MYO5_ARATH
ID MYO5_ARATH Reviewed; 1520 AA.
AC Q39160; Q9LNP7;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Myosin-5;
DE AltName: Full=AtMYA1;
GN Name=XI-1; Synonyms=MYA1; OrderedLocusNames=At1g17580; ORFNames=F1L3.28;
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 [MRNA].
RC TISSUE=Etiolated seedling;
RX PubMed=8006972; DOI=10.1006/jmbi.1994.1400;
RA Kinkema M., Schiefelbein J.;
RT "A myosin from a higher plant has structural similarities to class V
RT myosins.";
RL J. Mol. Biol. 239:591-597(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17288617; DOI=10.1186/1471-2229-7-6;
RA Reisen D., Hanson M.R.;
RT "Association of six YFP-myosin XI-tail fusions with mobile plant cell
RT organelles.";
RL BMC Plant Biol. 7:6-6(2007).
RN [7]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=17500056; DOI=10.1074/jbc.m700645200;
RA Li J.F., Nebenfuehr A.;
RT "Organelle targeting of myosin XI is mediated by two globular tail
RT subdomains with separate cargo binding sites.";
RL J. Biol. Chem. 282:20593-20602(2007).
RN [8]
RP FUNCTION.
RX PubMed=17504816; DOI=10.1093/pcp/pcm054;
RA Hachikubo Y., Ito K., Schiefelbein J., Manstein D.J., Yamamoto K.;
RT "Enzymatic activity and motility of recombinant Arabidopsis myosin XI,
RT MYA1.";
RL Plant Cell Physiol. 48:886-891(2007).
RN [9]
RP DIMERIZATION, AND COILED COIL.
RX PubMed=18429938; DOI=10.1111/j.1365-313x.2008.03522.x;
RA Li J.F., Nebenfuehr A.;
RT "Inter-dependence of dimerization and organelle binding in myosin XI.";
RL Plant J. 55:478-490(2008).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=18178669; DOI=10.1104/pp.107.113654;
RA Peremyslov V.V., Prokhnevsky A.I., Avisar D., Dolja V.V.;
RT "Two class XI myosins function in organelle trafficking and root hair
RT development in Arabidopsis.";
RL Plant Physiol. 146:1109-1116(2008).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19060218; DOI=10.1073/pnas.0810730105;
RA Prokhnevsky A.I., Peremyslov V.V., Dolja V.V.;
RT "Overlapping functions of the four class XI myosins in Arabidopsis growth,
RT root hair elongation, and organelle motility.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19744-19749(2008).
RN [12]
RP FUNCTION.
RX PubMed=19369591; DOI=10.1104/pp.109.136853;
RA Avisar D., Abu-Abied M., Belausov E., Sadot E., Hawes C., Sparkes I.A.;
RT "A comparative study of the involvement of 17 Arabidopsis myosin family
RT members on the motility of Golgi and other organelles.";
RL Plant Physiol. 150:700-709(2009).
RN [13]
RP FUNCTION.
RX PubMed=20581304; DOI=10.1105/tpc.110.076315;
RA Peremyslov V.V., Prokhnevsky A.I., Dolja V.V.;
RT "Class XI myosins are required for development, cell expansion, and F-Actin
RT organization in Arabidopsis.";
RL Plant Cell 22:1883-1897(2010).
RN [14]
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).
RN [15]
RP FUNCTION.
RX PubMed=22672737; DOI=10.1186/1471-2229-12-81;
RA Ojangu E.L., Tanner K., Pata P., Jaerve K., Holweg C.L., Truve E.,
RA Paves H.;
RT "Myosins XI-K, XI-1, and XI-2 are required for development of pavement
RT cells, trichomes, and stigmatic papillae in Arabidopsis.";
RL BMC Plant Biol. 12:81-81(2012).
RN [16]
RP FUNCTION.
RX PubMed=21914656; DOI=10.1093/jxb/err265;
RA Avisar D., Abu-Abied M., Belausov E., Sadot E.;
RT "Myosin XIK is a major player in cytoplasm dynamics and is regulated by two
RT amino acids in its tail.";
RL J. Exp. Bot. 63:241-249(2012).
