CUTA_ARATH
ID CUTA_ARATH Reviewed; 182 AA.
AC P93009; Q147J1; Q9C5X6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein CutA, chloroplastic;
DE AltName: Full=Copper-binding protein CutA;
DE Short=AtCUTA;
DE Flags: Precursor;
GN Name=CUTA; OrderedLocusNames=At2g33740; ORFNames=T1B8.5;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, SUBUNIT, AND FUNCTION.
RX PubMed=12795705; DOI=10.1046/j.1365-313x.2003.01769.x;
RA Burkhead J.L., Abdel-Ghany S.E., Morrill J.M., Pilon-Smits E.A., Pilon M.;
RT "The Arabidopsis thaliana CUTA gene encodes an evolutionarily conserved
RT copper binding chloroplast protein.";
RL Plant J. 34:856-867(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in metal homeostasis. Specifically binds Cu(2+). The
CC truncated isoform has less specificity in metal binding.
CC {ECO:0000269|PubMed:12795705}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12795705}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast intermembrane space
CC {ECO:0000269|PubMed:12795705}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P93009-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P93009-2; Sequence=VSP_014980, VSP_014981;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves, stems and roots.
CC {ECO:0000269|PubMed:12795705}.
CC -!- DOMAIN: A central prokaryotic signal-sequence-like domain may be used
CC to export the protein to the chloroplast envelope after import into the
CC stroma.
CC -!- MISCELLANEOUS: Knockout lines indicate that CUTA is not essential for
CC copper tolerance or accumulation.
CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}.
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DR EMBL; AF327524; AAK11228.1; -; mRNA.
DR EMBL; AF327525; AAK11229.1; -; mRNA.
DR EMBL; U78721; AAC69129.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08877.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08878.1; -; Genomic_DNA.
DR EMBL; BT026102; ABG48458.1; -; mRNA.
DR PIR; A84749; A84749.
DR RefSeq; NP_180930.1; NM_128933.4. [P93009-1]
DR RefSeq; NP_850217.1; NM_179886.1. [P93009-2]
DR AlphaFoldDB; P93009; -.
DR SMR; P93009; -.
DR STRING; 3702.AT2G33740.2; -.
DR iPTMnet; P93009; -.
DR PaxDb; P93009; -.
DR PRIDE; P93009; -.
DR ProteomicsDB; 222724; -. [P93009-1]
DR EnsemblPlants; AT2G33740.1; AT2G33740.1; AT2G33740. [P93009-2]
DR EnsemblPlants; AT2G33740.2; AT2G33740.2; AT2G33740. [P93009-1]
DR GeneID; 817940; -.
DR Gramene; AT2G33740.1; AT2G33740.1; AT2G33740. [P93009-2]
DR Gramene; AT2G33740.2; AT2G33740.2; AT2G33740. [P93009-1]
DR KEGG; ath:AT2G33740; -.
DR Araport; AT2G33740; -.
DR TAIR; locus:2057651; AT2G33740.
DR eggNOG; KOG3338; Eukaryota.
DR HOGENOM; CLU_098807_0_0_1; -.
DR InParanoid; P93009; -.
DR OMA; LQYLEWI; -.
DR OrthoDB; 1589955at2759; -.
DR PhylomeDB; P93009; -.
DR PRO; PR:P93009; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93009; baseline and differential.
DR Genevisible; P93009; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031972; C:chloroplast intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IDA:TAIR.
DR GO; GO:0010038; P:response to metal ion; IEA:InterPro.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR004323; Ion_tolerance_CutA.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR23419; PTHR23419; 1.
DR Pfam; PF03091; CutA1; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Copper; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..182
FT /note="Protein CutA, chloroplastic"
FT /id="PRO_0000006384"
FT VAR_SEQ 156
FT /note="D -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12795705, ECO:0000303|Ref.4"
FT /id="VSP_014980"
FT VAR_SEQ 157..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12795705, ECO:0000303|Ref.4"
FT /id="VSP_014981"
SQ SEQUENCE 182 AA; 19771 MW; CC178325DCF8439F CRC64;
MASSLTTRLS AVIGSRRSFP IVGAFCVLST LSISSLSSSS PFKSGCAQSF SVVPLLRSKF
SSKAFSSSIR MEESSKTVPS IVVYVTVPNR EAGKKLANSI VQEKLAACVN IVPGIESVYE
WEGKVQSDSE ELLIIKTRQS LLEPLTEHVN ANHEYDVPEV IALPITGGSD KYLEWLKNST
RN
