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MYOB2_ARATH
ID   MYOB2_ARATH             Reviewed;         749 AA.
AC   Q9CAC4;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Myosin-binding protein 2 {ECO:0000303|PubMed:23995081};
GN   Name=MYOB2 {ECO:0000303|PubMed:23995081};
GN   OrderedLocusNames=At1g70750 {ECO:0000312|Araport:AT1G70750};
GN   ORFNames=F5A18.7 {ECO:0000312|EMBL:AAG52339.1};
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|Proteomes:UP000006548};
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   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 AND XI-1, DOMAIN, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, 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 and XI-1.
CC       {ECO:0000269|PubMed:23995081}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000269|PubMed:23995081}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaf epidermal cells, roots and root
CC       hairs. {ECO:0000269|PubMed:23995081}.
CC   -!- DOMAIN: The GTD-binding domain is sufficient for myosin binding.
CC       {ECO:0000269|PubMed:23995081}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Myob1 and myob2 double
CC       mutant has no visible phenotype, but a delayed flowering. Myob1, myob2
CC       and myob3 triple mutant has a significant height reduction and a
CC       delayed 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}.
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DR   EMBL; AC011663; AAG52339.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35110.1; -; Genomic_DNA.
DR   EMBL; AK228916; BAF00805.1; -; mRNA.
DR   PIR; A96732; A96732.
DR   RefSeq; NP_564999.2; NM_105743.4.
DR   AlphaFoldDB; Q9CAC4; -.
DR   SMR; Q9CAC4; -.
DR   STRING; 3702.AT1G70750.1; -.
DR   iPTMnet; Q9CAC4; -.
DR   PaxDb; Q9CAC4; -.
DR   PRIDE; Q9CAC4; -.
DR   ProteomicsDB; 251220; -.
DR   EnsemblPlants; AT1G70750.1; AT1G70750.1; AT1G70750.
DR   GeneID; 843412; -.
DR   Gramene; AT1G70750.1; AT1G70750.1; AT1G70750.
DR   KEGG; ath:AT1G70750; -.
DR   Araport; AT1G70750; -.
DR   TAIR; locus:2033566; AT1G70750.
DR   eggNOG; ENOG502QVIB; Eukaryota.
DR   HOGENOM; CLU_009392_0_0_1; -.
DR   InParanoid; Q9CAC4; -.
DR   OMA; LDFDMHF; -.
DR   OrthoDB; 289983at2759; -.
DR   PhylomeDB; Q9CAC4; -.
DR   PRO; PR:Q9CAC4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAC4; baseline and differential.
DR   Genevisible; Q9CAC4; AT.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
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; 1.
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..749
FT                   /note="Myosin-binding protein 2"
FT                   /id="PRO_0000431708"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          411..509
FT                   /note="GTD-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01111"
FT   REGION          164..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          589..621
FT                   /evidence="ECO:0000255"
FT   COILED          676..710
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        168..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   749 AA;  86171 MW;  0A52A02CDB6B7BAA CRC64;
     MAANKFATLI HRKTNRITLI LVYAFLEWSL IFFILLNSLF SYFILRFADY FGLKRPCLFC
     SRLDRFFDAS GKSPSHRDLL CDDHALQLHS KPVEESNCGF GEFHNDLVHR GCCVEKISSS
     LCAPIESDFG NLDYPIGDEG QIYNGLKFPR SIFVFEEEKV GSVNLNDSQE ETEEKKVPQS
     HEKLEDDDVD EEFSCYVSSF DCKNKEIATE KEEENRVDLP IEVETAESAP KNLEFYIDEE
     DCHLIPVEFY KPSEEVREIS DINGDFILDF GVEHDFTAAA ETEEISDFAS PGESKPEDAE
     TNLVASEMEN DDEETDAEVS IGTEIPDHEQ IGDIPSHQLI PHHDDDDHEE ETLEFKTVTI
     ETKMPVLNIN EERILEAQGS MESSHSSLHN AMFHLEQRVS VDGIECPEGV LTVDKLKFEL
     QEERKALHAL YEELEVERNA SAVAASETMA MINRLHEEKA AMQMEALQYQ RMMEEQAEFD
     QEALQLLNEL MVNREKENAE LEKELEVYRK RMEEYEAKEK MGMLRRRLRD SSVDSYRNNG
     DSDENSNGEL QFKNVEGVTD WKYRENEMEN TPVDVVLRLD ECLDDYDGER LSILGRLKFL
     EEKLTDLNNE EDDEEEAKTF ESNGSINGNE HIHGKETNGK HRVIKSKRLL PLFDAVDGEM
     ENGLSNGNHH ENGFDDSEKG ENVTIEEEVD ELYERLEALE ADREFLRHCV GSLKKGDKGV
     HLLHEILQHL RDLRNIDLTR VRENGDMSL
 
 
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