CPP1_ARATH
ID CPP1_ARATH Reviewed; 258 AA.
AC Q9FN50;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein CHAPERONE-LIKE PROTEIN OF POR1, chloroplastic {ECO:0000303|PubMed:24151298};
DE Short=AtCPP1 {ECO:0000303|PubMed:24151298};
DE AltName: Full=Protein CELL GROWTH DEFECT FACTOR 1 {ECO:0000303|PubMed:16192270};
DE Short=AtCDF1 {ECO:0000303|PubMed:16192270};
DE Flags: Precursor;
GN Name=CPP1 {ECO:0000303|PubMed:24151298};
GN Synonyms=CDF1 {ECO:0000303|PubMed:16192270};
GN OrderedLocusNames=At5g23040 {ECO:0000312|Araport:AT5G23040};
GN ORFNames=MYJ24.3 {ECO:0000312|EMBL:BAB09821.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Callus;
RX PubMed=16192270; DOI=10.1074/jbc.m509632200;
RA Kawai-Yamada M., Saito Y., Jin L., Ogawa T., Kim K.-M., Yu L.-H., Tone Y.,
RA Hirata A., Umeda M., Uchimiya H.;
RT "A novel Arabidopsis gene causes Bax-like lethality in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 280:39468-39473(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT THR-49, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-48, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP INTERACTION WITH PORB.
RC STRAIN=cv. Columbia;
RX PubMed=24151298; DOI=10.1105/tpc.113.111096;
RA Lee J.-Y., Lee H.-S., Song J.-Y., Jung Y.J., Reinbothe S., Park Y.-I.,
RA Lee S.Y., Pai H.-S.;
RT "Cell growth defect factor1/chaperone-like protein of POR1 plays a role in
RT stabilization of light-dependent protochlorophyllide oxidoreductase in
RT Nicotiana benthamiana and Arabidopsis.";
RL Plant Cell 25:3944-3960(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=24097264; DOI=10.1007/s00425-013-1966-1;
RA Kawai-Yamada M., Nagano M., Kakimoto M., Uchimiya H.;
RT "Plastidic protein Cdf1 is essential in Arabidopsis embryogenesis.";
RL Planta 239:39-46(2014).
RN [8]
RP FUNCTION, AND INTERACTION WITH PORA.
RX PubMed=25901327; DOI=10.1073/pnas.1506339112;
RA Reinbothe S., Gray J., Rustgi S., von Wettstein D., Reinbothe C.;
RT "Cell growth defect factor 1 is crucial for the plastid import of
RT NADPH:protochlorophyllide oxidoreductase A in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5838-5843(2015).
CC -!- FUNCTION: Essential protein required during embryogenesis
CC (PubMed:24097264). Exhibits holdase chaperone activity involved in the
CC stabilization of NADPH:protochlorophyllide oxidoreductase (POR)
CC proteins against photooxidative stress during POR proteins import into
CC chloroplasts. Required for chloroplast biogenesis and development
CC (PubMed:24151298, PubMed:25901327). When expressed in yeast, triggers
CC mitochondria-mediated cell death associated with the loss of
CC mitochondrial membrane potential (PubMed:16192270).
CC {ECO:0000269|PubMed:16192270, ECO:0000269|PubMed:24097264,
CC ECO:0000269|PubMed:24151298, ECO:0000269|PubMed:25901327}.
CC -!- SUBUNIT: Interacts with PORB in chloroplast (PubMed:24151298).
CC Interacts with PORA during plastid import (PubMed:25901327).
CC {ECO:0000269|PubMed:24151298, ECO:0000269|PubMed:25901327}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:16192270}; Multi-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast envelope
CC {ECO:0000269|PubMed:24097264, ECO:0000269|PubMed:24151298}. Plastid,
CC chloroplast thylakoid membrane {ECO:0000269|PubMed:24151298}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Targeted to mitochondrion
CC when expressed in yeast. {ECO:0000269|PubMed:16192270}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously with higher levels in young
CC leaves, flowers, and the root elongation zone.
CC {ECO:0000269|PubMed:24097264}.
