CP123_ARATH
ID CP123_ARATH Reviewed; 134 AA.
AC Q9C9K2; Q8LEL6;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Calvin cycle protein CP12-3, chloroplastic;
DE AltName: Full=CP12 domain-containing protein 3;
DE AltName: Full=Chloroplast protein 12-3;
DE Flags: Precursor;
GN Name=CP12-3; OrderedLocusNames=At1g76560; ORFNames=F14G6.16;
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].
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY LIGHT AND HEAT.
RC STRAIN=cv. Columbia;
RX PubMed=18974062; DOI=10.1093/jxb/ern236;
RA Singh P., Kaloudas D., Raines C.A.;
RT "Expression analysis of the Arabidopsis CP12 gene family suggests novel
RT roles for these proteins in roots and floral tissues.";
RL J. Exp. Bot. 59:3975-3985(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISULFIDE BOND.
RX PubMed=20399532; DOI=10.1016/j.jplph.2010.02.008;
RA Marri L., Pesaresi A., Valerio C., Lamba D., Pupillo P., Trost P.,
RA Sparla F.;
RT "In vitro characterization of Arabidopsis CP12 isoforms reveals common
RT biochemical and molecular properties.";
RL J. Plant Physiol. 167:939-950(2010).
CC -!- FUNCTION: Acts as a linker essential in the assembly of a core complex
CC of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast
CC enzymes GAPDH and PRK during darkness in photosynthetic tissues.
CC {ECO:0000269|PubMed:20399532}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are -332 mV and -373 mV for the disulfide bonds at pH 7.9.
CC {ECO:0000269|PubMed:20399532};
CC -!- SUBUNIT: Monomer (By similarity). Component of a complex that contains
CC two dimers of PRK, two tetramers of GAPDH and CP12. CP12 associates
CC with GAPDH, causing its conformation to change. This GAPDH/CP12 complex
CC binds PRK to form a half-complex (one unit). This unit probably
CC dimerizes due partially to interactions between the enzymes of each
CC unit. {ECO:0000250, ECO:0000269|PubMed:20399532}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:20399532}.
CC -!- TISSUE SPECIFICITY: Mostly expressed, at low levels, in stems and, to a
CC lesser extent, in leaves and roots. {ECO:0000269|PubMed:18974062}.
CC -!- DEVELOPMENTAL STAGE: In flowers, restricted to the stigma and anthers.
CC {ECO:0000269|PubMed:18974062}.
CC -!- INDUCTION: Insensitive to light/darkness. Slightly repressed by heat.
CC Induced by anaerobic treatment. {ECO:0000269|PubMed:18974062}.
CC -!- PTM: Contains two disulfide bonds; only the oxidized protein, with two
CC disulfide bonds, is active in complex formation. The C-terminal
CC disulfide is involved in the interaction with GAPDH and the N-terminal
CC disulfide mediates the binding of PRK with this binary complex.
CC -!- MISCELLANEOUS: Binds copper and nickel ions. Copper ions catalyze the
CC oxidation of reduced thiol groups and thus promote formation of the
CC disulfide bonds required for linker activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CP12 family. {ECO:0000305}.
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DR EMBL; AC015450; AAG51942.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35859.1; -; Genomic_DNA.
DR EMBL; BT004753; AAO44019.1; -; mRNA.
DR EMBL; AK227842; BAE99820.1; -; mRNA.
DR EMBL; AY085359; AAM62589.1; -; mRNA.
DR PIR; F96793; F96793.
DR RefSeq; NP_565134.1; NM_106306.3.
DR AlphaFoldDB; Q9C9K2; -.
DR STRING; 3702.AT1G76560.1; -.
DR PaxDb; Q9C9K2; -.
DR PRIDE; Q9C9K2; -.
DR ProteomicsDB; 220617; -.
DR EnsemblPlants; AT1G76560.1; AT1G76560.1; AT1G76560.
DR GeneID; 843989; -.
DR Gramene; AT1G76560.1; AT1G76560.1; AT1G76560.
DR KEGG; ath:AT1G76560; -.
DR Araport; AT1G76560; -.
DR TAIR; locus:2011676; AT1G76560.
DR eggNOG; ENOG502S5FN; Eukaryota.
DR HOGENOM; CLU_1899077_0_0_1; -.
DR InParanoid; Q9C9K2; -.
DR OMA; CGEDARS; -.
DR OrthoDB; 1634668at2759; -.
DR PhylomeDB; Q9C9K2; -.
DR PRO; PR:Q9C9K2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9K2; baseline and differential.
DR Genevisible; Q9C9K2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0016151; F:nickel cation binding; ISS:UniProtKB.
DR GO; GO:0071454; P:cellular response to anoxia; IEP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEP:UniProtKB.
DR GO; GO:0080153; P:negative regulation of reductive pentose-phosphate cycle; IDA:TAIR.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR InterPro; IPR039314; CP12-like.
DR InterPro; IPR003823; CP12_dom.
DR PANTHER; PTHR33921; PTHR33921; 1.
DR SMART; SM01093; CP12; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Chloroplast; Copper; Disulfide bond; Nickel; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..134
FT /note="Calvin cycle protein CP12-3, chloroplastic"
FT /id="PRO_0000417432"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 78..87
FT /evidence="ECO:0000250"
FT DISULFID 120..129
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="Q -> H (in Ref. 5; AAM62589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 15449 MW; 0C3A826B95311B4F CRC64;
MISGSATASH GRVLLPSQRE RRPVSTGSNI LRFRETVPRQ FSLMMVTKAT AKYMGTKMRE
EKLSEMIEEK VKEATEVCEA EEMSEECRVA WDEVEEVSQA RADLRIKLKL LNQDPLESFC
QENPETDECR IYED
