ID F4JVZ5_ARATH Unreviewed; 1503 AA.
AC F4JVZ5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Myosin {ECO:0000313|EMBL:AEE86189.1};
GN Name=XI-I {ECO:0000313|EMBL:AEE86189.1, ECO:0000313|TAIR:AT4G33200};
GN Synonyms=ATXI-I {ECO:0000313|EMBL:AEE86189.1}, MYOSIN XI I
GN {ECO:0000313|EMBL:AEE86189.1}, MYOSIN XI-15
GN {ECO:0000313|EMBL:AEE86189.1}, XI-15 {ECO:0000313|EMBL:AEE86189.1};
GN OrderedLocusNames=At4g33200 {ECO:0000313|Araport:AT4G33200,
GN ECO:0000313|EMBL:AEE86189.1};
GN ORFNames=F4I10.130 {ECO:0000313|EMBL:AEE86189.1}, F4I10_130
GN {ECO:0000313|EMBL:AEE86189.1};
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 {ECO:0000313|EMBL:AEE86189.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AEE86189.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617198; DOI=10.1038/47134;
RG EU;
RG CSHL and WU Arabidopsis Sequencing Project;
RA Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Kotter 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., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA Montfort 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., Sehkon 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., Nelson J.,
RA Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA 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., Hoffmann J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
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] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000256|ARBA:ARBA00008049}.
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DR EMBL; CP002687; AEE86189.1; -; Genomic_DNA.
DR RefSeq; NP_001190897.1; NM_001203968.1.
DR SMR; F4JVZ5; -.
DR ProteomicsDB; 206279; -.
DR EnsemblPlants; AT4G33200.3; AT4G33200.3; AT4G33200.
DR GeneID; 829456; -.
DR Gramene; AT4G33200.3; AT4G33200.3; AT4G33200.
DR Araport; AT4G33200; -.
DR TAIR; AT4G33200; XI-I.
DR OMA; LGHPRSF; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JVZ5; baseline and differential.
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-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.5.340; -; 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; 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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF781; MYOSIN-15; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 4.
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; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 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 {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4JVZ5,
KW ECO:0007829|ProteomicsDB:F4JVZ5};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT DOMAIN 12..61
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 67..737
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1164..1471
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 618..640
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 882..916
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 956..1056
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1503 AA; 171102 MW; 4B901AD843785D3F CRC64;
MRNCLPMELN LRKGDKVWVE DKDLAWIAAD VLDSFDNKLH VETSTGKKVF VSPEKLFRRD
PDDEEHNGVD DMTKLTYLHE AGVLYNLQRR YALNDIYTYT GSILIAVNPF KKLPHLYNGH
MMEQYMGAPF GELSPHVFAV SDVAYRAMID DSRSQSILVS GESGAGKTET TKLIMQYLTF
VGGRATDDDR SVEQQVLESN PLLEAFGNAK TVRNDNSSRF GKFVEIQFDT NGRISGAAIR
TYLLERSRVV RITDPERNYH CFYQLCASGN DAEKYKLSNP RQFHYLNQSK TYELEGVSSA
EEYKNTRRAM DIVGISQDEQ EGIFRTLAAI LHLGNVEFSS GREHDSSVVK DPESRHHLQM
AADLFKCDAN LLLASLCTRS ILTREGIIIK ALDPNAAVTS RDTLAKTVYA HLFDWLVDKI
NKSVGQDPES RFQIGVLDIY GFECFKNNSF EQFCINFANE KLQQHFNEHV FKMEQDEYRK
EEINWSYIEF IDNQDVLDLI EKKPIGVIAL LDEACMFPRS THESFSMKLF QNFRFHPRLE
KPKFSETDFT LSHYAGKVTY QTEAFLDKNR DYTIVEHCNL LSSSKCPFVA GIFPSAPEES
TRSSYKFSSV SSRFKQQLQA LMETLSKTEP HYVRCVKPNS LNRPQKFESL SVLHQLRCGG
VLEAVRISLA GYPTRRNYSD FVDRFGLLAP EFMDESNDEQ ALTEKILSKL GLGNYQLGRT
KVFLRAGQIG ILDSRRAEVL DASARLIQRR LRTFVTHQNF ISARASAISI QAYCRGCLSR
NAYATRRNAA AAVLVQKHVR RWLSRCAFVK LVSAAIVLQS CIRADSTRLK FSHQKEHRAA
SLIQAHWRIH KFRSAFRHRQ SSIIAIQCRW RQKLAKREFR KLKQVANEAG ALRLAKTKLE
KRLEDLEWRL QLEKRLRTSG EEAKSSEISK LQKTLESFSL KLDAARLATI NECNKNAVLE
KQLDISMKEK SAVERELNGM VELKKDNALL KNSMNSLEKK NRVLEKELLN AKTNCNNTLQ
KLKEAEKRCS ELQTSVQSLE EKLSHLENEN QVLMQKTLIT SPERIGQILG EKHSSAVVPA
QNDRRSVFET PTPSKHIMPF SHSLSESRRS KLTAERNLEN YELLSRCIKE NLGFNDDKPL
AACVIYKCLL HWRAFESEST AIFNIIIEGI NEALKGGDEN GVLPYWLSNA SALLCLLQRN
LRSNSFLNAS AQRSGRAAYG VKSPFKLHGP DDGASHIEAR YPALLFKQQL TACVEKIYGL
IRDNLKKELS PLLGSCIQAP KASRGIAGKS RSPGGVPQQS PSSQWESILK FLDSLMSRLR
ENHVPSFFIR KLVTQVFSFI NLSLFNSLLL RRECCTFSNG EYVKSGISEL EKWIANAKEE
FAGTSWHELN YIRQAVGFLV LTIRQIYRIS TMYWDDKYGT QSVSSEVVSQ MRVLVDKDNQ
KQTSNSFLLD DDMSIPFSAE DIDKAIPVLD PSEIEPPKFV SEYTCAQSLV KKPSIASTSK
QII
//