RN [17]
RP INTERACTION WITH MYOB1 AND MYOB2.
RX PubMed=23995081; DOI=10.1105/tpc.113.113704;
RA Peremyslov V.V., Morgun E.A., Kurth E.G., Makarova K.S., Koonin E.V.,
RA Dolja V.V.;
RT "Identification of myosin XI receptors in Arabidopsis defines a distinct
RT class of transport vesicles.";
RL Plant Cell 25:3022-3038(2013).
RN [18]
RP INTERACTION WITH PHOX1.
RX PubMed=28096376; DOI=10.1073/pnas.1620577114;
RA Kurth E.G., Peremyslov V.V., Turner H.L., Makarova K.S., Iranzo J.,
RA Mekhedov S.L., Koonin E.V., Dolja V.V.;
RT "Myosin-driven transport network in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1385-E1394(2017).
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. Contributes to the trafficking of Golgi stacks,
CC mitochondria and peroxisomes. Required for development of pavement
CC cells, trichomes, and stigmatic papillae. {ECO:0000269|PubMed:17504816,
CC ECO:0000269|PubMed:19060218, ECO:0000269|PubMed:19369591,
CC ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656,
CC ECO:0000269|PubMed:22672737}.
CC -!- SUBUNIT: Homodimer (PubMed:18429938). Interacts with MYOB1 and MYOB2
CC (PubMed:23995081). Interacts with PHOX1 (PubMed:28096376).
CC {ECO:0000269|PubMed:18429938, ECO:0000269|PubMed:23995081,
CC ECO:0000269|PubMed:28096376}.
CC -!- INTERACTION:
CC Q39160; Q39160: XI-1; NbExp=4; IntAct=EBI-2010084, EBI-2010084;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617,
CC ECO:0000269|PubMed:17500056}. Note=Colocalizes with peroxisome,
CC cytoplasmic vesicles and/or organelles.
CC -!- DOMAIN: IQ domain mediates interaction with calmodulin. {ECO:0000250}.
CC -!- DOMAIN: The tail domain is a globular cargo-binding domain.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:18178669, ECO:0000269|PubMed:19060218}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79470.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z28389; CAA82234.1; -; mRNA.
DR EMBL; AC022492; AAF79470.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29607.1; -; Genomic_DNA.
DR PIR; S46444; S46444.
DR RefSeq; NP_173201.2; NM_101620.3.
DR AlphaFoldDB; Q39160; -.
DR SMR; Q39160; -.
DR BioGRID; 23573; 1.
DR STRING; 3702.AT1G17580.1; -.
DR iPTMnet; Q39160; -.
DR PaxDb; Q39160; -.
DR PRIDE; Q39160; -.
DR ProteomicsDB; 251357; -.
DR EnsemblPlants; AT1G17580.1; AT1G17580.1; AT1G17580.
DR GeneID; 838333; -.
DR Gramene; AT1G17580.1; AT1G17580.1; AT1G17580.
DR KEGG; ath:AT1G17580; -.
DR Araport; AT1G17580; -.
DR TAIR; locus:2007938; AT1G17580.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; Q39160; -.
DR OMA; LLMCNAQ; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q39160; -.
DR PRO; PR:Q39160; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39160; baseline and differential.
DR Genevisible; Q39160; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; TAS:TAIR.
DR GO; GO:0051301; P:cell division; IGI:TAIR.
DR GO; GO:0010154; P:fruit development; IGI:TAIR.
DR GO; GO:0051645; P:Golgi localization; IMP:TAIR.
DR GO; GO:0048467; P:gynoecium development; IGI:TAIR.
DR GO; GO:0090436; P:leaf pavement cell development; IGI:TAIR.
DR GO; GO:0051646; P:mitochondrion localization; IGI:TAIR.
DR GO; GO:0060151; P:peroxisome localization; IGI:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IGI:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IGI:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 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; IPR037975; MyosinXI_CBD.
