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O22265

- SR43C_ARATH

UniProt

O22265 - SR43C_ARATH

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Protein

Signal recognition particle 43 kDa protein, chloroplastic

Gene

CAO

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Component of the chloroplast signal recognition particle pathway. Required for post-translational targeting of proteins into the tylakoid membrane but seems to be dispensable for co-translational targeting with a translating ribosome present. May be able to function independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the thylakoids. Acts as a highly specific chaperone for LHCPs, preventing aggregation and being able to dissolve aggregates.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi232 – 2321Magnesium

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein import into chloroplast thylakoid membrane Source: TAIR
  2. response to high light intensity Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

Metal-binding

Protein family/group databases

TCDBi3.A.5.1.2. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle 43 kDa protein, chloroplastic
Alternative name(s):
Chromo protein SRP43
Short name:
CpSRP43
Gene namesi
Name:CAO
Synonyms:CPSRP43
Ordered Locus Names:At2g47450
ORF Names:T30B22.25
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G47450.

Subcellular locationi

Plastidchloroplast stroma 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast envelope Source: TAIR
  3. chloroplast thylakoid membrane Source: TAIR
  4. signal recognition particle, chloroplast targeting Source: TAIR
  5. signal recognition particle, endoplasmic reticulum targeting Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Signal recognition particle

Pathology & Biotechi

Disruption phenotypei

Plants show a reduced level of the major light-harvesting chlorophyll a/b-binding proteins (LHCPs).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1611R → A: Decreased interaction with LHCP. 1 Publication
Mutagenesisi192 – 1921R → A: Decreased interaction with LHCP. 1 Publication
Mutagenesisi204 – 2041Y → A: Loss of interaction with LHCP. 1 Publication
Mutagenesisi226 – 2261R → A: Decreased interaction with LHCP. 1 Publication
Mutagenesisi269 – 2691Y → A: Decreased interaction with ALB3. 1 Publication
Mutagenesisi291 – 2911W → A: Decreased interaction with ALB3. 1 Publication
Mutagenesisi293 – 2931D → A: Decreased interaction with ALB3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5656ChloroplastSequence AnalysisAdd
BLAST
Chaini57 – 373317Signal recognition particle 43 kDa protein, chloroplasticPRO_0000238461Add
BLAST

Proteomic databases

PaxDbiO22265.
PRIDEiO22265.

Expressioni

Tissue specificityi

Expressed in leaves. Detected in roots.2 Publications

Gene expression databases

GenevestigatoriO22265.

Interactioni

Subunit structurei

Homodimer. Component of the cpSRP complex, composed of a FFC/cpSRP54 monomer and a CAO/cpSRP43 dimer. Interacts (via chromo domains 2 and 3) with ALB3 (via C-terminus), but not with ALB3L1/ALB4. Can interact simultaneously with ALB3 and FFC/cpSRP54. Interacts with LHCP and LTD.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-780656,EBI-780656
ALB3Q8LBP410EBI-780656,EBI-1806831
CAB8P274904EBI-780656,EBI-8295162From a different organism.
FFCP3710716EBI-780656,EBI-780642

Protein-protein interaction databases

BioGridi4693. 13 interactions.
DIPiDIP-37639N.
IntActiO22265. 19 interactions.
MINTiMINT-126461.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi86 – 9510Combined sources
Turni96 – 983Combined sources
Beta strandi99 – 1068Combined sources
Turni107 – 1104Combined sources
Beta strandi113 – 1164Combined sources
Helixi117 – 1193Combined sources
Helixi122 – 13716Combined sources
Helixi141 – 1477Combined sources
Turni148 – 1503Combined sources
Helixi163 – 1708Combined sources
Helixi173 – 1819Combined sources
Beta strandi191 – 1944Combined sources
Helixi197 – 2037Combined sources
Helixi207 – 21610Combined sources
Helixi230 – 23910Combined sources
Helixi246 – 26318Combined sources
Beta strandi267 – 28014Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi286 – 29510Combined sources
Beta strandi297 – 3026Combined sources
Helixi307 – 31711Combined sources
Beta strandi328 – 3303Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi357 – 3615Combined sources
Helixi362 – 3654Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X32NMR-A84-128[»]
1X3PNMR-A320-373[»]
1X3QNMR-A265-319[»]
2HUGNMR-A265-319[»]
3DEOX-ray1.50A85-267[»]
3DEPX-ray2.70A85-267[»]
3UI2X-ray3.18A84-327[»]
ProteinModelPortaliO22265.
SMRiO22265. Positions 46-318, 320-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO22265.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 13552Chromo 1PROSITE-ProRule annotationAdd
BLAST
Repeati136 – 15823ANK 1Add
BLAST
Repeati159 – 18830ANK 2Add
BLAST
Repeati193 – 22230ANK 3Add
BLAST
Repeati242 – 26928ANK 4Add
BLAST
Domaini270 – 32051Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini321 – 37353Chromo 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili57 – 7923Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi79 – 824Poly-Ser
Compositional biasi366 – 3694Poly-Gln

