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MT2B_ARATH
ID   MT2B_ARATH              Reviewed;          77 AA.
AC   Q38805; Q0WTI6; Q8LDX5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Metallothionein-like protein 2B;
DE            Short=MT-2B;
GN   Name=MT2B; OrderedLocusNames=At5g02380; ORFNames=T1E22_140;
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 [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=7565594; DOI=10.1007/bf02191599;
RA   Zhou J., Goldsbrough P.B.;
RT   "Structure, organization and expression of the metallothionein gene family
RT   in Arabidopsis.";
RL   Mol. Gen. Genet. 248:318-328(1995).
RN   [2]
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   [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   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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   DOI=10.1046/j.1469-8137.2003.00813.x;
RA   Guo W.J., Bundithya W., Goldsbrough P.B.;
RT   "Characterization of the Arabidopsis metallothionein gene family: tissue-
RT   specific expression and induction during senescence and in response to
RT   copper.";
RL   New Phytol. 159:369-381(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=18287486; DOI=10.1104/pp.108.115782;
RA   Guo W.J., Meetam M., Goldsbrough P.B.;
RT   "Examining the specific contributions of individual Arabidopsis
RT   metallothioneins to copper distribution and metal tolerance.";
RL   Plant Physiol. 146:1697-1706(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=24635746; DOI=10.1111/nph.12718;
RA   Benatti M.R., Yookongkaew N., Meetam M., Guo W.J., Punyasuk N.,
RA   Abuqamar S., Goldsbrough P.;
RT   "Metallothionein deficiency impacts copper accumulation and redistribution
RT   in leaves and seeds of Arabidopsis.";
RL   New Phytol. 202:940-951(2014).
CC   -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC       that bind various heavy metals (Probable). Functions as metal chelator
CC       of copper (Cu) and zinc (Zn). Functions cooperatively with the
CC       phytochelatin synthase PCS1 to protect plants from Cu and cadmium
CC       toxicity (PubMed:18287486). Plays a role in Cu homeostasis,
CC       specifically in the remobilization of Cu from senescing leaves. The
CC       mobilization of Cu from internal sources is important for seed
CC       development (PubMed:24635746). {ECO:0000269|PubMed:18287486,
CC       ECO:0000269|PubMed:24635746, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in vascular tissues of all organs.
CC       Expressed in root and leaf phloem, pollen and root hairs.
CC       {ECO:0000269|Ref.7}.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 15 family.
CC       {ECO:0000305}.
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DR   EMBL; U11256; AAA82212.1; -; Genomic_DNA.
DR   EMBL; AL162874; CAB85543.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90465.1; -; Genomic_DNA.
DR   EMBL; AF324665; AAG40016.1; -; mRNA.
DR   EMBL; AF339712; AAK00394.1; -; mRNA.
DR   EMBL; BT004570; AAO42816.1; -; mRNA.
DR   EMBL; AK227568; BAE99562.1; -; mRNA.
DR   EMBL; AY085738; AAM62956.1; -; mRNA.
DR   PIR; S57862; S57862.
DR   RefSeq; NP_195858.1; NM_120316.2.
DR   AlphaFoldDB; Q38805; -.
DR   STRING; 3702.AT5G02380.1; -.
DR   PaxDb; Q38805; -.
DR   PRIDE; Q38805; -.
DR   EnsemblPlants; AT5G02380.1; AT5G02380.1; AT5G02380.
DR   GeneID; 831816; -.
DR   Gramene; AT5G02380.1; AT5G02380.1; AT5G02380.
DR   KEGG; ath:AT5G02380; -.
DR   Araport; AT5G02380; -.
DR   TAIR; locus:2180132; AT5G02380.
DR   eggNOG; KOG4738; Eukaryota.
DR   HOGENOM; CLU_161105_1_0_1; -.
DR   InParanoid; Q38805; -.
DR   OMA; NYEVSEM; -.
DR   OrthoDB; 1627904at2759; -.
DR   PhylomeDB; Q38805; -.
DR   PRO; PR:Q38805; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q38805; baseline and differential.
DR   Genevisible; Q38805; AT.
DR   GO; GO:0005507; F:copper ion binding; IDA:TAIR.
DR   InterPro; IPR000347; Metalthion_15p.
DR   PANTHER; PTHR33543; PTHR33543; 1.
DR   Pfam; PF01439; Metallothio_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Metal-thiolate cluster; Reference proteome.
FT   CHAIN           1..77
FT                   /note="Metallothionein-like protein 2B"
FT                   /id="PRO_0000197387"
FT   CONFLICT        27
FT                   /note="P -> S (in Ref. 6; AAM62956)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   77 AA;  7766 MW;  B67CB2277F8EFFB7 CRC64;
     MSCCGGSCGC GSACKCGNGC GGCKRYPDLE NTATETLVLG VAPAMNSQYE ASGETFVAEN
     DACKCGSDCK CNPCTCK
 
 
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