MYO4_YEAST
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 03-AUG-2022, entry version 193.
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=10; IntAct=EBI-11681, EBI-21600;
CC P32492; P51534: SHE4; NbExp=3; 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 PDBsum; 3MMI; -.
DR PDBsum; 4LL6; -.
DR PDBsum; 4LL8; -.
DR AlphaFoldDB; P32492; -.
DR SMR; P32492; -.
DR BioGRID; 31737; 137.
DR ComplexPortal; CPX-1501; Myosin class V complex, MYO4 variant.
DR DIP; DIP-5761N; -.
DR IntAct; P32492; 35.
DR MINT; P32492; -.
DR STRING; 4932.YAL029C; -.
DR iPTMnet; P32492; -.
DR MaxQB; P32492; -.
DR PaxDb; P32492; -.
DR PRIDE; P32492; -.
DR EnsemblFungi; YAL029C_mRNA; YAL029C; YAL029C.
DR GeneID; 851204; -.
DR KEGG; sce:YAL029C; -.
DR SGD; S000000027; MYO4.
DR VEuPathDB; FungiDB:YAL029C; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000170389; -.
DR HOGENOM; CLU_000192_9_0_1; -.
DR InParanoid; P32492; -.
DR OMA; DESWASK; -.
DR BioCyc; YEAST:G3O-28840-MON; -.
DR Reactome; R-SCE-9013419; RHOT2 GTPase cycle.
DR Reactome; R-SCE-9013425; RHOT1 GTPase cycle.
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; IC:ComplexPortal.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:SGD.
DR GO; GO:0007015; P:actin filament organization; 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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 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.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
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; SSF52540; SSF52540; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
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..1121
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