Domaini

The binding to LHCP occurs through the first ankyrin repeat and the L18 domain of LHCP.
Homodimerization occurs through both the third and the fourth ankyrin repeats.
Chromo domain 1 may act as a negative regulator of GTP hydrolysis by FFC/cpSRP54. It is unnecessary for targeting complex formation but is required for integration into the thylakoid membrane.
Chromo domain 2 is involved in binding to the M domain of FFC/cpSRP54.

Sequence similaritiesi

Contains 4 ANK repeats.PROSITE-ProRule annotation
Contains 3 chromo domains.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Transit peptide

Phylogenomic databases

eggNOGiNOG268128.
HOGENOMiHOG000239692.
KOiK12271.
OMAiMEYLIEW.
PhylomeDBiO22265.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF00385. Chromo. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
SM00298. CHROMO. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF54160. SSF54160. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O22265-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQKVFLAMDT CALVIHQSLS RIKLSPPKSS SSSSSAFSPE SLPIRRIELC
60 70 80 90 100
FRGAICAAVQ RNYEETTSSV EEAEEDDESS SSYGEVNKII GSRTAGEGAM
110 120 130 140 150
EYLIEWKDGH SPSWVPSSYI AADVVSEYET PWWTAARKAD EQALSQLLED
160 170 180 190 200
RDVDAVDENG RTALLFVAGL GSDKCVRLLA EAGADLDHRD MRGGLTALHM
210 220 230 240 250
AAGYVRPEVV EALVELGADI EVEDERGLTA LELAREILKT TPKGNPMQFG
260 270 280 290 300
RRIGLEKVIN VLEGQVFEYA EVDEIVEKRG KGKDVEYLVR WKDGGDCEWV
310 320 330 340 350
KGVHVAEDVA KDYEDGLEYA VAESVIGKRV GDDGKTIEYL VKWTDMSDAT
360 370
WEPQDNVDST LVLLYQQQQP MNE
Length:373
Mass (Da):41,279
Last modified:June 1, 2002 - v2
Checksum:iF75ED9C7046A1441
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351S → SSSS in AAD01509. (PubMed:9878634)Curated
Sequence conflicti73 – 731A → V in AAK96775. (PubMed:14593172)Curated
Sequence conflicti73 – 731A → V in AAN72202. (PubMed:14593172)Curated
Sequence conflicti137 – 1371R → K in AAD01509. (PubMed:9878634)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013115 Genomic DNA. Translation: AAD01509.1.
AC002535 Genomic DNA. Translation: AAC62865.2.
CP002685 Genomic DNA. Translation: AEC10842.1.
AY050442 mRNA. Translation: AAK91457.1.
AY054584 mRNA. Translation: AAK96775.1.
AY057532 mRNA. Translation: AAL09772.1.
AY133540 mRNA. Translation: AAM91370.1.
BT002191 mRNA. Translation: AAN72202.1.
PIRiT00439.
RefSeqiNP_566101.1. NM_130313.2.
UniGeneiAt.19748.
At.72297.

Genome annotation databases

EnsemblPlantsiAT2G47450.1; AT2G47450.1; AT2G47450.
GeneIDi819358.
KEGGiath:AT2G47450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013115 Genomic DNA. Translation: AAD01509.1 .
AC002535 Genomic DNA. Translation: AAC62865.2 .
CP002685 Genomic DNA. Translation: AEC10842.1 .
AY050442 mRNA. Translation: AAK91457.1 .
AY054584 mRNA. Translation: AAK96775.1 .
AY057532 mRNA. Translation: AAL09772.1 .
AY133540 mRNA. Translation: AAM91370.1 .
BT002191 mRNA. Translation: AAN72202.1 .
PIRi T00439.
RefSeqi NP_566101.1. NM_130313.2.
UniGenei At.19748.
At.72297.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X32 NMR - A 84-128 [» ]
1X3P NMR - A 320-373 [» ]
1X3Q NMR - A 265-319 [» ]
2HUG NMR - A 265-319 [» ]
3DEO X-ray 1.50 A 85-267 [» ]
3DEP X-ray 2.70 A 85-267 [» ]
3UI2 X-ray 3.18 A 84-327 [» ]
ProteinModelPortali O22265.
SMRi O22265. Positions 46-318, 320-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 4693. 13 interactions.
DIPi DIP-37639N.
IntActi O22265. 19 interactions.
MINTi MINT-126461.

