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MP701_ARATH
ID   MP701_ARATH             Reviewed;         622 AA.
AC   Q9C9X0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Microtubule-associated protein 70-1;
DE            Short=AtMAP70-1;
DE   AltName: Full=70 kDa microtubule-associated protein 1;
GN   Name=MAP70.1; OrderedLocusNames=At1g68060; ORFNames=T23K23.9;
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 [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15860013; DOI=10.1111/j.1365-313x.2005.02393.x;
RA   Korolev A.V., Chan J., Naldrett M.J., Doonan J.H., Lloyd C.W.;
RT   "Identification of a novel family of 70 kDa microtubule-associated proteins
RT   in Arabidopsis cells.";
RL   Plant J. 42:547-555(2005).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17567681; DOI=10.1242/jcs.007393;
RA   Korolev A.V., Buschmann H., Doonan J.H., Lloyd C.W.;
RT   "AtMAP70-5, a divergent member of the MAP70 family of microtubule-
RT   associated proteins, is required for anisotropic cell growth in
RT   Arabidopsis.";
RL   J. Cell Sci. 120:2241-2247(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP70.5.
RX   PubMed=20399097; DOI=10.1016/j.cub.2010.02.057;
RA   Pesquet E., Korolev A.V., Calder G., Lloyd C.W.;
RT   "The microtubule-associated protein AtMAP70-5 regulates secondary wall
RT   patterning in Arabidopsis wood cells.";
RL   Curr. Biol. 20:744-749(2010).
RN   [8]
RP   INDUCTION.
RX   PubMed=20966154; DOI=10.1104/pp.110.163402;
RA   Keech O., Pesquet E., Gutierrez L., Ahad A., Bellini C., Smith S.M.,
RA   Gardestroem P.;
RT   "Leaf senescence is accompanied by an early disruption of the microtubule
RT   network in Arabidopsis.";
RL   Plant Physiol. 154:1710-1720(2010).
CC   -!- FUNCTION: Plant-specific protein that interact with microtubules. In
CC       association with MAP70.5, is essential for the normal banding pattern
CC       of secondary cell wall and for the proper development of xylem
CC       tracheary elements and wood formation. {ECO:0000269|PubMed:20399097}.
CC   -!- SUBUNIT: Interacts with MAP70.5 and itself.
CC       {ECO:0000269|PubMed:20399097}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:15860013, ECO:0000269|PubMed:17567681,
CC       ECO:0000269|PubMed:20399097}. Cytoplasm, cytoskeleton, phragmoplast
CC       {ECO:0000269|PubMed:15860013}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:15860013}. Note=Associated with microtubules in
CC       interphase arrays, preprophase bands, spindles, and phragmoplasts.
CC       Associated with microtubules in tracheary elements.
CC       {ECO:0000269|PubMed:15860013}.
CC   -!- INDUCTION: Down-regulated during senescence.
CC       {ECO:0000269|PubMed:20966154}.
CC   -!- SIMILARITY: Belongs to the MAP70 family. {ECO:0000305}.
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DR   EMBL; AM086438; CAJ31078.1; -; mRNA.
DR   EMBL; AC012563; AAG52019.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34742.1; -; Genomic_DNA.
DR   EMBL; AY074303; AAL67000.1; -; mRNA.
DR   EMBL; AY096658; AAM20292.1; -; mRNA.
DR   PIR; G96703; G96703.
DR   RefSeq; NP_176973.1; NM_105476.5.
DR   AlphaFoldDB; Q9C9X0; -.
DR   SMR; Q9C9X0; -.
DR   BioGRID; 28355; 5.
DR   IntAct; Q9C9X0; 7.
DR   STRING; 3702.AT1G68060.1; -.
DR   iPTMnet; Q9C9X0; -.
DR   MetOSite; Q9C9X0; -.
DR   PaxDb; Q9C9X0; -.
DR   PRIDE; Q9C9X0; -.
DR   ProteomicsDB; 250941; -.
DR   EnsemblPlants; AT1G68060.1; AT1G68060.1; AT1G68060.
DR   GeneID; 843134; -.
DR   Gramene; AT1G68060.1; AT1G68060.1; AT1G68060.
DR   KEGG; ath:AT1G68060; -.
DR   Araport; AT1G68060; -.
DR   TAIR; locus:2200306; AT1G68060.
DR   eggNOG; ENOG502QTPA; Eukaryota.
DR   HOGENOM; CLU_023069_0_0_1; -.
DR   InParanoid; Q9C9X0; -.
DR   OMA; HMRLKVL; -.
DR   OrthoDB; 579471at2759; -.
DR   PhylomeDB; Q9C9X0; -.
DR   PRO; PR:Q9C9X0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9X0; baseline and differential.
DR   Genevisible; Q9C9X0; AT.
DR   GO; GO:0010005; C:cortical microtubule, transverse to long axis; IDA:TAIR.
DR   GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0007010; P:cytoskeleton organization; TAS:TAIR.
DR   GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR   GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR   InterPro; IPR009768; MAP70.
DR   PANTHER; PTHR31246; PTHR31246; 1.
DR   Pfam; PF07058; MAP70; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Reference proteome.
FT   CHAIN           1..622
FT                   /note="Microtubule-associated protein 70-1"
FT                   /id="PRO_0000409457"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..483
FT                   /note="Required for targeting to microtubules"
FT   REGION          388..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          66..365
FT                   /evidence="ECO:0000255"
FT   COILED          541..590
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        388..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  69290 MW;  65E70B259001F692 CRC64;
     MSDVSADGGF LSAEQATTPV AIPTPYPSLT VSASYKEKSS GRRRPVRPSF DAAADNEFIT
     LLHGSDPVKV ELNRLENEVR DKDRELSEAN AEIKALRLSE RQREKACEEL TDELAKLDGK
     LKLTESLLQS KNLEIKKINE EKKASMAAQF AAEATLRRVH AAQKDDDMPP IEAILAPLEA
     ELKLARSEIG KLQEDNRALD RLTKSKEAAL LDAERTVETA LAKAALVDDL QNKNQELMKQ
     IEICQEENKI LDRMHRQKVA EVEKLTQTVR ELEEAVLAGG AAANAVRDYQ RKFQEMNEER
     KTLDRELARA KVTANRVATV VANEWKDGND KVMPVKQWLE ERRFLQGEMQ QLRDKLAISD
     RAAKSEAQLK DKFQLRLRVL EETLRGTSSI SIRNTPEGRS MSNGPSRRQS IGGSDNLQKF
     ASNGFLSKKT PMRNSFTSNS TSVLKNAKGT SKSFDGGTRS LDRGKALLKG PGNYSFNKAC
     DETKESESPN TWKEDSEEKP PSELPAPATE DNVPGVLYDL LQKEVVALRK SSHEKDQSLK
     DKDDAIEMLA KKVETLTKAM EVEAKKMRRE VAAMEKEVAA MRVDKDQDNR AKRSSNTKPS
     SNTAQILAAR AAGRSGLTRS TQ
 
 
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