CC -!- DEVELOPMENTAL STAGE: Low levels in the globular stage, but accumulates
CC during early heart stage of embryogenesis and remains expressed during
CC all later embryogenesis stages. {ECO:0000269|PubMed:24097264}.
CC -!- DISRUPTION PHENOTYPE: Reduced chloroplast biogenesis and chlorophyll
CC synthesis associated with less POR protein accumulation. Photobleaching
CC and growth inhibition of plants under light conditions. In dark-grown
CC plants, reduced POR accumulation in etioplasts and impaired formation
CC of prolamellar bodies, subsequently affecting chloroplast biogenesis
CC upon illumination (PubMed:24151298). Embryo lethal with arrested
CC embryogenesis at the globular stage (PubMed:24097264).
CC {ECO:0000269|PubMed:24097264, ECO:0000269|PubMed:24151298}.
CC -!- SIMILARITY: Belongs to the chaperone-like protein of POR1 protein
CC family. {ECO:0000305}.
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DR EMBL; AB210817; BAD95465.1; -; mRNA.
DR EMBL; AB006708; BAB09821.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93112.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70165.1; -; Genomic_DNA.
DR EMBL; AY125520; AAM78111.1; -; mRNA.
DR EMBL; AY143835; AAN28774.1; -; mRNA.
DR RefSeq; NP_001331796.1; NM_001343786.1.
DR RefSeq; NP_197695.1; NM_122210.5.
DR AlphaFoldDB; Q9FN50; -.
DR SMR; Q9FN50; -.
DR STRING; 3702.AT5G23040.1; -.
DR iPTMnet; Q9FN50; -.
DR PaxDb; Q9FN50; -.
DR PRIDE; Q9FN50; -.
DR ProteomicsDB; 220486; -.
DR EnsemblPlants; AT5G23040.1; AT5G23040.1; AT5G23040.
DR EnsemblPlants; AT5G23040.2; AT5G23040.2; AT5G23040.
DR GeneID; 832368; -.
DR Gramene; AT5G23040.1; AT5G23040.1; AT5G23040.
DR Gramene; AT5G23040.2; AT5G23040.2; AT5G23040.
DR KEGG; ath:AT5G23040; -.
DR Araport; AT5G23040; -.
DR TAIR; locus:2178267; AT5G23040.
DR eggNOG; ENOG502QRPN; Eukaryota.
DR HOGENOM; CLU_064828_2_0_1; -.
DR OMA; LLQPTWT; -.
DR OrthoDB; 1076947at2759; -.
DR PhylomeDB; Q9FN50; -.
DR PRO; PR:Q9FN50; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN50; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IBA:GO_Central.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0055035; C:plastid thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IDA:TAIR.
DR GO; GO:0008219; P:cell death; IDA:TAIR.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0009704; P:de-etiolation; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:1904216; P:positive regulation of protein import into chloroplast stroma; IMP:TAIR.
DR InterPro; IPR021788; CPP1-like.
DR PANTHER; PTHR33372; PTHR33372; 1.
DR Pfam; PF11833; CPP1-like; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Chloroplast; Developmental protein; Membrane;
KW Mitochondrion; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 49..258
FT /note="Protein CHAPERONE-LIKE PROTEIN OF POR1,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432770"
FT TRANSMEM 162..182
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT REGION 67..122
FT /note="J-like domain required for holdase chaperone
FT activity"
FT /evidence="ECO:0000250|UniProtKB:G5DBJ0"
FT MOD_RES 49
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 258 AA; 28816 MW; 717AA08069D36B65 CRC64;
MSSSLLLSGS TVSSSFIAPS KPSLVRNSSK TSLLPFRNVS RSFKTVKCTV DSSYGGNVPT
FPRTRVWDPY KRLGVSPYAS EEEIWASRNF LLQQYAGHER SEESIEGAFE KLLMSSFIRR
KKTKINLKSK LKKKVEESPP WLKALLDFVE MPPMDTIFRR LFLFAFMGGW SIMNSAEGGP
AFQVAVSLAA CVYFLNEKTK SLGRACLIGI GALVAGWFCG SLIIPMIPTF LIQPTWTLEL
LTSLVAYVFL FLSCTFLK
