ID MYO14_ARATH Reviewed; 1516 AA.
AC F4JM19; Q9M0G3; Q9SVT9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Myosin-14;
DE AltName: Full=Myosin XI H;
DE Short=AtXIH;
GN Name=XI-H; Synonyms=XIH; OrderedLocusNames=At4g28710; ORFNames=F16A16.180;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 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 -!- 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=CAA22981.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81459.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035353; CAA22981.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161573; CAB81459.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85533.1; -; Genomic_DNA.
DR PIR; F85334; F85334.
DR PIR; T04528; T04528.
DR RefSeq; NP_194600.2; NM_119015.4.
DR AlphaFoldDB; F4JM19; -.
DR SMR; F4JM19; -.
DR STRING; 3702.F4JM19; -.
DR iPTMnet; F4JM19; -.
DR MetOSite; F4JM19; -.
DR PaxDb; 3702-AT4G28710-1; -.
DR ProteomicsDB; 248916; -.
DR EnsemblPlants; AT4G28710.1; AT4G28710.1; AT4G28710.
DR GeneID; 828991; -.
DR Gramene; AT4G28710.1; AT4G28710.1; AT4G28710.
DR KEGG; ath:AT4G28710; -.
DR Araport; AT4G28710; -.
DR TAIR; AT4G28710; XIH.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; F4JM19; -.
DR OMA; RDIRMHL; -.
DR OrthoDB; 5489458at2759; -.
DR PRO; PR:F4JM19; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JM19; baseline and differential.
DR Genevisible; F4JM19; AT.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0030048; P:actin filament-based movement; TAS:TAIR.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF851; MYOSIN-14; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 4.
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; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
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; Motor protein;
KW Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1516
FT /note="Myosin-14"
FT /id="PRO_0000422869"
FT DOMAIN 7..56
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 61..738
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 741..770
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 764..793
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 789..818
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 812..841
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..866
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 860..889
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1158..1463
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 494..528
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 530..553
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 588..612
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 612..634
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1061..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 890..1056
FT /evidence="ECO:0000255"
FT COMPBIAS 1065..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 208..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1516 AA; 172155 MW; 4A65CE5978514D51 CRC64;
MACTTVNVGS CVWVEDPEVA WIDGEVIEVK GSDIKVKCTS GKTVAIKVSS AYPKDVEAPA
SGVDDMTRLA YLHEPGVLQN MKSRFDINEI YTYTGNILIA VNPFRRLPHL YNNHMMQQYK
GAGFGELSPH PFAVADAAYR QMKNQGISQS ILVSGESGAG KTETTKLLMQ YLADMGGRAV
SEGRTVEKKV LESNPVLEAF GNAKTVRNNN SSRFGKFVEI QFDQRGRISG AAIRTYLLER
SRVCQVSDPE RNYHCFYMLC AAPPEDIKKW KLADPRKFHY LNQSQCIELE RMDDAKEYRE
TRKAMDVVGI NSEEQEAIFQ VVAAILHLGN VEFGKGKEAD SSAPKDDTSN YHLKTAAELF
MCDEQALEDS LCKRVIVTRG ETITKCLDQE SAALSRDALA KTVYSRLFDW IVNKINDSIG
QDPDSEYLIG VLDIYGFESF KTNSFEQFCI NLTNEKLQQH FNQHVFKMEQ DEYNKEEIDW
SYIEFVDNQE ILDLIEKKAG GIISLLNEAC MFPRATHETF AEKMYQTFKD HKHFSKPKLS
RTDFTICHYA GDVTYQTEQF LEKNKDYVVA EHQTLLNASR CAFVASLFPL LAEDANKKSK
FSSISSRFKQ QLVTLLETLS TTEPHYIRCV KPNNLLKPLI FENQNVLQQL RCGGVMEAIR
ISCAGFPTRK KFEEFLERFS VLAPEVLDKS TDGWPLSSTD DVACKKLLEK VALQGYQIGK
TKVFLRAGQM ADLDARRNEV LGRAASRIQR KFRSYLSRKT FLMLRKVATN MQAVCRGQLS
RLIFEGLRRD AAVLEIQRDI RMHLARKSYK ELYFAAVSIQ LGIRGMASRG RLRFQRQDKA
AIMIQSHCRK FLAQLHYQRL KKAAITTQSA WRARLARKEL RKLKMAAKET GVLEAAKSKL
EKQVEELTWK LQLEKRMRTD MEESKTQENA KLRSALEEMQ LQFKETKALH LQEVEAAKKM
AETVPVLQEV PVVDTELVEK LTSENEKLKS LVSSLDQKID ETEKKFEERS KINEERLKQA
IEAETTIVNL KTAVHELQEK ILDVESENKI LRQKSLIQAS GHLPPTPVKG SQNGHFSSKE
SPFNGSEIET LARTQEQESD AKTRRYHLDR QRENIGALIN CVVNNIGFNQ GKPVAAFTIY
KCLLHWKSFE AERTSVFDRL VQMIGSAIKD EGDNEHLAYW LSNTSTLLFM IQQSLKPGAT
PQQKTPVSTS LFGRMAMGFR SAPSSAETSA AAEAAAAAVI RPVVAKDPAL LFKQQLTAYV
EKIFGMIRDN LKNELQTLLS LCIQAPRTST GRSLRSFRSS KTMRNNSPLD HWNGIYDGLN
AILSTLQENF VPPVLIQNIF IQTFSFINVQ LFNSLLLRRE CCTFSNGEFV KSGLALLEEW
CNETTEEYAG SSWDELKHIR QAVGFMVIHK KYRISYDDIA HDLCPILSVQ QLYRICTLYW
DDSYNTRSVS QDVIANMRVL MTEDSNNADS SAFLLDEDSS IPFSADDLSS SMKEKDFAEM
KPAEELEENP AFSFLI
//
