
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          781..801
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          804..824
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          829..849
FT                   /note="IQ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          876..898
FT                   /note="IQ 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          899..928
FT                   /note="IQ 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1164..1419
FT                   /note="Dilute"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT   REGION          647..669
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   COILED          938..1063
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   HELIX           1104..1109
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1111..1116
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1117..1122
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1128..1130
FT                   /evidence="ECO:0007829|PDB:4LL6"
FT   HELIX           1138..1152
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1156..1176
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   TURN            1179..1181
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1182..1193
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1196..1204
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1205..1207
FT                   /evidence="ECO:0007829|PDB:4LL6"
FT   HELIX           1217..1253
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1255..1259
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1262..1264
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   STRAND          1265..1267
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1270..1289
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1294..1319
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1325..1342
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   TURN            1343..1345
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1350..1353
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1354..1364
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1370..1377
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1385..1393
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   STRAND          1398..1401
FT                   /evidence="ECO:0007829|PDB:4LL6"
FT   HELIX           1407..1423
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1440..1442
FT                   /evidence="ECO:0007829|PDB:3MMI"
FT   HELIX           1460..1467
FT                   /evidence="ECO:0007829|PDB:3MMI"
SQ   SEQUENCE   1471 AA;  169344 MW;  E79C0FE72B041E95 CRC64;
     MSFEVGTKCW YPHKEQGWIG GEVTKNDFFE GTFHLELKLE DGETVSIETN SFENDDDHPT
     LPVLRNPPIL ESTDDLTTLS YLNEPAVLHA IKKRYMNGQI YTYSGIVLIA ANPFDKVDHL
     YSREMIQNYS SKRKDELEPH LFAIAEEAYR FMVHEKANQT VVVSGESGAG KTVSAKYIMR
     YFASVQESNN REGEVEMSQI ESQILATNPI MEAFGNAKTT RNDNSSRFGK YLQILFDENT
     TIRGSKIRTY LLEKSRLVYQ PETERNYHIF YQILEGLPEP VKQELHLSSP KDYHYTNQGG
     QPNIAGIDEA REYKITTDAL SLVGINHETQ LGIFKILAGL LHIGNIEMKM TRNDASLSSE
     EQNLQIACEL LGIDPFNFAK WIVKKQIVTR SEKIVTNLNY NQALIARDSV AKFIYSTLFD
     WLVDNINKTL YDPELDQQDH VFSFIGILDI YGFEHFEKNS FEQFCINYAN EKLQQEFNQH
     VFKLEQEEYV KEEIEWSFIE FSDNQPCIDL IENKLGILSL LDEESRLPSG SDESWASKLY
     SAFNKPPSNE VFSKPRFGQT KFIVSHYAVD VEYEVEGFIE KNRDSVSLGH LDVFKATTNP
     IFKQILDNRE LRSDDAPEEQ NTEKKIMIPA RLSQKKPTLG SMFKKSLGEL MAIINSTNVH
     YIRCIKPNSE KKPWEFDNLM VLSQLRACGV LETIRISCAG FPSRWTFDEF VQRYFLLTDY
     SLWSGILYNP DLPKEAIVNF CQSILDATIS DSAKYQIGNT KIFFKAGMLA FLEKLRTNKM
     NEICIIIQKK IRARYYRLQY LQTMESIKKC QSQIRSLLVR TRVDHELKTR AAILLQTNIR
     ALWKREYYRA AIGQIIKLQC TCKRKLILDS VNRKFMLMAA VIIQSYIRSY GHKTDYRTLK
     RSSILVQSAM RMQLARRRYI VLQKEVEERN IRASYGIGLL EEAIEFKNSF ILNLEMLNDS
     YTRLTQLLQG DLSNIPSKQR QEYETIVNGY NDKISKLKTL QVEIMNTLNK KNALKERKKK
     QSSLIQSHMQ SLAAIKGNKP SRLSDEVKSM KQELAFIENV IAQDFTTTYS ANKNDKVKGL
     GIAGQQVKPK LVNVIRRESG NPDLLELLMD LNCYTLEVTE GYLKKVNVTE VNGDNVLGPI
     HVITTVVSSL VRNGLLIQSS KFISKVLLTV ESIVMSLPKD ETMLGGIFWL SNLSRLPAFA
     ANQKTLYEAN GGDEKDKLTL IYLNDLENET LKVFDKIYST WLVKFMKHAS AHIEIFDMVL
     NEKLFKNSGD EKFAKLFTFL NEFDAVLCKF QVVDSMHTKI FNDTLKYLNV MLFNDLITKC
     PALNWKYGYE VDRNIERLVS WFEPRIEDVR PNLIQIIQAV KILQLKISNL NEFKLLFDFW
     YALNPAQIQA ILLKYKPANK GEAGVPNEIL NYLANVIKRE NLSLPGKMEI MLSAQFDSAK
     NHLRYDTSAI TQNSNTEGLA TVSKIIKLDR K
//