MYO12_ARATH
ID MYO12_ARATH Reviewed; 1556 AA.
AC F4IRU3; Q9SKB0;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Myosin-12;
DE AltName: Full=Myosin XI F;
DE Short=AtXIF;
GN Name=XI-F; Synonyms=XIF; OrderedLocusNames=At2g31900; ORFNames=F20M17.6;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 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 -!- TISSUE SPECIFICITY: Preferentially expressed in stems.
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=AAD32282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006533; AAD32282.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08601.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61378.1; -; Genomic_DNA.
DR PIR; E84726; E84726.
DR PIR; S51821; S51821.
DR RefSeq; NP_001318329.1; NM_001336351.1.
DR RefSeq; NP_180749.2; NM_128748.3.
DR AlphaFoldDB; F4IRU3; -.
DR SMR; F4IRU3; -.
DR BioGRID; 3095; 1.
DR IntAct; F4IRU3; 1.
DR STRING; 3702.AT2G31900.1; -.
DR iPTMnet; F4IRU3; -.
DR PaxDb; F4IRU3; -.
DR PRIDE; F4IRU3; -.
DR ProteomicsDB; 251390; -.
DR EnsemblPlants; AT2G31900.1; AT2G31900.1; AT2G31900.
DR EnsemblPlants; AT2G31900.4; AT2G31900.4; AT2G31900.
DR GeneID; 817748; -.
DR Gramene; AT2G31900.1; AT2G31900.1; AT2G31900.
DR Gramene; AT2G31900.4; AT2G31900.4; AT2G31900.
DR KEGG; ath:AT2G31900; -.
DR Araport; AT2G31900; -.
DR TAIR; locus:2045198; AT2G31900.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; F4IRU3; -.
DR OMA; INQDEQD; -.
DR PRO; PR:F4IRU3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IRU3; baseline and differential.
DR Genevisible; F4IRU3; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0016461; C:unconventional 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; 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; 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; 5.
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 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..1556
FT /note="Myosin-12"
FT /id="PRO_0000422867"
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 62..731
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 734..763
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 757..786
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 782..811
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 805..834
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 830..859
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 853..882
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1181..1496
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 495..529
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 531..554
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 589..613
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 613..635
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 883..1091
FT /evidence="ECO:0000255"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1556 AA; 176970 MW; 80BAAC0655827ACF CRC64;
MGTPVNITLG SHVWVEDPEL AWISGEVTEI KGTNAKIVTA NGKTVVASIS SIYPKDTEAP
PAGVDDMTKL AYLHEPGVLH NLDCRFALNE IYTYTGNILI AVNPFQRLPH LYSVHMMEQY
KGAAFGELSP HLFAVADTSY RAMINEARSQ SILVSGESGA GKTETTKMLM RYLAFMGGRS
DTEGRSVEQQ VLESNPVLEA FGNAKTVKNN NSSRFGKFVE IQFDKRGKIS GAAIRTYLLE
RSRVCQVSDP ERNYHCFYML CAAPPEEAKK FKVGDPRTFH YLNQTNCYEV SNVDDAREYL
ETRNAMDIVG IGQEAQDAIF RVVAAILHLG NVNFIKGEEA DSSKLRDDKS RYHLQTAAEL
LMCNEKMMED SLCKRVIVTP DGNITKPLDP ESAASNRDAL AKTVYSRLFD WIVDKINSSI
GQDPDAKSLI GVLDIYGFES FKINSFEQLC INLTNEKLQQ HFNQHVFKME QEEYTREEIN
WSYVEFVDNQ DVLDLIEKKP GGIIALLDEA CMFPKSTHET FAQKMYQTYK GHKRFSKPKL
AQTAFTVNHY AGDVTYSAEQ FLDKNKDYVV AEHQALLDAS KCSFVANLFP PLPEDASKQS
KFSSIGTRFK QQLQALMETL NTTEPHYIRC VKPNAVLKPG IFENDNVLNQ LRCGGVLEAI
RISCAGYPTK RAFDEFLDRF VMLATDVPEG SDEKSACASI CNKMGLKGYQ IGKTKIFLRA
GQMAELDARR TEVLAGATKL IQRQIRTYLT RKEFLGQKRA TIYMQKLWRA KLARKLYQNM
RREAASICIQ KNIRAHRARK NYTKLQASAT VIQTGLRTMS ARNKHRHRRR TKAAIIIQRE
WRRHQVHEAY KKHKKATLAL QCLWRAKVAR KELKNLRMAA RETGALKEAK DKLEKRVEEL
TWRLELEKNQ KADLEDAKAQ EIAKLQNNLT ELQEKLDEAY AAIIRDKEAA KLAIEQAPPI
IKEVPVVDNT QLELLNSQNN ELEVEVAKLK GKIKEFEVKC FALENDSRAS VTEAEDAKSK
AVEFQEIIER LHTNLSNLES ENQVLRQQAL AASTSVEEIG ELNSLKDKVA ILESENETLR
RQTESAEKTM PPARVFASEK NLENEHQTKE IQATKEPRNP INVLAKQGSL TDRQQESHEV
LMKCLTDERR FDNEKSVAAW IVYKALLQWR LFEAEKTNIF DRIVHKIRSS IEGQDDTREL
AYWLTTSSTL LYLLQSTLKF SNTNNAASRR NRSSHATLFG RLVQGMQPSS VGLETSSGYS
GMAGIPNDQQ MVEAKYPALL FKQHLAAYVE KTYGMIRDKL KKEINPLLNL CIHAPRPTRA
KTLRDVTKSI HLTTIAKQQA SYVQWQNIVN KLEHTLTFMA ENHVPSMITR KLFHQVFSYI
NVQLFNSLLL RRECCSVSNG EYLKMGLHEL EQWCLKADDE ATRSPWDELQ HIRQAVMFLV
SHQKTQKSLD EIAKEICPVL SIPQVYRIGT MFWDDKYGTQ GLSPEVINQM RKLMTEDSAN
MTYPSFLLDV DSSIPFSVED VSQSFHGGNI SLSDVDPSPL LRQRSDFHFL FQTLPE
