CCH_ARATH
ID CCH_ARATH Reviewed; 121 AA.
AC O82089;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Copper transport protein CCH;
DE AltName: Full=Copper chaperone CCH;
GN Name=CCH; OrderedLocusNames=At3g56240; ORFNames=F18O21.200;
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], FUNCTION, AND INDUCTION BY SENESCENCE.
RX PubMed=9701579; DOI=10.1104/pp.117.4.1227;
RA Himelblau E., Mira H., Lin S.J., Cizewski Culotta V., Penarrubia L.,
RA Amasino R.M.;
RT "Identification of a functional homolog of the yeast copper homeostasis
RT gene ATX1 from Arabidopsis.";
RL Plant Physiol. 117:1227-1234(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION.
RX PubMed=11439106; DOI=10.1042/0264-6021:3570545;
RA Mira H., Vilar M., Perez-Paya E., Penarrubia L.;
RT "Functional and conformational properties of the exclusive C-domain from
RT the Arabidopsis copper chaperone (CCH).";
RL Biochem. J. 357:545-549(2001).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11309142; DOI=10.1046/j.1365-313x.2001.00985.x;
RA Mira H., Martinez-Garcia F., Penarrubia L.;
RT "Evidence for the plant-specific intercellular transport of the Arabidopsis
RT copper chaperone CCH.";
RL Plant J. 25:521-528(2001).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 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).
CC -!- FUNCTION: Involved in copper homeostasis. Can complement the yeast
CC mutants atx1 and sod1. {ECO:0000269|PubMed:11439106,
CC ECO:0000269|PubMed:9701579}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- TISSUE SPECIFICITY: Expressed in phloem (at protein level).
CC {ECO:0000269|PubMed:11309142}.
CC -!- INDUCTION: Induced by copper deficiency, ozone and senescence. Down-
CC regulated by excess of copper. {ECO:0000269|PubMed:11309142,
CC ECO:0000269|PubMed:22555879, ECO:0000269|PubMed:9701579}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:22555879}.
CC -!- SIMILARITY: Belongs to the ATX1 family. {ECO:0000305}.
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DR EMBL; U88711; AAC33510.1; -; mRNA.
DR EMBL; AL163763; CAB87423.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79500.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64077.1; -; Genomic_DNA.
DR EMBL; AF361860; AAK32872.1; -; mRNA.
DR EMBL; AY066056; AAL47423.1; -; mRNA.
DR EMBL; AY085657; AAM62878.1; -; mRNA.
DR PIR; T47741; T47741.
DR RefSeq; NP_001326128.1; NM_001339780.1.
DR RefSeq; NP_191183.1; NM_115482.4.
DR AlphaFoldDB; O82089; -.
DR SMR; O82089; -.
DR BioGRID; 10106; 2.
DR IntAct; O82089; 1.
DR STRING; 3702.AT3G56240.1; -.
DR iPTMnet; O82089; -.
DR PaxDb; O82089; -.
DR PRIDE; O82089; -.
DR ProteomicsDB; 223917; -.
DR EnsemblPlants; AT3G56240.1; AT3G56240.1; AT3G56240.
DR EnsemblPlants; AT3G56240.3; AT3G56240.3; AT3G56240.
DR GeneID; 824790; -.
DR Gramene; AT3G56240.1; AT3G56240.1; AT3G56240.
DR Gramene; AT3G56240.3; AT3G56240.3; AT3G56240.
DR KEGG; ath:AT3G56240; -.
DR Araport; AT3G56240; -.
DR TAIR; locus:2078461; AT3G56240.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_134973_3_0_1; -.
DR InParanoid; O82089; -.
DR OMA; MYYQYMQ; -.
DR OrthoDB; 1564517at2759; -.
DR PhylomeDB; O82089; -.
DR PRO; PR:O82089; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O82089; baseline and differential.
DR Genevisible; O82089; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016531; F:copper chaperone activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:TAIR.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
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; Chaperone; Copper; Copper transport; Ion transport;
KW Metal-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..121
FT /note="Copper transport protein CCH"
FT /id="PRO_0000422761"
FT DOMAIN 2..65
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 70..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 121 AA; 12971 MW; 271D38907ED4012C CRC64;
MAQTVVLKVG MSCQGCVGAV NRVLGKMEGV ESFDIDIKEQ KVTVKGNVEP EAVFQTVSKT
GKKTSYWPVE AEAEPKAEAD PKVETVTETK TEAETKTEAK VDAKADVEPK AAEAETKPSQ
V
