ATOX1_ARATH
ID ATOX1_ARATH Reviewed; 76 AA.
AC Q94BT9; C0Z3B8; Q9C7U6;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Copper transport protein ATX1;
DE AltName: Full=Copper chaperone ATX1;
GN Name=ATX1; OrderedLocusNames=At1g66240; ORFNames=T6J19.6;
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 [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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP INTERACTION WITH HMA5.
RX PubMed=16367966; DOI=10.1111/j.1365-313x.2005.02601.x;
RA Andres-Colas N., Sancenon V., Rodriguez-Navarro S., Mayo S., Thiele D.J.,
RA Ecker J.R., Puig S., Penarrubia L.;
RT "The Arabidopsis heavy metal P-type ATPase HMA5 interacts with
RT metallochaperones and functions in copper detoxification of roots.";
RL Plant J. 45:225-236(2006).
RN [6]
RP FUNCTION, INTERACTION WITH RAN1, AND SUBCELLULAR LOCATION.
RX PubMed=17223078; DOI=10.1016/j.bbrc.2006.12.215;
RA Puig S., Mira H., Dorcey E., Sancenon V., Andres-Colas N.,
RA Garcia-Molina A., Burkhead J.L., Gogolin K.A., Abdel-Ghany S.E.,
RA Thiele D.J., Ecker J.R., Pilon M., Penarrubia L.;
RT "Higher plants possess two different types of ATX1-like copper
RT chaperones.";
RL Biochem. Biophys. Res. Commun. 354:385-390(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22555879; DOI=10.1104/pp.112.195974;
RA Shin L.J., Lo J.C., Yeh K.C.;
RT "Copper chaperone antioxidant protein1 is essential for copper
RT homeostasis.";
RL Plant Physiol. 159:1099-1110(2012).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=22899077; DOI=10.4161/psb.21147;
RA Shin L.J., Yeh K.C.;
RT "Overexpression of Arabidopsis ATX1 retards plant growth under severe
RT copper deficiency.";
RL Plant Signal. Behav. 7:1082-1083(2012).
CC -!- FUNCTION: Plays an important role in copper homeostasis by conferring
CC tolerance to excess of copper and subclinical copper deficiency during
CC vegetative stage. Can complement the yeast mutants atx1 and sod1.
CC {ECO:0000269|PubMed:17223078, ECO:0000269|PubMed:22555879}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with HMA5 and RAN1/HMA7.
CC {ECO:0000269|PubMed:16367966, ECO:0000269|PubMed:17223078}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17223078}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94BT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94BT9-2; Sequence=VSP_046614;
CC -!- INDUCTION: Induced by excess of copper (at protein level).
CC {ECO:0000269|PubMed:22555879}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased sensitivity to excess of
CC copper. {ECO:0000269|PubMed:22555879, ECO:0000269|PubMed:22899077}.
CC -!- MISCELLANEOUS: Over-expression of ATX1 confers increased tolerance to
CC copper excess as well as subclinical copper deficiency
CC (PubMed:22555879), but over-expressing plants are hypersensitive to
CC severe copper deficiency (PubMed:22899077).
CC {ECO:0000305|PubMed:22555879, ECO:0000305|PubMed:22899077}.
CC -!- SIMILARITY: Belongs to the ATX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51766.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK64002.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL76156.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEE34481.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC066691; AAG51766.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE34481.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE34482.1; -; Genomic_DNA.
DR EMBL; AY039898; AAK64002.1; ALT_INIT; mRNA.
DR EMBL; AY077678; AAL76156.1; ALT_INIT; mRNA.
DR EMBL; AK319082; BAH57197.1; -; mRNA.
DR PIR; D96687; D96687.
DR RefSeq; NP_001154453.1; NM_001160981.2. [Q94BT9-2]
DR RefSeq; NP_564870.1; NM_105295.4.
DR AlphaFoldDB; Q94BT9; -.
DR SMR; Q94BT9; -.
DR BioGRID; 28161; 1.
DR IntAct; Q94BT9; 2.
DR STRING; 3702.AT1G66240.1; -.
DR iPTMnet; Q94BT9; -.
DR PaxDb; Q94BT9; -.
DR PRIDE; Q94BT9; -.
DR ProteomicsDB; 246587; -. [Q94BT9-1]
DR EnsemblPlants; AT1G66240.1; AT1G66240.1; AT1G66240.
DR EnsemblPlants; AT1G66240.2; AT1G66240.2; AT1G66240. [Q94BT9-2]
DR GeneID; 842940; -.
DR Gramene; AT1G66240.1; AT1G66240.1; AT1G66240.
DR Gramene; AT1G66240.2; AT1G66240.2; AT1G66240. [Q94BT9-2]
DR KEGG; ath:AT1G66240; -.
DR Araport; AT1G66240; -.
DR TAIR; locus:2205288; AT1G66240.
DR eggNOG; KOG1603; Eukaryota.
DR OMA; MAETHTY; -.
DR OrthoDB; 1564517at2759; -.
DR PRO; PR:Q94BT9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94BT9; baseline and differential.
DR Genevisible; Q94BT9; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR InterPro; IPR045181; HIPP/ATX1-like.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR22814; PTHR22814; 1.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Copper; Copper transport;
KW Cytoplasm; Ion transport; Metal-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..76
FT /note="Copper transport protein ATX1"
FT /id="PRO_0000422760"
FT DOMAIN 2..65
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 13
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_046614"
FT CONFLICT 69
FT /note="A -> V (in Ref. 4; BAH57197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 76 AA; 8158 MW; 30874B7A605AB8F0 CRC64;
MSQTVVLRVA MTCEGCVGAV KRVLGKMEGV ESFDVDIKEQ KVTVKGNVQP DAVLQTVTKT
GKKTAFWEAE GETAKA
