MYO3_ARATH
ID MYO3_ARATH Reviewed; 1153 AA.
AC F4I507; Q56ZX3; Q9SX51;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Myosin-3;
DE AltName: Full=Myosin VIII A;
DE Short=AtVIIIA;
GN Name=VIII-A; Synonyms=VIIIA; OrderedLocusNames=At1g50360; ORFNames=F14I3.6;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 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=AAD50052.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007980; AAD50052.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32540.1; -; Genomic_DNA.
DR EMBL; AK220707; BAD93813.1; -; mRNA.
DR EMBL; AK220837; BAD94158.1; -; mRNA.
DR EMBL; AK220844; BAD94177.1; -; mRNA.
DR PIR; G96539; G96539.
DR RefSeq; NP_175453.2; NM_103919.5.
DR AlphaFoldDB; F4I507; -.
DR SMR; F4I507; -.
DR STRING; 3702.AT1G50360.1; -.
DR iPTMnet; F4I507; -.
DR PaxDb; F4I507; -.
DR PRIDE; F4I507; -.
DR ProteomicsDB; 251275; -.
DR EnsemblPlants; AT1G50360.1; AT1G50360.1; AT1G50360.
DR GeneID; 841458; -.
DR Gramene; AT1G50360.1; AT1G50360.1; AT1G50360.
DR KEGG; ath:AT1G50360; -.
DR Araport; AT1G50360; -.
DR TAIR; locus:2011922; AT1G50360.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_7_2_1; -.
DR InParanoid; F4I507; -.
DR OMA; ENRDQCI; -.
DR OrthoDB; 311886at2759; -.
DR PRO; PR:F4I507; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I507; baseline and differential.
DR Genevisible; F4I507; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA: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; 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:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01383; MYSc_Myo8; 1.
DR Gene3D; 3.40.850.10; -; 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 Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Motor protein;
KW Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1153
FT /note="Myosin-3"
FT /id="PRO_0000422859"
FT DOMAIN 104..153
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 157..829
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 831..860
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 854..883
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 903..932
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 581..615
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 709..731
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1020..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 948..996
FT /evidence="ECO:0000255"
FT COMPBIAS 1022..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 296..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 423
FT /note="T -> S (in Ref. 3; BAD93813/BAD94158/BAD94177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1153 AA; 130009 MW; 31E6C6B41D9B47A3 CRC64;
MAHKVKASFQ SLKTMPADYR FLGSPISDHL ETNLITPPNG HLKNGVNGTA SSVGGMDSVN
EDSPYSVRSI LNGERSSIGD GDSILPLPES NDRKWSDTNV YARKKVLQFW VQLPNGNWEL
GKIMSTSGEE SVIVVTEGKV LKVKSETLVP ANPDILDGVD DLMQLSYLNE PAVLYNLEYR
YNQDMIYTKA GPVLVAVNPF KEVPLYGNRN IEAYRKRSNE SPHVYAIADT AIREMIRDEV
NQSIIISGES GAGKTETAKI AMQYLAALGG GSGIEYEILK TNPILEAFGN AKTLRNDNSS
RFGKLIEIHF SETGKISGAQ IQTFLLEKSR VVQCTEGERS YHIFYQLCAG ASPTLREKLN
LTSAKQYNYL KQSNCYSING VDDAERFHAV KEALDIVHVS KEDQENVFAM LAAVLWLGNV
SFTIIDNENH VEPEPDESLS TVAKLIGCNI NELKLALSKR NMRVNNDTIV QKLTLSQAID
ARDALAKSIY ACLFDWLVEQ INKSLAVGKR RTGRSISILD IYGFESFNKN SFEQFCINYA
NERLQQHFNR HLFKLEQEEY IQDGIDWTRV DFEDNQECLS LFEKKPLGLL SLLDEESTFP
NGTDLTLANK LKQHLNDNSC FRGDRGKAFT VAHYAGEVTY ETTGFLEKNR DLLHSDSIQL
LSSCSCHLPQ AFASSMLIYS EKPLVGPLHK AGGADSQRLS VATKFKGQLF QLMQRLGNTT
PHFIRCIKPN NVQSAGLYEQ GLVLQQLRCC GVLEVVRISR SGFPTRMFHH KFARRYGFLL
LENIAAKDPL SVSVAILHQF NILPEMYQVG YTKLFFRTGQ IGVLEDTRNR TLHGILRLQS
YFRGHQARCR LKELKTGITI LQSFVRGEKM RKEYTELLQR HRASAAIQSH VKRRIASQQY
KATVDASAVI QSAIRGELVR RCAGDIGWLS SGGTKRNESD EVLVKASYLS DLQRRVLRTE
AALREKEEEN DILRQRVQQY DNRWSEYETK MKSMEEIWQK QMKSLQSSLS IAKKSLEVED
SARNSDASVN ASDATDLDSG GSHYQMGHGR SRSVGVGLSV ISRLAEEFGQ RAQVFGDDRK
FLMEVKSGQV EANLNPDREL RRLKQMFETW KKDYGGRLRE TKLILSKLGS EETGGSAEKV
KMNWWGRLRS TRY
