MYO9_ARATH
ID MYO9_ARATH Reviewed; 1538 AA.
AC F4HXP9; Q9FRR5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Myosin-9;
DE AltName: Full=Myosin XI C;
DE Short=AtXIC;
GN Name=XI-C; Synonyms=XIC; OrderedLocusNames=At1g08730; ORFNames=F22O13.20;
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] OF 1078-1538.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 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 and
CC mitochondria. {ECO:0000269|PubMed:19369591,
CC ECO:0000269|PubMed:21914656}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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=AAF99762.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g08720 and At1g08730.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC003981; AAF99762.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28340.1; -; Genomic_DNA.
DR EMBL; BX816587; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T00727; T00727.
DR RefSeq; NP_172349.2; NM_100746.3.
DR AlphaFoldDB; F4HXP9; -.
DR SMR; F4HXP9; -.
DR STRING; 3702.AT1G08730.1; -.
DR iPTMnet; F4HXP9; -.
DR PaxDb; F4HXP9; -.
DR PRIDE; F4HXP9; -.
DR EnsemblPlants; AT1G08730.1; AT1G08730.1; AT1G08730.
DR GeneID; 837394; -.
DR Gramene; AT1G08730.1; AT1G08730.1; AT1G08730.
DR KEGG; ath:AT1G08730; -.
DR Araport; AT1G08730; -.
DR TAIR; locus:2025535; AT1G08730.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_0_1; -.
DR InParanoid; F4HXP9; -.
DR OMA; CRWRGKI; -.
DR OrthoDB; 311886at2759; -.
DR PRO; PR:F4HXP9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HXP9; baseline and differential.
DR Genevisible; F4HXP9; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
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; 6.
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..1538
FT /note="Myosin-9"
FT /id="PRO_0000422864"
FT DOMAIN 16..65
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 70..740
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 743..772
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 766..795
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 791..820
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 814..843
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 839..868
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 862..891
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1168..1481
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 503..537
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 539..562
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 597..621
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 621..643
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1017..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 892..1064
FT /evidence="ECO:0000255"
FT COMPBIAS 1098..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 217..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1538 AA; 174626 MW; EA7866D11EBC8F7A CRC64;
MVRECFTFLN IFVLHSIGSH VWFEDPEVAW IDGEVEKING QEVVIQATTG KKVTAKLSKI
YPKDVEAPAG GVDDMTKLSY LHEPGVLQNL KIRYELNEIY TYTGNILIAI NPFQRLPHIY
DAHMMQQYKG APLGELSPHV FAVADVAYRA MINEGKSNSI LVSGESGAGK TETTKMLMRY
LAYLGGRAVT EGRTVEQQVL ESNPVLEAFG NAKTVRNNNS SRFGKFVEIQ FDKQGRISGA
AIRTYLLERS RVCQISDPER NYHCFYLLCA APQEEIEKYK LGHPKTFHYL NQSKCFELVG
ISDAHDYLAT RRAMDIVGIS EKEQEAIFRV VAAILHIGNI DFTKGKEVDS SVPKDEKSKF
HLKTAAELLM CDLKALEDAL CKRVMITPEE VIKRSLDPQS AVTSRDGLAK TVYSRLFDWL
VDKINKSIGQ DANSRSLIGV LDIYGFESFK TNSFEQFCIN FTNEKLQQHF NQHVFKMEQE
EYTKEAIDWS YIEFVDNQDV LDLIEKKPGG IVALLDEACM FPKSTHETFA NKLYQTFKTH
KRFIKPKLSR TDFAVAHYAG EVLYQSELFL DKNKDYVIPE HQDLLGASKC PFVVGLFPPL
PEETSKSSKF SSIGSRFKLQ LQQLMETLNC TEPHYIRCVK PNNLLKPAIF ENVNIMQQLR
CGGVLEAIRI SCAGYPTRKP FFEFINRFGL LSPAALEGNF DEKVACQKIL DNMGLKGYQI
GKTKVFLRAG QMAELDARRA EVLSSAAKKI QRRIRTHQAQ KRFIVLRKAT ISLQAICRGR
LSCKHYDNLR REAAAVKIQK NGRRHYSRKS YKKLHVASLV VQTGLRAMAA RKQFRFRKQT
KAATIVQAQW RCHRAISYYK KLKNGVVLSQ TRWRGRLAKR ELRKLKMAAR ETGALKEAKD
MLEKKVEELT YRVQLEKRSR GDLEEAKTQE ILKLKSSFEE MRKKVDETNA LLLKEREAAK
KAAEEAPPVI KETQILVEDT KKIELMTEEL ESVKVTLENE KQRADDAVRK FEEAQESLED
KKKKLEETEK KGQQLQESLT RMEEKCSNLE SENKVLRQQA VSMAPNKFLS GRSRSILQRG
SESGHLAVDA RSNLDLHSHS INHRDPSEVE DKPQKSLNEK QQENQDLLIR SIVQHLGFQG
NRPITACIIY KCLLQWRSFE VERTSVFDRI IQTIGHAIET QDNNNTLAYW LSNTSTLLLL
LQRTLKASGA AGMAPQRRRS SSATLFGRMS QSFRGAPPGV NLAMINGAAG GGADTFRQVE
AKYPALLFKQ QLTAYVEKIY GMIRDNLKKE ISPLLGLCIQ APRTSRASLV KGASRSVGNT
AAQQALIAHW QGIVKSLTNF LNTLKSNNVP SFLVRKVFTQ IFSFINVQLF NSLLLRRECC
SFSNGEYVKA GLSELEHWCF KATNEYAGSS WDELKHIRQA IGFLVVHQKP KKTLDEISHD
LCPVLSIQQL YRISTMYWDD KYGTHSVSPD VIANMRVLMT EDSNNAVSNS FLLDDDSSIP
FSVDDLSKSM EKFEIADIEP PPLIRENSGF SFLLPVSE
