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Copper transport protein ATX1 (Copper chaperone ATX1)

 ATOX1_ARATH             Reviewed;          76 AA.
Q94BT9; C0Z3B8; Q9C7U6;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
14-OCT-2015, sequence version 2.
10-OCT-2018, entry version 104.
RecName: Full=Copper transport protein ATX1;
AltName: Full=Copper chaperone ATX1;
Name=ATX1; OrderedLocusNames=At1g66240; ORFNames=T6J19.6;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia; TISSUE=Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
INTERACTION WITH HMA5.
PubMed=16367966; DOI=10.1111/j.1365-313X.2005.02601.x;
Andres-Colas N., Sancenon V., Rodriguez-Navarro S., Mayo S.,
Thiele D.J., Ecker J.R., Puig S., Penarrubia L.;
"The Arabidopsis heavy metal P-type ATPase HMA5 interacts with
metallochaperones and functions in copper detoxification of roots.";
Plant J. 45:225-236(2006).
[6]
FUNCTION, INTERACTION WITH RAN1, AND SUBCELLULAR LOCATION.
PubMed=17223078; DOI=10.1016/j.bbrc.2006.12.215;
Puig S., Mira H., Dorcey E., Sancenon V., Andres-Colas N.,
Garcia-Molina A., Burkhead J.L., Gogolin K.A., Abdel-Ghany S.E.,
Thiele D.J., Ecker J.R., Pilon M., Penarrubia L.;
"Higher plants possess two different types of ATX1-like copper
chaperones.";
Biochem. Biophys. Res. Commun. 354:385-390(2007).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[8]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=22555879; DOI=10.1104/pp.112.195974;
Shin L.J., Lo J.C., Yeh K.C.;
"Copper chaperone antioxidant protein1 is essential for copper
homeostasis.";
Plant Physiol. 159:1099-1110(2012).
[9]
DISRUPTION PHENOTYPE.
PubMed=22899077; DOI=10.4161/psb.21147;
Shin L.J., Yeh K.C.;
"Overexpression of Arabidopsis ATX1 retards plant growth under severe
copper deficiency.";
Plant Signal. Behav. 7:1082-1083(2012).
-!- FUNCTION: Plays an important role in copper homeostasis by
conferring tolerance to excess of copper and subclinical copper
deficiency during vegetative stage. Can complement the yeast
mutants atx1 and sod1. {ECO:0000269|PubMed:17223078,
ECO:0000269|PubMed:22555879}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 1 copper ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with HMA5 and RAN1/HMA7.
{ECO:0000269|PubMed:16367966, ECO:0000269|PubMed:17223078}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17223078}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q94BT9-1; Sequence=Displayed;
Name=2;
IsoId=Q94BT9-2; Sequence=VSP_046614;
Note=No experimental confirmation available.;
-!- INDUCTION: Induced by excess of copper (at protein level).
{ECO:0000269|PubMed:22555879}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but mutant plants have increased sensitivity to excess
of copper. {ECO:0000269|PubMed:22555879,
ECO:0000269|PubMed:22899077}.
-!- MISCELLANEOUS: Over-expression of ATX1 confers increased tolerance
to copper excess as well as subclinical copper deficiency
(PubMed:22555879), but over-expressing plants are hypersensitive
to severe copper deficiency (PubMed:22899077).
{ECO:0000305|PubMed:22555879, ECO:0000305|PubMed:22899077}.
-!- SIMILARITY: Belongs to the ATX1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG51766.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAK64002.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAL76156.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AEE34481.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC066691; AAG51766.1; ALT_INIT; Genomic_DNA.
EMBL; CP002684; AEE34481.1; ALT_INIT; Genomic_DNA.
EMBL; CP002684; AEE34482.1; -; Genomic_DNA.
EMBL; AY039898; AAK64002.1; ALT_INIT; mRNA.
EMBL; AY077678; AAL76156.1; ALT_INIT; mRNA.
EMBL; AK319082; BAH57197.1; -; mRNA.
PIR; D96687; D96687.
RefSeq; NP_001154453.1; NM_001160981.2. [Q94BT9-2]
RefSeq; NP_564870.1; NM_105295.4.
UniGene; At.57055; -.
ProteinModelPortal; Q94BT9; -.
SMR; Q94BT9; -.
BioGrid; 28161; 1.
IntAct; Q94BT9; 2.
STRING; 3702.AT1G66240.1; -.
iPTMnet; Q94BT9; -.
PaxDb; Q94BT9; -.
PRIDE; Q94BT9; -.
EnsemblPlants; AT1G66240.2; AT1G66240.2; AT1G66240. [Q94BT9-2]
GeneID; 842940; -.
Gramene; AT1G66240.2; AT1G66240.2; AT1G66240. [Q94BT9-2]
KEGG; ath:AT1G66240; -.
Araport; AT1G66240; -.
TAIR; locus:2205288; AT1G66240.
eggNOG; KOG1603; Eukaryota.
eggNOG; COG2608; LUCA.
HOGENOM; HOG000038877; -.
KO; K07213; -.
OrthoDB; EOG09360XMT; -.
PRO; PR:Q94BT9; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q94BT9; baseline and differential.
Genevisible; Q94BT9; AT.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0046914; F:transition metal ion binding; IBA:GO_Central.
GO; GO:0046916; P:cellular transition metal ion homeostasis; IBA:GO_Central.
GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
CDD; cd00371; HMA; 1.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
Pfam; PF00403; HMA; 1.
SUPFAM; SSF55008; SSF55008; 1.
PROSITE; PS50846; HMA_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chaperone; Complete proteome;
Copper; Copper transport; Cytoplasm; Ion transport; Metal-binding;
Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 76 Copper transport protein ATX1.
/FTId=PRO_0000422760.
DOMAIN 3 66 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 13 13 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 16 16 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
VAR_SEQ 1 10 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_046614.
CONFLICT 69 69 A -> V (in Ref. 4; BAH57197).
{ECO:0000305}.
SEQUENCE 76 AA; 8158 MW; 30874B7A605AB8F0 CRC64;
MSQTVVLRVA MTCEGCVGAV KRVLGKMEGV ESFDVDIKEQ KVTVKGNVQP DAVLQTVTKT
GKKTAFWEAE GETAKA


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