DR InterPro; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1520
FT /note="Myosin-5"
FT /id="PRO_5000147478"
FT DOMAIN 7..56
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 59..729
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 732..761
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 755..784
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 780..809
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 803..832
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 828..857
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 851..880
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1148..1463
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 492..526
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 528..551
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 586..610
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 610..632
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1062..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 881..1047
FT /evidence="ECO:0000255"
FT COMPBIAS 1069..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 206..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1520 AA; 172908 MW; 3A07CCDF9088C344 CRC64;
MAAPVIIVGS HVWVEDPHLA WIDGEVTRID GINVHVKTKK GKTVVTNVYF PKDTEAPSGG
VDDMTKLSYL HEPGVLRNLE TRYELNEIYT YTGNILIAVN PFQRLPHIYE TDMMEQYKGI
ALGELSPHVF AIGDAAYRAM INEGKNNSIL VSGESGAGKT ETTKMLMRYL AFLGGRSGVE
GRTVEQQVLE SNPVLEAFGN AKTLRNNNSS RFGKFVEIQF DKNGRISGAA IRTYLLERSR
VCQISDPERN YHCFYLLCAA PPEDIKKYKL ENPHKFHYLN QSSCYKLDGV DDASEYLETR
RAMDVVGISN EEQEAIFRVV AAILHLGNID FGKGEEIDSS VIKDKDSRSH LNMAAELLMC
NAQSLEDALI RRVMVTPEEI ITRTLDPDNA IASRDTLAKT IYSHLFDWIV NKINTSIGQD
PRSKSIIGVL DIYGFESFKC NSFEQFCINF TNEKLQQHFN QHVFKMEQEE YTKEEIAWSY
IEFIDNQDVL ELIEKKPGGI ISLLDEACMF PKSTHETFSQ KLFQTFKEHE RFAKPKLSRT
DFTISHYAGE VTYQSNHFID KNKDYIVAEH QALFTASNCK FVAGLFHALH EDSSRSSKFS
SIGSRFKQQL HSLMESLNGT EPHYIRCIKP NNVLKPGIFE NFNVIHQLRC GGVLEAIRIS
CAGYPTRLAF YDFLDRFGLL APEVLEGNYD DKVACQMILD KKSLTDYQIG KTKIFLRAGQ
MAELDARRAE VLGNAARVIQ RQFRTCMARK NYRSIRNAAI VLQSFLRGEI ARAVHKKLRI
EAAALRVQKN FRRYVDRKSF VTTRSSTIVL QTGLRAMIAR SEFRLRRQRK AAIVLQAHWR
GRQAFSYYTR LQKAAIVTQC AWRCRLARRE LRMLKMAARD TGALKDAKNK LEQRVEELSL
RLHLEKRLRT DLEEAKVQEV AKLQEALHTM RLQLKETTAM VVKEQEAARV AIEEASSVNK
EPVVVEDTEK IDSLSNEIDR LKGLLSSETH KADEAQHAYQ SALVQNEELC KKLEEAGRKI
DQLQDSVQRF QEKVFSLESE NKVLRQQTLT ISPTTRALAL RPKTTIIQRT PEKDTFSNGE
TTQLQEPETE DRPQKSLNQK QQENQELLLK SISEDIGFSE GKPVAACLIY KCLIHWRSFE
VERTSIFNRI IETIASAIEM QENSDVLCYW LSNSATLLMF LQRTLKAGAT GSITTPRRRG
MPSSLFGRVS QSFRGSPQSA GFPFMTGRAI GGGLDELRQV EAKYPALLFK QQLTAFLEKI
YGMIRDKMKK EISPLLASCI QVPRTPRSGL VKGRSQNTQN NVVAPKPMIA HWQNIVTCLN
GHLRTMRANY VPSLLISKVF GQIFSFINVQ LFNSLLLRRE CCSFSNGEYV KTGLAELEKW
CHDATEEFVG SAWDELKHIR QAVGFLVIHQ KPKKSLKEIT TELCPVLSIQ QLYRISTMYW
DDKYGTHSVS TEVIATMRAE VSDVSKSAIS NSFLLDDDSS IPFSLDDISK SMQNVEVAEV
DPPPLIRQNS NFMFLLERSD
