CX171_ARATH
ID CX171_ARATH Reviewed; 74 AA.
AC Q9LJQ9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytochrome c oxidase copper chaperone 1;
DE AltName: Full=Cytochrome c oxidase 17 copper chaperone;
DE Short=AtCOX17;
GN Name=COX17-1; Synonyms=COX17; OrderedLocusNames=At3g15352;
GN ORFNames=K7L4.21;
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].
RA Wintz H.;
RT "COX17-1, an A. thaliana copper chaperone.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX PubMed=12177498; DOI=10.1104/pp.010963;
RA Balandin T., Castresana C.;
RT "AtCOX17, an Arabidopsis homolog of the yeast copper chaperone COX17.";
RL Plant Physiol. 129:1852-1857(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Copper chaperone for cytochrome c oxidase (COX). Binds 2
CC copper ions and delivers them to the Cu(A) site of COX (By similarity).
CC Can complement the yeast mutant cox17. {ECO:0000250,
CC ECO:0000269|PubMed:12177498}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC -!- INDUCTION: By copper, salicylic acid (SA), nitric oxide (NO) and
CC infection with P.syringae pv. tomato. {ECO:0000269|PubMed:12177498}.
CC -!- SIMILARITY: Belongs to the COX17 family. {ECO:0000305}.
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DR EMBL; AF349684; AAK73496.1; -; mRNA.
DR EMBL; AF505654; AAM95390.1; -; mRNA.
DR EMBL; AP000413; BAB02169.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75654.1; -; Genomic_DNA.
DR EMBL; BT024522; ABD38861.1; -; mRNA.
DR RefSeq; NP_566508.1; NM_112400.3.
DR AlphaFoldDB; Q9LJQ9; -.
DR SMR; Q9LJQ9; -.
DR STRING; 3702.AT3G15352.1; -.
DR iPTMnet; Q9LJQ9; -.
DR PaxDb; Q9LJQ9; -.
DR ProteomicsDB; 220509; -.
DR EnsemblPlants; AT3G15352.1; AT3G15352.1; AT3G15352.
DR GeneID; 820770; -.
DR Gramene; AT3G15352.1; AT3G15352.1; AT3G15352.
DR KEGG; ath:AT3G15352; -.
DR Araport; AT3G15352; -.
DR TAIR; locus:505006350; AT3G15352.
DR eggNOG; KOG3496; Eukaryota.
DR HOGENOM; CLU_149618_1_0_1; -.
DR InParanoid; Q9LJQ9; -.
DR OMA; ACKICCA; -.
DR PhylomeDB; Q9LJQ9; -.
DR PRO; PR:Q9LJQ9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJQ9; baseline and differential.
DR Genevisible; Q9LJQ9; AT.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0016531; F:copper chaperone activity; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0046688; P:response to copper ion; IEP:TAIR.
DR InterPro; IPR009069; Cys_alpha_HP_mot_SF.
DR InterPro; IPR007745; Cyt_c_oxidase_Cu-chaperone.
DR PANTHER; PTHR16719; PTHR16719; 1.
DR Pfam; PF05051; COX17; 1.
DR SUPFAM; SSF47072; SSF47072; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Copper; Disulfide bond; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..74
FT /note="Cytochrome c oxidase copper chaperone 1"
FT /id="PRO_0000422758"
FT DOMAIN 34..74
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..47
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 56..66
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT BINDING 34
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q14061"
FT BINDING 35
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q14061"
FT DISULFID 37..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 47..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 74 AA; 8051 MW; 053426574AE9BAA3 CRC64;
MTDQPAQNGL IPPPTSEPSK AAASAETKPK KRICCACPDT KKLRDECIVE HGESACTKWI
EAHKICLRAE GFNV
