CIA2_ARATH
ID CIA2_ARATH Reviewed; 435 AA.
AC Q9LU68; Q56Y02; Q94JU7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Protein CHLOROPLAST IMPORT APPARATUS 2;
DE Flags: Precursor;
GN Name=CIA2; OrderedLocusNames=At5g57180; ORFNames=MUL3.13;
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11549763; DOI=10.2307/3871427;
RA Sun C.-W., Chen L.-J., Lin L.-C., Li H.-M.;
RT "Leaf-specific upregulation of chloroplast translocon genes by a CCT motif-
RT containing protein, CIA2.";
RL Plant Cell 13:2053-2061(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=19386807; DOI=10.1104/pp.109.137240;
RA Sun C.-W., Huang Y.-C., Chang H.-Y.;
RT "CIA2 coordinately up-regulates protein import and synthesis in leaf
RT chloroplasts.";
RL Plant Physiol. 150:879-888(2009).
CC -!- FUNCTION: Responsible for specific up-regulation of the translocon
CC genes TOC33 and TOC75 in leaves. Involved in the general chloroplast
CC protein import pathway regulation, including protein import and protein
CC translation efficiencies. {ECO:0000269|PubMed:11549763,
CC ECO:0000269|PubMed:19386807}.
CC -!- INTERACTION:
CC Q9LU68; Q4PSE2: NFYC8; NbExp=3; IntAct=EBI-4435051, EBI-15191571;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00357, ECO:0000269|PubMed:11549763}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LU68-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LU68-2; Sequence=VSP_037773;
CC Name=3;
CC IsoId=Q9LU68-3; Sequence=VSP_037772;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and young flower buds.
CC {ECO:0000269|PubMed:11549763}.
CC -!- DISRUPTION PHENOTYPE: Pale phenotype. Defective in the general
CC chloroplast protein import pathway. {ECO:0000269|PubMed:11549763}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
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DR EMBL; AF359387; AAK51445.1; -; mRNA.
DR EMBL; AB023042; BAA97368.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96860.1; -; Genomic_DNA.
DR EMBL; AF372929; AAK50069.1; -; mRNA.
DR EMBL; AY078036; AAL77737.1; -; mRNA.
DR EMBL; AK316813; BAH19527.1; -; mRNA.
DR EMBL; AK221521; BAD94809.1; -; mRNA.
DR RefSeq; NP_001032087.1; NM_001037010.2.
DR RefSeq; NP_001332283.1; NM_001345246.1.
DR RefSeq; NP_568852.2; NM_125100.4. [Q9LU68-1]
DR RefSeq; NP_851201.1; NM_180870.2.
DR AlphaFoldDB; Q9LU68; -.
DR SMR; Q9LU68; -.
DR BioGRID; 21068; 26.
DR IntAct; Q9LU68; 26.
DR STRING; 3702.AT5G57180.2; -.
DR iPTMnet; Q9LU68; -.
DR PaxDb; Q9LU68; -.
DR PRIDE; Q9LU68; -.
DR ProteomicsDB; 246893; -. [Q9LU68-1]
DR EnsemblPlants; AT5G57180.2; AT5G57180.2; AT5G57180. [Q9LU68-1]
DR GeneID; 835824; -.
DR Gramene; AT5G57180.2; AT5G57180.2; AT5G57180. [Q9LU68-1]
DR KEGG; ath:AT5G57180; -.
DR Araport; AT5G57180; -.
DR TAIR; locus:2175564; AT5G57180.
DR eggNOG; KOG1601; Eukaryota.
DR InParanoid; Q9LU68; -.
DR OMA; DFDDDCF; -.
DR PhylomeDB; Q9LU68; -.
DR PRO; PR:Q9LU68; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU68; baseline and differential.
DR Genevisible; Q9LU68; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0045036; P:protein targeting to chloroplast; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEP:TAIR.
DR InterPro; IPR010402; CCT_domain.
DR Pfam; PF06203; CCT; 1.
DR PROSITE; PS51017; CCT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Nucleus; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..435
FT /note="Protein CHLOROPLAST IMPORT APPARATUS 2"
FT /id="PRO_0000380110"
FT DOMAIN 383..425
FT /note="CCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00357"
FT REGION 21..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 369..376
FT /note="ARLAQIDL -> VCLTLISS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_037772"
FT VAR_SEQ 420..430
FT /note="GRFVRRPNEST -> VSN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_037773"
SQ SEQUENCE 435 AA; 48410 MW; E057CA062AA2987E CRC64;
MSACLSSGGG GAAAYSFELE KVKSPPPSSS TTTTRATSPS STISESSNSP LAISTRKPRT
QRKRPNQTYN EAATLLSTAY PNIFSSNLSS KQKTHSSSNS HFYGPLLSDN DDASDLLLPY
ESIEEPDFLF HPTIQTKTEF FSDQKEVNSG GDCYGGEIEK FDFSDEFDAE SILDEDIEEG
IDSIMGTVVE SNSNSGIYES RVPGMINRGG RSSSNRIGKL EQMMMINSWN RSSNGFNFPL
GLGLRSALRE NDDTKLWKIH TVDFEQISPR IQTVKTETAI STVDEEKSDG KKVVISGEKS
NKKKKKKKMT VTTTLITESK SLEDTEETSL KRTGPLLKLD YDGVLEAWSD KTSPFPDEIQ
GSEAVDVNAR LAQIDLFGDS GMREASVLRY KEKRRTRLFS KKIRYQVRKL NADQRPRMKG
RFVRRPNEST PSGQR
