MYO16_ARATH
ID MYO16_ARATH Reviewed; 1242 AA.
AC Q9M2K0; Q39159;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Myosin-16;
DE AltName: Full=AtMYA3;
DE AltName: Full=AtMYOS3;
DE AltName: Full=Myosin XI J;
DE Short=AtXIJ;
GN Name=XI-J; Synonyms=MYA3, MYOS3, XIJ; OrderedLocusNames=At3g58160;
GN ORFNames=F9D24.70;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [MRNA] OF 280-1242, REPEATS, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=7811972; DOI=10.1007/bf00040695;
RA Kinkema M.D., Wang H., Schiefelbein J.;
RT "Molecular analysis of the myosin gene family in Arabidopsis thaliana.";
RL Plant Mol. Biol. 26:1139-1153(1994).
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 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 [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).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617}.
CC Note=Colocalizes with cytoplasmic vesicles and/or organelles.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and leaves.
CC {ECO:0000269|PubMed:7811972}.
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=CAA84067.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL137081; CAB68154.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79749.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65823.1; -; Genomic_DNA.
DR EMBL; Z34294; CAA84067.1; ALT_FRAME; mRNA.
DR PIR; S47105; S47105.
DR PIR; T45976; T45976.
DR RefSeq; NP_001319790.1; NM_001339909.1.
DR RefSeq; NP_191375.1; NM_115678.2.
DR AlphaFoldDB; Q9M2K0; -.
DR SMR; Q9M2K0; -.
DR STRING; 3702.AT3G58160.1; -.
DR iPTMnet; Q9M2K0; -.
DR MetOSite; Q9M2K0; -.
DR PaxDb; Q9M2K0; -.
DR PRIDE; Q9M2K0; -.
DR ProteomicsDB; 251218; -.
DR EnsemblPlants; AT3G58160.1; AT3G58160.1; AT3G58160.
DR EnsemblPlants; AT3G58160.5; AT3G58160.5; AT3G58160.
DR GeneID; 824985; -.
DR Gramene; AT3G58160.1; AT3G58160.1; AT3G58160.
DR Gramene; AT3G58160.5; AT3G58160.5; AT3G58160.
DR KEGG; ath:AT3G58160; -.
DR Araport; AT3G58160; -.
DR TAIR; locus:2085340; AT3G58160.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; Q9M2K0; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q9M2K0; -.
DR PRO; PR:Q9M2K0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2K0; baseline and differential.
DR Genevisible; Q9M2K0; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; ISS:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; 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:0016787; F:hydrolase activity; 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:0030048; P:actin filament-based movement; TAS:TAIR.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01384; MYSc_Myo11; 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; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50096; IQ; 4.
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; Cytoplasm;
KW Hydrolase; Motor protein; Myosin; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1242
FT /note="Myosin-16"
FT /id="PRO_0000422871"
FT DOMAIN 6..55
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 60..729
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 732..761
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 755..784
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 780..809
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 803..832
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 828..857
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 851..880
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REPEAT 876..908
FT /note="1"
FT /evidence="ECO:0000269|PubMed:7811972"
FT REPEAT 909..940
FT /note="2"
FT /evidence="ECO:0000269|PubMed:7811972"
FT REPEAT 941..965
FT /note="3"
FT /evidence="ECO:0000269|PubMed:7811972"
FT REPEAT 966..997
FT /note="4"
FT /evidence="ECO:0000269|PubMed:7811972"
FT REPEAT 998..1029
FT /note="5"
FT /evidence="ECO:0000269|PubMed:7811972"
FT REPEAT 1030..1061
FT /note="6"
FT /evidence="ECO:0000269|PubMed:7811972"
FT REGION 493..527
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 529..552
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 587..610
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 610..632
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 869..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..1061
FT /note="6 X 33 AA repeats of Q-S-D-D-x-E-E-x(2)-H-x-R-K-x-K-
FT x(2)-I-x(2)-E-D-G-x(3)-S-x-V-x-H-S-x"
FT REGION 908..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1079..1142
FT /evidence="ECO:0000255"
FT COMPBIAS 872..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 207..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 1031
FT /note="S -> SD (in Ref. 3; CAA84067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="T -> A (in Ref. 3; CAA84067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1242 AA; 141413 MW; 9D439B81019EF4EF CRC64;
MAENIMVDSH VWVEDPERAW IDGVVLNIKG EEAEIKTNDG RDVIANLSRL YPKDTEAPSE
GVEDMTRLSY LHEPAVLDNL ATRYELNEIY TYTGNILIAV NPFQGLPHLY DAEVMEKYKE
AYFKELNPHV FAIGGIAYRE MINEGRNKCI LVSGESGSGK TETTKMLMRY LAYFGGHTAV
EGRTVENQVL ESNPVLEAFG NAKTVKNNNS SRFGKFVEIQ FDDVGRISGA AIRTYLLERS
RVCQVSDPER NYHCFYLLCA APPEDVERFK LGDPKSFRYL NQSSCYKLDG VNDAEEYLAT
RRAMDVVGIS EKEQDAIFRV VASILHLGNI EFSKGEDADS SSVKDEQSMF HLQMTSELLM
CDPHSLEDAL CKRMMVTPEE VIKRSLDPLG AAVSRDGLAK TIYSRLFDWL VNKINISIGQ
DSHSRRLIGV LDIYGFESFK TNSFEQFCIN YTNEKLQQHF NQHVFKMEQG EYQKEEIDWS
YVEFVDNKDV VDLIEKKPGG IIALLDEACM LPKSTPETFS EKLYHTFKDH KRFMKPKLTR
SDFTLVHYAG DVQYQSDQFL DKNKDYVVAE HQDLLNASKC SFVSGLFPPL PKESSKSKFS
SIGARFKLQL QQLMETLNST EPHYIRCVKP NNLLQPTVFD NANVLHQLRS GGVLEAIRVK
CAGYPTNRTF IEFLNRFLIL APEILKGEYE AEVACKWILE KKGLTGYQIG KSKVFLRAGQ
MAELDAHRTR VLGESARMIQ GQVRTRLTRE RFVLMRRASV NIQANWRGNI ARKISKEMRR
EEAAIKIQKN LRRQIAKKDY GKTKSSALTL QSGVRTMAAR HEFRYKLTTR AATVIQAYWR
GYSAISDYKK LKRVSLLCKS NLRGRIARKQ LGQSKQADRK EETEKERKVE LSNRAEEAVD
MSFVLHSEQS DDAESGHGRK AKLSIESEDG LDKSSVLHSE QSDDEELGHE RKTKLSIESE
DGHSDQSDDE EIEHERKTKH CIQAEDGIEK SYVMHSDQSD DEEIGHKRKT KHSIQAEDGI
EKSFVVHSDQ SDDEEIGHER KTKHAIQVED GIQKSFVTCS EKPYNTFSVV SQITSPIRDT
EIESLTAEVE MLKALLQVEK QRADISERKC AEARELGERR RKRLEETERR VYQLQDSLNR
LLYSMSDQFS QLKSILRSPS MSASTMASAP VVRDDLADSS ENSEASSSDS DFTFPAPSPS
SDNFSTFNPN QLQVIVQDLS TTEAKGTESY DSDKEGGFED YF
