MYO2_ARATH
ID MYO2_ARATH Reviewed; 1220 AA.
AC F4K0A6; Q0WNH0; Q39157; Q9FL71;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Myosin-2;
DE AltName: Full=AtATM2;
DE AltName: Full=AtMYOS1;
GN Name=VIII-2; Synonyms=ATM2, ATM4, MYOS1; OrderedLocusNames=At5g54280;
GN ORFNames=MDK4.10;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 118-1220, 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 [5]
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 [6]
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 [7]
RP 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 [8]
RP SUBCELLULAR LOCATION, AND FUNCTION.
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 [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 (By similarity). Involved in endocytosis via its
CC action in endosomal trafficking. {ECO:0000250,
CC ECO:0000269|PubMed:18393384}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma. Endosome.
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=F4K0A6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves and roots.
CC {ECO:0000269|PubMed:7811972}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA84065.1; Type=Frameshift; 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; AB010695; BAB10751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96479.1; -; Genomic_DNA.
DR EMBL; AK229471; BAF01329.1; -; mRNA.
DR EMBL; Z34292; CAA84065.1; ALT_FRAME; mRNA.
DR PIR; S51823; S51823.
DR RefSeq; NP_001078755.1; NM_001085286.2. [F4K0A6-1]
DR AlphaFoldDB; F4K0A6; -.
DR SMR; F4K0A6; -.
DR STRING; 3702.AT5G54280.2; -.
DR iPTMnet; F4K0A6; -.
DR PaxDb; F4K0A6; -.
DR PRIDE; F4K0A6; -.
DR ProteomicsDB; 251404; -. [F4K0A6-1]
DR EnsemblPlants; AT5G54280.2; AT5G54280.2; AT5G54280. [F4K0A6-1]
DR GeneID; 835516; -.
DR Gramene; AT5G54280.2; AT5G54280.2; AT5G54280. [F4K0A6-1]
DR KEGG; ath:AT5G54280; -.
DR Araport; AT5G54280; -.
DR TAIR; locus:2162550; AT5G54280.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; F4K0A6; -.
DR OrthoDB; 311886at2759; -.
DR PRO; PR:F4K0A6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K0A6; baseline and differential.
DR Genevisible; F4K0A6; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; ISS:TAIR.
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: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: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; 3.
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 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell junction; Coiled coil; Endocytosis; Endosome; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1220
FT /note="Myosin-2"
FT /id="PRO_0000422858"
FT DOMAIN 160..209
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 213..879
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 881..910
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 904..933
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 942..971
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..672
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 759..781
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 968..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1003..1071
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 353..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 130
FT /note="I -> V (in Ref. 3; BAF01329)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="Missing (in Ref. 4; CAA84065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1220 AA; 138562 MW; 03285B139ACAEC98 CRC64;
MMLSASPNTL AKSSLEEMLE SLRQKDECDR PKDMPPALPS RPNSRARLPS ARRSLPANFN
VSSVMEDQNG SVVSVTPAVE AESERKEEGV KRKEKDLGVK RNSFGSKKMR TGLRSESPYA
AEKEEEGVKI SIAKVSLVEN TEEHNKPESE WNNNVEYFIK KKLRVWCRVS NGQWQLGKIQ
STSADTSLVM LSTANVVKVS TEELFPANPD ILEGVEDLIQ LSYLNEPSVL YNLRVRYLQD
VIYSKAGPVL IAVNPFKNVE IYGNDVISAY QKKVMDAPHV YAVADAAYDE MMREEKNQSL
IISGESGAGK TETAKFAMQY LAALGGGSCG VEYEILKTTC ILEAFGNAKT SRNANSSRFG
KLIEIHFSAM GKICGAKLET FLLEKSRVVQ LFNGERSYHI FYELCAGASP ILKERLKLKT
ASEYTYLSQS DCLTIAGVDD AQKFHKLLEA FDIVQIPKEH QERAFALLAA VLWLGNVSFR
VTDNENHVEV VADEAVANAA MLMGCNTEEL MVVLSTRKLQ AGTDCIAKKL TLRQATDMRD
GIAKFIYANL FDWLVEQINI ALEVGKSRTG RSISILDIYG FESFKNNSFE QFCINYANER
LQQHFNRHLF KLEQEEYEED GIDWTKVEFV DNQECLDLIE KKPIGLLSLL DEESNFPKAT
DLTFANKLKQ HLKTNSCFKG ERGRAFRVNH YAGEVLYDTN GFLEKNRDPL PADLINLLSS
CDCQLLKLFS TKMRGKSQKP LMLSDSTNQT VGTKFKGQLF KLMNKLENTS PHFIRCIKPN
SKQLPRVYEE DLVLQQLRCC GVLEVVRISR SGYPTRLTHQ EFAGRYGFLL SDKKVAQDPL
SVSIAVLKQY DVHPEMYQVG YTKLYLRTGQ IGIFEDRRKK VLQGIVGLQK HFRGHLSRAY
FQNMRKVTLV LQSYIRGENA RRLFDTEAKF HADSVSEAST DELSAVIHLQ SAVRGWLARK
HFNSMQRQKE LRNVATKSKR KAGRRISEDK DIPLEQPQVQ PTSMSDLQKR ILKSEAALSQ
KEEENTALRE QLRQFEERWS EYDIKMKSME ETWQKQMSSL QMSLAAARKS LAAESITGQA
GGRQDTSISP FGYDSEDTMS TGTPGVRTPT NKFTNGNTPE LRIRELNGSL NAVNHLAREF
DQRRLNFDED ARAIVEVKLG PQATPNGQQQ QHPEDEFRRL KLRFETWKKD YKARLRDTKA
RLHRVDGDKG RHRKWWGKRG
