MYO1_ARATH
ID MYO1_ARATH Reviewed; 1166 AA.
AC Q9LHE9; Q8RWT2; Q9SNF0;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Myosin-1;
DE AltName: Full=AtATM1;
GN Name=VIII-1; Synonyms=ATM, ATM1; OrderedLocusNames=At3g19960;
GN ORFNames=MZE19.1;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7684453; DOI=10.1006/jmbi.1993.1266;
RA Knight A.E., Kendrick-Jones J.;
RT "A myosin-like protein from a higher plant.";
RL J. Mol. Biol. 231:148-154(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10504577; DOI=10.1046/j.1365-313x.1999.00553.x;
RA Reichelt S., Knight A.E., Hodge T.P., Baluska F., Samaj J., Volkmann D.,
RA Kendrick-Jones J.;
RT "Characterization of the unconventional myosin VIII in plant cells and its
RT localization at the post-cytokinetic cell wall.";
RL Plant J. 19:555-567(1999).
RN [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15469496; DOI=10.1111/j.1365-313x.2004.02222.x;
RA Van Damme D., Bouget F.-Y., Van Poucke K., Inze D., Geelen D.;
RT "Molecular dissection of plant cytokinesis and phragmoplast structure: a
RT survey of GFP-tagged proteins.";
RL Plant J. 40:386-398(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18179725; DOI=10.1186/1471-2229-8-3;
RA Golomb L., Abu-Abied M., Belausov E., Sadot E.;
RT "Different subcellular localizations and functions of Arabidopsis myosin
RT VIII.";
RL BMC Plant Biol. 8:3-3(2008).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18393384; DOI=10.1002/cm.20271;
RA Sattarzadeh A., Franzen R., Schmelzer E.;
RT "The Arabidopsis class VIII myosin ATM2 is involved in endocytosis.";
RL Cell Motil. Cytoskeleton 65:457-468(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
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). Involved in endocytosis via its
CC action in endosomal trafficking. {ECO:0000250,
CC ECO:0000269|PubMed:18179725}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma. Cytoplasm,
CC cytoskeleton, phragmoplast. Endosome. Endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LHE9-1; Sequence=Displayed;
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}.
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DR EMBL; X69505; CAB61875.1; -; mRNA.
DR EMBL; AP002050; BAB03161.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76312.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63574.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63575.1; -; Genomic_DNA.
DR EMBL; AY091126; AAM14075.1; -; mRNA.
DR EMBL; BT001941; AAN71940.1; -; mRNA.
DR PIR; S33812; S33812.
DR RefSeq; NP_001325653.1; NM_001338433.1. [Q9LHE9-1]
DR RefSeq; NP_001325654.1; NM_001338432.1. [Q9LHE9-1]
DR RefSeq; NP_188630.1; NM_112886.4. [Q9LHE9-1]
DR AlphaFoldDB; Q9LHE9; -.
DR SMR; Q9LHE9; -.
DR BioGRID; 6866; 1.
DR IntAct; Q9LHE9; 1.
DR STRING; 3702.AT3G19960.2; -.
DR iPTMnet; Q9LHE9; -.
DR PRIDE; Q9LHE9; -.
DR EnsemblPlants; AT3G19960.1; AT3G19960.1; AT3G19960. [Q9LHE9-1]
DR EnsemblPlants; AT3G19960.4; AT3G19960.4; AT3G19960. [Q9LHE9-1]
DR EnsemblPlants; AT3G19960.5; AT3G19960.5; AT3G19960. [Q9LHE9-1]
DR GeneID; 821534; -.
DR Gramene; AT3G19960.1; AT3G19960.1; AT3G19960. [Q9LHE9-1]
DR Gramene; AT3G19960.4; AT3G19960.4; AT3G19960. [Q9LHE9-1]
DR Gramene; AT3G19960.5; AT3G19960.5; AT3G19960. [Q9LHE9-1]
DR KEGG; ath:AT3G19960; -.
DR Araport; AT3G19960; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_7_2_1; -.
DR PhylomeDB; Q9LHE9; -.
DR PRO; PR:Q9LHE9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHE9; baseline and differential.
DR Genevisible; Q9LHE9; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
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:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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; 2.
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; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell junction; Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis;
KW Endoplasmic reticulum; Endosome; Motor protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1166
FT /note="Myosin-1"
FT /id="PRO_0000422857"
FT DOMAIN 112..161
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 165..837
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 839..868
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 862..891
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 888..917
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 911..940
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..623
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 717..739
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1030..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 955..1005
FT /evidence="ECO:0000255"
FT COMPBIAS 27..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256..263
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"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 79
FT /note="E -> G (in Ref. 4; AAM14075)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="G -> R (in Ref. 1; CAB61875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1166 AA; 131129 MW; D3AFE4F8F219728D CRC64;
MSQKVTPFMQ SLKSLPADYR FDGSPVSDRL ENSSGASVRL TNSNVPRKGG LRNGVSRTDT
AAGDSEDSPY SGHGVFVEEQ SLTDDVDSGA ATMPLPQSDE RRWSDTSAYA RKKILQSWIQ
LPNGNWELGK ILSTSGEESV ISLPEGKVIK VISETLVPAN PDILDGVDDL MQLSYLNEPS
VLYNLNYRYN QDMIYTKAGP VLVAVNPFKE VPLYGNRYIE AYRKKSNESP HVYAIADTAI
REMIRDEVNQ SIIISGESGA GKTETAKIAM QYLAALGGGS GIEYEILKTN PILEAFGNAK
TLRNDNSSRF GKLIEIHFSE SGKISGAQIQ TFLLEKSRVV QCAEGERSYH IFYQLCAGAS
PALREKLNLT SAHEYKYLGQ SNCYSINGVD DAERFHTVKE ALDIVHVSKE DQESVFAMLA
AVLWLGNVSF TVIDNENHVE PVADESLSTV AKLIGCNINE LTLTLSKRNM RVRNDTIVQK
LTLPQAIDAR DALAKSIYSC LFDWLVEQIN KSLAVGKRRT GRSISILDIY GFESFDKNSF
EQFCINYANE RLQQHFNRHL FKLEQEEYIQ DGIDWTRVDF EDNQNCLSLF EKKPLGLLSL
LDEESTFPNG TDLTLANKLK QHLQSNSCFR GDKGKLFTVV HYAGEVTYET TGFLEKNRDL
LHSDSIQLLS SCSCLLPQAF ASSMLIQSEK PVVGPLYKAG GADSQRLSVA TKFKSQLFQL
MQRLGNTTPH FIRCIKPNNI QSPGVYEQGL VLQQLRCCGV LEVVRISRSG FPTRMSHQKF
SRRYGFLLVE NIADRDPLSV SVAILHQFNI LPEMYQVGYT KLFFRTGQIG VLEDTRNRTL
HGILRVQSSF RGYQARCLLK ELKRGISILQ SFVRGEKIRK EFAELRRRHK AAATIQSQVK
SKIARIQYKG IADASVVIQS AIRGWLVRRC SGDIGWLKSG GAKTNELGEV LVKASVLSEL
QRRVLKAEAA LREKEEENDI LQQRLQQYEN RWSEYETKMK SMEEIWQKQM RSLQSSLSIA
KKSLAVEDSA RNSDASVNAS DATDWDSSSN QFRSQTSNGV GSRLQPMSAG LSVIGRLAEE
FEQRAQVFGD DAKFLVEVKS GQVEANLDPD RELRRLKQMF ETWKKDYGGR LRETKLILSK
LGSEESSGSM EKVKRKWWGR RNSTRY
