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Database: UniProt
Entry: MYO4_ARATH
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Original site: MYO4_ARATH 
ID   MYO4_ARATH              Reviewed;        1134 AA.
AC   F4JIU4; O81840; Q9M0J7;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Myosin-4;
DE   AltName: Full=MYOSIN VIII B;
DE            Short=AtVIIIB;
GN   Name=VIII-B; Synonyms=VIIIB; OrderedLocusNames=At4g27370;
GN   ORFNames=M4I22.180;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=10984423; DOI=10.1242/jcs.113.19.3353;
RA   Hodge T., Cope M.J.;
RT   "A myosin family tree.";
RL   J. Cell Sci. 113:3353-3354(2000).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=11516337; DOI=10.1186/gb-2001-2-7-research0024;
RA   Reddy A.S., Day I.S.;
RT   "Analysis of the myosins encoded in the recently completed Arabidopsis
RT   thaliana genome sequence.";
RL   Genome Biol. 2:RESEARCH0024.1-RESEARCH0024.17(2001).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=21233331; DOI=10.1104/pp.110.170720;
RA   Peremyslov V.V., Mockler T.C., Filichkin S.A., Fox S.E., Jaiswal P.,
RA   Makarova K.S., Koonin E.V., Dolja V.V.;
RT   "Expression, splicing, and evolution of the myosin gene family in plants.";
RL   Plant Physiol. 155:1191-1204(2011).
CC   -!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
CC       regulated transport of various organelles and proteins for their
CC       segregation. Functions by binding with its tail domain to receptor
CC       proteins on organelles and exerting force with its N-terminal motor
CC       domain against actin filaments, thereby transporting its cargo along
CC       polarized actin cables (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- DOMAIN: IQ domain mediates interaction with calmodulin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. Plant myosin class VIII subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA19731.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81387.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL030978; CAA19731.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161571; CAB81387.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85329.1; -; Genomic_DNA.
DR   PIR; A85318; A85318.
DR   PIR; T05761; T05761.
DR   RefSeq; NP_194467.5; NM_118871.6.
DR   AlphaFoldDB; F4JIU4; -.
DR   SMR; F4JIU4; -.
DR   STRING; 3702.F4JIU4; -.
DR   PaxDb; 3702-AT4G27370-1; -.
DR   EnsemblPlants; AT4G27370.1; AT4G27370.1; AT4G27370.
DR   GeneID; 828845; -.
DR   Gramene; AT4G27370.1; AT4G27370.1; AT4G27370.
DR   KEGG; ath:AT4G27370; -.
DR   Araport; AT4G27370; -.
DR   TAIR; AT4G27370; VIIIB.
DR   eggNOG; KOG0160; Eukaryota.
DR   HOGENOM; CLU_000192_7_2_1; -.
DR   InParanoid; F4JIU4; -.
DR   PRO; PR:F4JIU4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JIU4; baseline and differential.
DR   Genevisible; F4JIU4; AT.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; ISS:TAIR.
DR   GO; GO:0030048; P:actin filament-based movement; TAS:TAIR.
DR   CDD; cd01383; MYSc_Myo8; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 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; 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; IPR036022; MYSc_Myo8.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF763; MYOSIN-4; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Motor protein;
KW   Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..1134
FT                   /note="Myosin-4"
FT                   /id="PRO_0000422860"
FT   DOMAIN          110..160
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          164..830
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          832..861
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          855..884
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          891..920
FT                   /note="IQ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          589..623
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          710..732
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          913..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          953..999
FT                   /evidence="ECO:0000255"
FT   BINDING         255..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         304..312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1134 AA;  129832 MW;  86CFF7F87F88389A CRC64;
     MMKSSVKEIL ESLRLLDSSE RSSSLPSPST FRAPMPLIRQ SLPAKFRNAI SLESKTIEKE
     DKDWSTEQIT QSAEKEKTGN EVVKISTAQM SRAKNSHDPE WINSAEYFVR EKLCVWCRVA
     ANGQWHLGKI HSTSSSDDVC VMLSANDDVR TMEEIFPANP EILEGVEDLT QLSYLNEPSL
     LYNLRVRYSQ DLIYSKAGPV LIAVNPFKNV QIYGEEFLSA YQKNALDAPH VYAVADAAYD
     DMMREEKNQS IIISGESGAG KTETAKYAMQ YLEALGGGSF GVENEILKTN CILEAFGNAK
     TSRNDNSSRF GKLMEIHFSA KGKICGAKLE TFSLDQSRVA QLCNGERCYH IFYQLCAGAS
     PILKERLKIK AASEYNYLNQ SNCLTIDRTD DAQKFHKLME AFNIVQIPQE YQERTFALLA
     AVLWLGNVSF EVIDNENHVE VVADEAVTNV AMLMGCNSKK LMVVLSTCKL QAGRDCIAKR
     LTLRQATDMR DSLAKIIYAS LFNWLVEQIN ISLEVGNSRT GRSISILDIY GFESFKDNSF
     EQFCINYANE RLQQHFNRHL FKLEQEEYEG DGIDWTKVEF IDNQECLNLI EKKPIGLVSL
     LNEESNFPKA TDTTFANKLK QHLNANSCFK GERGRGFRIK HYAGEVLYNT NGFLEKNRDP
     LHVDLIQLLS LCKCQLLNLF STKMHHDFLK PATFSDSMNQ SVIAKFKGQL FKLMNKLEDT
     TPHFIRCIKP NSNQLPGLYE ENHVLQQLRC CGVLEIVRIS RSGYPTRLTH QELAVRYGCL
     LLDTRISQDP LSTSKAILKQ CNLPPEMYQV GYTKIYLRTG VISVLEERKK YVLRGILGLQ
     KQFRGYQTRE YFHNMRNAAV ILQSYIRGEN ARRNYIVVGE SAIVSTAITK ELDAAIHLQY
     MVRKWLARKL LNSTQQKNKP RNEKKKTRRK STKRVSEDKE LLSEQFEVQP CVLADLQSRV
     LKVEAAIMQK EDENTALQEE LQRFEERWLE NETRMKSMED TWQKHMSSMQ MSLAAACKVL
     APDKTASHGT DSEDTMSFGT PTKELKGSLS DVNNLSTEFD QRSVIIHEDP KSLVEVKSDS
     ISNRKQHAEE LRRLKSRFEK WKKDYKTRLR ETKARVRLNG DEGRHRNWWC KKSY
//
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