MYO8_ARATH
ID MYO8_ARATH Reviewed; 1500 AA.
AC F4I460; O64491;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Myosin-8;
DE AltName: Full=Myosin XI B;
DE Short=AtXIB;
GN Name=XI-B; Synonyms=XIB; OrderedLocusNames=At1g04160; ORFNames=F20D22.7;
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 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 [6]
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 [7]
RP DISRUPTION PHENOTYPE.
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 [8]
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 [9]
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. {ECO:0000269|PubMed:20581304}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617}.
CC Note=Colocalizes with 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=AAC16753.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002411; AAC16753.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27664.1; -; Genomic_DNA.
DR PIR; T00957; T00957.
DR RefSeq; NP_171912.2; NM_100297.3.
DR AlphaFoldDB; F4I460; -.
DR SMR; F4I460; -.
DR BioGRID; 24481; 1.
DR STRING; 3702.AT1G04160.1; -.
DR iPTMnet; F4I460; -.
DR PaxDb; F4I460; -.
DR PRIDE; F4I460; -.
DR ProteomicsDB; 248919; -.
DR EnsemblPlants; AT1G04160.1; AT1G04160.1; AT1G04160.
DR GeneID; 839246; -.
DR Gramene; AT1G04160.1; AT1G04160.1; AT1G04160.
DR KEGG; ath:AT1G04160; -.
DR Araport; AT1G04160; -.
DR TAIR; locus:2020270; AT1G04160.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; F4I460; -.
DR OrthoDB; 311886at2759; -.
DR PRO; PR:F4I460; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I460; baseline and differential.
DR Genevisible; F4I460; 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: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:0048767; P:root hair elongation; 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; 2.30.30.360; -; 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; IPR008989; Myosin_S1_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; 6.
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..1500
FT /note="Myosin-8"
FT /id="PRO_0000422863"
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 62..732
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 735..764
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 758..787
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 783..812
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 806..835
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 831..860
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 854..883
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1146..1447
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 496..530
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 532..555
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 590..613
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 613..635
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 884..1049
FT /evidence="ECO:0000255"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 210..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1500 AA; 169493 MW; D8A0EE1A24BB4BFC CRC64;
MVATFNPAVG SHVWVEDPDE AWLDGEVVEI NGDQIKVLCA SGKQVVVKDS NIYPKDVEAP
ASGVEDMTRL AYLHEPGVLQ NLQSRYDINE IYTYTGSILI AVNPFRRLPH LYSSHMMTQY
KGASLGELSP HPFAVADAAY RQMVNEGVSQ SILVSGESGA GKTESTKLLM RYLAFMGGRG
AATEGRTVEQ KVLESNPVLE AFGNAKTVKN NNSSRFGKFV EIQFDQSGRI SGAAIRTYLL
ERSRVCQVSD PERNYHCFYM LCAAPEEDAK KFKLGDPKIY HYLNQSKCIQ LDAMNDAEEY
HATKKAMDVV GISSEEQDAI FRVVASILHL GNIEFAKGTE IDSSIPRDEK SWFHLKTAAE
LLMCNEKSLE DSLCKRIMAT RDETITKTLD PEAALLSRDA LAKVMYSRLF DWLVEKINTS
IGQDPDSKYL IGVLDIYGFE SFKTNSFEQF CINLTNEKLQ QHFNQHVFKM EQEEYKKEEI
NWSYIEFVDN QDILDLIEKK PGGIIALLDE ACMFPRSTHE TFAQKLYQTY KNHKRFTKPK
LARSDFTICH YAGDVTYQTE LFLDKNKDYV IAEHQALLNA STCSFVANLF PPVSDDSKQS
KFSSIGTRFK QQLVSLLEIL NTTEPHYIRC IKPNNLLKPG IFENQNVLQQ LRCGGVMEAI
RISCAGYPTR KHFDEFLNRF GIIAPQVLDK NSNEPAACKK LLDKAGLEGY QIGKSKVFLR
AGQMADLDTR RTEILGRSAS IIQRKVRSYL AQKTFIQLRI SATQIQAVCR GYLARSIYEG
MRREAAALKI QRDLRKFLAR KAYTELFSAT ILIQAGMRGM VSRKELCLRR QTKAATIIQT
RCRVYLARLH YRKLKKAAIT TQCAWRGKVA RKELKNLKMA ARETGALQEA KNKLEKQVEE
LTWRLQLEKR MRTDLEEAKK QENAKYESSL EEIQNKFKET EALLIKEREA AKTVSEVLPI
IKEVPVVDQE LMEKLTNENE KLKGMVSSLE IKIDETAKEL HETARISQDR LKQALAAESK
VAKLKTAMQR LEEKISDMET EKQIMLQQTI LNTPVKSVAG HPPTATIKNL ENGHRTNLEN
QFNEVEVNGN AGKSAAERQL ENVDTLIDCV KENIGFSNGK PIAAFTIYKC LLHWKCFESE
KTSAFDRLIE MIGSAIENED DNGHLAYWLT NTSALLFLLQ KSLKPAGAGA TASKKPPITT
SLFGRMALSF RSSPNLAAAA EAAALAVIRP VEAKYPALLF KQQLAAYVEK IFGMIRDNLK
KELSALISMC IQAPRISKGG IQRSARSLGK DSPAIHWQSI IDGLNSLLAI LKDNYVPLVL
IQKIHTQTFS FVNVQLFNSL LLRKECCTFS NGEFVKSGLA ELELWCGQVN EYAGPSWDEL
KHIRQAVGFL VIHQKYRVSY DDIVHDLCPI LSVQQLYRIC TLYWDDCYNT RSVSQEVISS
MRALMTEESN DADSNSFLLD DNSSIPFSID EISNSMHEKD FASVKPAKEL LENPEFVFLH
