MYO11_ARATH
ID MYO11_ARATH Reviewed; 1529 AA.
AC F4HWY6; Q9ZVN3;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Myosin-11;
DE AltName: Full=Myosin XI E;
DE Short=AtXIE;
GN Name=XI-E; Synonyms=XIE; OrderedLocusNames=At1g54560; ORFNames=T22H22.1;
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=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 [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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18503043; DOI=10.1093/jxb/ern114;
RA Sparkes I.A., Teanby N.A., Hawes C.;
RT "Truncated myosin XI tail fusions inhibit peroxisome, Golgi, and
RT mitochondrial movement in tobacco leaf epidermal cells: a genetic tool for
RT the next generation.";
RL J. Exp. Bot. 59:2499-2512(2008).
RN [6]
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 [7]
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 [8]
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).
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. Involved in trafficking of Golgi stacks,
CC mitochondria and peroxisomes. {ECO:0000269|PubMed:18503043,
CC ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:21914656}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18503043}.
CC Note=Colocalizes with peroxisome, cytoplasmic vesicles and/or
CC 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 -!- 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=AAC64896.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005388; AAC64896.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33118.1; -; Genomic_DNA.
DR PIR; F96587; F96587.
DR RefSeq; NP_175858.1; NM_104334.2.
DR AlphaFoldDB; F4HWY6; -.
DR SMR; F4HWY6; -.
DR STRING; 3702.AT1G54560.1; -.
DR iPTMnet; F4HWY6; -.
DR PaxDb; F4HWY6; -.
DR PRIDE; F4HWY6; -.
DR ProteomicsDB; 251335; -.
DR EnsemblPlants; AT1G54560.1; AT1G54560.1; AT1G54560.
DR GeneID; 841898; -.
DR Gramene; AT1G54560.1; AT1G54560.1; AT1G54560.
DR KEGG; ath:AT1G54560; -.
DR Araport; AT1G54560; -.
DR TAIR; locus:2199449; AT1G54560.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; F4HWY6; -.
DR OrthoDB; 311886at2759; -.
DR PRO; PR:F4HWY6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HWY6; baseline and differential.
DR Genevisible; F4HWY6; 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; ISS:TAIR.
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:0000146; F:microfilament motor activity; IMP:TAIR.
DR GO; GO:0007015; P:actin filament organization; IGI:TAIR.
DR GO; GO:0030048; P:actin filament-based movement; TAS:TAIR.
DR GO; GO:0051640; P:organelle localization; IGI:TAIR.
DR GO; GO:0009860; P:pollen tube 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; 2.
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; 5.
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; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1529
FT /note="Myosin-11"
FT /id="PRO_0000422866"
FT DOMAIN 11..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 65..735
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 738..767
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 761..790
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 786..815
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 809..838
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 834..863
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 857..886
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1163..1472
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 498..532
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 534..557
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 592..616
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 616..638
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 993..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 887..1059
FT /evidence="ECO:0000255"
FT COMPBIAS 1096..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 212..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1529 AA; 173610 MW; 1176797078E8193B CRC64;
MRNSGTPVNI IVGSHVWIED SDVAWIDGLV EKINGQDVEV QATNGKKITA KLSKIYPKDM
EAPAGGVDDM TKLSYLHEPG VLQNLKIRYE LNEIYTYTGN ILIAINPFQR LPHIYDAHMM
QQYKGAPFGE LSPHVFAVAD VAYRAMINEG KSNSILVSGE SGAGKTETTK MLMRYLAYLG
GRAVTEGRTV EQQVLESNPV LEAFGNAKTV RNNNSSRFGK FVEIQFDKQG RISGAAVRTY
LLERSRVCQI SDPERNYHCF YLLCAAPQEE LEKYKLGHPK TFHYLNQSKC FELVGISDAH
DYIATRRAMD IVGMSEKEQE AIFRVVAAIL HLGNVEFTKG KEVDSSVPKD DKSKFHLNTV
AELLMCDVKA LEDALCKRVM VTPEEVIKRS LDPQSALISR DGLAKTIYSR LFDWLVEKIN
VSIGQDATSR SLIGVLDIYG FESFKTNSFE QFCINFTNEK LQQHFNQHVF KMEQEEYTKE
AIDWSYIEFV DNQDVLDLIE KKPGGIVALL DEACMFPKST HETFANKLYQ TFKTHKRFIK
PKLSRTDFAV AHYAGEVQYQ SDLFLDKNKD YVIPEHQDLL GASKCPFVVG LFPPLPEETS
KSSKFSSIGS RFKLQLQQLM ETLNSTEPHY IRCVKPNNLL KPAVFENVNI MQQLRCGGVL
EAIRISCAGY PTRKPFFEFI NRFGLLYPRA LEGNYEEKAA AQKILDNIGL KGYQVGKTKV
FLRAGQMAEL DARRTMVLSA AAKKIQRRIR THQAQRRFIL LRKATISLQA LCRGRLSSKI
FDNLRRQAAA VKIQKNARRL HSRKSYKNLH VAALVVQTGL RAMAAHKQFR FRKQTKAATT
IQAQFRCHRA TLYFKKLKKG VILSQTRWRG KLARRELRQL KMASRETGAL KEAKDMLEKK
VEELTYRAQL EKRSRVDLEE EKNQEIKKLQ SSLEEMRKKV DETNGLLVKE REAAKKAIEE
APPVVTETQV LVEDTQKIEA LTEEVEGLKA NLEQEKQRAD DATRKFDEAQ ESSEDRKKKL
EDTEKKAQQL QESVTRLEEK CNNLESENKV LRQQAVSIAP NKFLSGRSRS ILQRGSESGH
LSVDARPSLD LHSHSINRRD LSEVDDKPQK SLNEKQQENQ ELLIRCIVQH LGFQGKRPVT
ACIIYKCLLQ WRSFEVERTS VFDRIIQTIG QAIETQDNNN ILAYWLSNAS TLLLLLQRTL
KASGAAGMAP QRRRSSSATL FGRMTQSFRG TPQGVNLAMI NGGVDTLRQV EAKYPALLFK
QQLTAYVEKI YGMIRDNLKK EISPLLGLCI QAPRTSRASL VKGASRSVGN TAAQQALIAH
WQGIVKSLTN FLNNLKSNHV PPFLVRKVFT QIFSFINVQL FNSLLLRREC CSFSNGEYVK
AGLAELEHWC YNATDEYAGS SWDELKHIRQ AIGFLVIHQK PKKTLDEISH ELCPVLSIQQ
LYRISTMYWD DKYGTHSVSP DVIANMRVLM TEDSNNAVSN SFLLDDDSSI PFSVDDLSKS
MERIEIGDVE PPPLIRENSG FSFLLPCSD
