MYO7_ARATH
ID MYO7_ARATH Reviewed; 1730 AA.
AC F4I5Q6; O23025;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Myosin-7;
DE AltName: Full=Myosin XI A;
DE Short=AtXIA;
GN Name=XI-A; Synonyms=XIA; OrderedLocusNames=At1g04600; ORFNames=T1G11.15;
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 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=AAB80627.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002376; AAB80627.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27720.1; -; Genomic_DNA.
DR PIR; F86178; F86178.
DR RefSeq; NP_171954.1; NM_100339.2.
DR AlphaFoldDB; F4I5Q6; -.
DR SMR; F4I5Q6; -.
DR BioGRID; 24715; 1.
DR STRING; 3702.AT1G04600.1; -.
DR iPTMnet; F4I5Q6; -.
DR PaxDb; F4I5Q6; -.
DR PRIDE; F4I5Q6; -.
DR ProteomicsDB; 251276; -.
DR EnsemblPlants; AT1G04600.1; AT1G04600.1; AT1G04600.
DR GeneID; 839480; -.
DR Gramene; AT1G04600.1; AT1G04600.1; AT1G04600.
DR KEGG; ath:AT1G04600; -.
DR Araport; AT1G04600; -.
DR TAIR; locus:2197773; AT1G04600.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; F4I5Q6; -.
DR OMA; PTDFTIC; -.
DR OrthoDB; 311886at2759; -.
DR PRO; PR:F4I5Q6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I5Q6; baseline and differential.
DR Genevisible; F4I5Q6; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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; 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; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 2.
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..1730
FT /note="Myosin-7"
FT /id="PRO_0000422862"
FT DOMAIN 8..56
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 61..731
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 757..786
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 782..811
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 831..850
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 853..882
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1327..1678
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 1367..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..1224
FT /evidence="ECO:0000255"
FT COMPBIAS 1456..1470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1520
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 1730 AA; 196122 MW; 47EC2EF1072B5126 CRC64;
MAASAKVTVG SHVWVEDPDD AWIDGEVEEV NSEEITVNCS GKTVVAKLNN VYPKDPEFPE
LGVDDMTKLA YLHEPGVLLN LKCRYNANEI YTYTGNILIA VNPFKRLPHL YGSETMKQYK
GTAFGELSPH PFAVADSAYR KMINEGVSQA ILVSGESGAG KTESTKMLMQ YLAYMGGRAE
SEGRSVEQQV LESNPVLEAF GNAKTVRNNN SSRFGKFVEI QFDQRGRISG AAIRTYLLER
SRVCQVSDPE RNYHCFYMLC AAPEQETERY KLGKPSTFRY LNQSNCYALD GLDDSKEYLA
TRKAMDVVGI NSEEQDGIFR VVAAILHLGN IEFAKGEESE ASEPKDEKSR FHLKVAAELF
MCDGKALEDS LCKRVMVTRD ESITKSLDPD SAALGRDALA KIVYSKLFDW LVTKINNSIG
QDPNSKHIIG VLDIYGFESF KTNSFEQFCI NLTNEKLQQH FNQHVFKMEQ EEYTKEEIDW
SYIEFIDNQD VLDLIEKKPG GIIALLDEAC MFPRSTHDTF AQKLYQTFKN HKRFGKPKLA
QTDFTICHYA GDVTYQTELF LDKNKDYVVG EHQALLSSSD CSFVSSLFPP LPEESSKTSK
FSSIGSQFKQ QLQSLLESLS TTEPHYIRCV KPNNLLKPDI FENINILHQL RCGGVMEAIR
ISCAGYPTRK PFNEFLTRFR ILAPETTKSS YDEVDACKKL LAKVDLKGFQ IGKTKVFLRA
GQMAEMDAHR AEVLGHSARI IQRNVLTYQS RKKFLLLQAA STEIQALCRG QVARVWFETM
RREAASLRIQ KQARTYICQN AYKTLCSSAC SIQTGMRAKA ARIELQLRKK RRATIIIQSQ
IRRCLCHQRY VRTKKAAITT QCGWRVKVAR RELRNLKMAA KETGALQDAK TKLENQVEEL
TSNLELEKQM RMEIEEAKSQ EIEALQSVLT DIKLQLRDTQ ETKSKEISDL QSVLTDIKLQ
LRDTQETKSK EISDLQSALQ DMQLEIEELS KGLEMTNDLA AENEQLKESV SSLQNKIDES
ERKYEEISKI SEERIKDEVP VIDQSAIIKL ETENQKLKAL VSSMEEKIDE LDRKHDETSP
NITEKLKEDV SFDYEIVSNL EAENERLKAL VGSLEKKINE SGNNSTDEQE EGKYILKEES
LTEDASIDNE RVKKLADENK DLNDLVSSLE KKIDETEKKY EEASRLCEER LKQALDAETG
LIDLKTSMQR LEEKVSDMET AEQIRRQQAL VNSASRRMSP QVSFTGAPPL ENGHQEPLAP
IPSRRFGTES FRRSRIERQP HEFVDVLLKC VSKNIGFSHG KPVAALTIYK CLMRWKIFEA
EKTSIFDRIV PVFGSAIENQ EDDNHLAYWL TNTSTLLFLL QRSLRQQSST GSSPTKPPQP
TSFFGRMTQG FRSTSSPNLS TDVVQQVDAR YPALLFKQQL TAYVETMYGI IRENVKREVS
SLLSSCIQSL KESSCDSSVV NSPSKSSEEN LPAKSSEENS PKKSSEENSP KESSGDKSPQ
KLSDDNSPSK EGQAVKSSEE NSPASSWQSI IEFLNYILIT WKKNYVPLFL VQKMFSQTFQ
YINVQLFNSL LLEREYCTVN MGIKVKAGLD ELESWCSQAT EEFVGSSWDE LKHTRQAVVL
LVTEPKSTIT YDDLTINLCS VLSTEQLYRI CTLCKDKDDG DHNVSPEVIS NLKLLLTNED
ENSRSFLLDD DSSIPFDTDE ISSCMQEKDF ANVKSASELA DNPNFLFLKE
