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MYOB3_ARATH
ID   MYOB3_ARATH             Reviewed;         675 AA.
AC   Q0WNW4; Q9LFE5;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Myosin-binding protein 3 {ECO:0000303|PubMed:23995081};
GN   Name=MYOB3 {ECO:0000303|PubMed:23995081};
GN   OrderedLocusNames=At5g16720 {ECO:0000312|Araport:AT5G16720};
GN   ORFNames=F5E19.60 {ECO:0000312|EMBL:CAC01836.1};
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 {ECO:0000312|EMBL:BAF01185.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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 [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   FUNCTION, INTERACTION WITH XI-K, DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=23995081; DOI=10.1105/tpc.113.113704;
RA   Peremyslov V.V., Morgun E.A., Kurth E.G., Makarova K.S., Koonin E.V.,
RA   Dolja V.V.;
RT   "Identification of myosin XI receptors in Arabidopsis defines a distinct
RT   class of transport vesicles.";
RL   Plant Cell 25:3022-3038(2013).
CC   -!- FUNCTION: Membrane-anchored myosin receptors that define a distinct,
CC       plant-specific transport vesicle compartment.
CC       {ECO:0000269|PubMed:23995081}.
CC   -!- SUBUNIT: Interacts with myosin XI-K. {ECO:0000269|PubMed:23995081}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DOMAIN: The GTD-binding domain is sufficient for myosin binding.
CC       {ECO:0000269|PubMed:23995081}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Myob1, myob2 and myob3
CC       triple mutant has a significant height reduction and a delayed
CC       flowering. Myob1, myob2, myob3 and myob4 quadruple mutant has a
CC       significant height reduction, a reduced rosette diameter and a delayed
CC       flowering. {ECO:0000269|PubMed:23995081}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC01836.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL391147; CAC01836.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92330.1; -; Genomic_DNA.
DR   EMBL; AK229322; BAF01185.1; -; mRNA.
DR   PIR; T51504; T51504.
DR   RefSeq; NP_197174.2; NM_121678.3.
DR   AlphaFoldDB; Q0WNW4; -.
DR   SMR; Q0WNW4; -.
DR   STRING; 3702.AT5G16720.1; -.
DR   iPTMnet; Q0WNW4; -.
DR   PaxDb; Q0WNW4; -.
DR   PRIDE; Q0WNW4; -.
DR   ProteomicsDB; 251221; -.
DR   EnsemblPlants; AT5G16720.1; AT5G16720.1; AT5G16720.
DR   GeneID; 831534; -.
DR   Gramene; AT5G16720.1; AT5G16720.1; AT5G16720.
DR   KEGG; ath:AT5G16720; -.
DR   Araport; AT5G16720; -.
DR   TAIR; locus:2149025; AT5G16720.
DR   eggNOG; ENOG502QPIG; Eukaryota.
DR   HOGENOM; CLU_009392_0_0_1; -.
DR   InParanoid; Q0WNW4; -.
DR   OMA; CMSSAKK; -.
DR   OrthoDB; 289983at2759; -.
DR   PhylomeDB; Q0WNW4; -.
DR   PRO; PR:Q0WNW4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q0WNW4; baseline and differential.
DR   Genevisible; Q0WNW4; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR   GO; GO:0080115; F:myosin XI tail binding; IDA:TAIR.
DR   InterPro; IPR007656; GTD-bd.
DR   InterPro; IPR039306; MYOB.
DR   PANTHER; PTHR31448; PTHR31448; 2.
DR   Pfam; PF04576; Zein-binding; 1.
DR   PROSITE; PS51775; GTD_BINDING; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..675
FT                   /note="Myosin-binding protein 3"
FT                   /id="PRO_0000431709"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          355..453
FT                   /note="GTD-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01111"
FT   REGION          225..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          605..633
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        474..492
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  77021 MW;  D3D56150A83A467C CRC64;
     MAANNFATKL SRNTNRITVI LVYAFLEWLL MFFIFLNSFF TYFIVKFASF FGLKQVCLLC
     PKLDRIFERK PENRFTYKEL LCQNHIAELA SLSFCRTHGK LSESANLCSD CSNREEEQSN
     IGLGFCTCCQ KSLADKPYPN YLLLKSSIWG KTLGDREDGG LILEMIDDDK FGDGFEIDRE
     SYPLGFFRDK AEEGKKQDQQ QNGEVISDVE SYGLSLREVS EEDGLRSIIS NNSPGNEAKS
     RVSEDEQRND DTSNVATYGE DQISGRVEEK EEETGVADLL YDQFESKNFT GSQIEEEEED
     REETTKELDP ETPTSVSTLF NKKLHFLARN EYAAAEDAGD GNVLVSEMDG GDPLRTIERL
     RETVRAEQEA LRDLYAELEE ERSASAISAN QTMAMITRLQ EEKAKVQMEA LQYQRMMEEQ
     AEYDQEALQL LNHLMVKREK EKEQLQRELE VYRAKVLEYE SKAKNKIIVV ENDCEADDDD
     KEEENREEDN SSEMDVDLEK ITLDCVQHMS MLGESLSEFE EERLVILDQL KVLEDRLVTM
     QDKESAEDPG EFSNSYEEAS NGHGGLTMAS MAKSLLPLLD AAENESEDGS QGLPESDEKN
     FGSDSEKLEI IKQVDSVYER LQELETDGEF LKNCMSSAKK GDKGTDILKD ILQHLRDLRT
     IELTNTIENQ TTQEE
 
 
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