Protein family/group databases

TCDBi 3.A.5.1.2. the general secretory pathway (sec) family.

Proteomic databases

PaxDbi O22265.
PRIDEi O22265.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G47450.1 ; AT2G47450.1 ; AT2G47450 .
GeneIDi 819358.
KEGGi ath:AT2G47450.

Organism-specific databases

GeneFarmi 2589. 230.
TAIRi AT2G47450.

Phylogenomic databases

eggNOGi NOG268128.
HOGENOMi HOG000239692.
KOi K12271.
OMAi MEYLIEW.
PhylomeDBi O22265.

Miscellaneous databases

EvolutionaryTracei O22265.

Gene expression databases

Genevestigatori O22265.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
[Graphical view ]
Pfami PF00023. Ank. 2 hits.
PF00385. Chromo. 1 hit.
[Graphical view ]
SMARTi SM00248. ANK. 3 hits.
SM00298. CHROMO. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF54160. SSF54160. 3 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50013. CHROMO_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A chromodomain protein encoded by the arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting."
    Klimyuk V.I., Persello-Cartieaux F., Havaux M., Contard-David P., Schuenemann D., Meiherhoff K., Gouet P., Jones J.D.G., Hoffman N.E., Nussaume L.
    Plant Cell 11:87-99(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes."
    Tu C.J., Schuenemann D., Hoffman N.E.
    J. Biol. Chem. 274:27219-27224(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH FFC/CPSRP54.
  6. "Functional analysis of the protein-interacting domains of chloroplast SRP43."
    Jonas-Straube E., Hutin C., Hoffman N.E., Schuenemann D.
    J. Biol. Chem. 276:24654-24660(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, SUBUNIT, BINDING TO LIGHT-HARVESTING CHLOROPHYLL PROTEINS AND TO FFC/CPSRP54.
  7. "Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43."
    Goforth R.L., Peterson E.C., Yuan J., Moore M.J., Kight A.D., Lohse M.B., Sakon J., Henry R.L.
    J. Biol. Chem. 279:43077-43084(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FFC/CPSRP54.
  8. "Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an inability to increase iron deficiency-inducible root Fe(III) chelate reductase activity."
    Durrett T.P., Connolly E.L., Rogers E.E.
    Plant J. 47:467-479(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Canonical signal recognition particle components can be bypassed for posttranslational protein targeting in chloroplasts."
    Tzvetkova-Chevolleau T., Hutin C., Noel L.D., Goforth R., Carde J.P., Caffarri S., Sinning I., Groves M., Teulon J.M., Hoffman N.E., Henry R., Havaux M., Nussaume L.
    Plant Cell 19:1635-1648(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ALB3.
  10. "Interplay between the cpSRP pathway components, the substrate LHCP and the translocase Alb3: an in vivo and in vitro study."
    Bals T., Duenschede B., Funke S., Schuenemann D.
    FEBS Lett. 584:4138-4144(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALB3; FFC/CPSRP54; CPFTSY AND LHCP.
  11. "The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane."
    Falk S., Ravaud S., Koch J., Sinning I.
    J. Biol. Chem. 285:5954-5962(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALB3 AND FFC/CPSRP54, MUTAGENESIS OF TYR-269; TRP-291 AND ASP-293.
  12. "cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins."
    Falk S., Sinning I.
    J. Biol. Chem. 285:21655-21661(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway."
    Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.
    Nat. Commun. 2:277-277(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LTD.
  14. Cited for: STRUCTURE BY NMR OF 84-128 AND 265-373, INTERACTION WITH FFC/CPSRP54.
  15. "Assembly of chloroplast signal recognition particle involves structural rearrangement in cpSRP43."
    Kathir K.M., Rajalingam D., Sivaraja V., Kight A., Goforth R.L., Yu C., Henry R., Kumar T.K.
    J. Mol. Biol. 381:49-60(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 265-319.
  16. "Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43."
    Stengel K.F., Holdermann I., Cain P., Robinson C., Wild K., Sinning I.
    Science 321:253-256(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 85-267 IN COMPLEX WITH THE L18 DOMAIN OF LHCP, MUTAGENESIS OF ARG-161; ARG-192; TYR-204 AND ARG-226.

Entry informationi

Entry nameiSR43C_ARATH
AccessioniPrimary (citable) accession number: O22265
Secondary accession number(s): Q93V50, Q940I7, Q9SAU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Unlike eukaryotic or prokaryotic signal recognition particle (SRP), the chloroplast SRP from higher plants lacks an SRP-RNA component. It targets both chloroplast-encoded and nucleus-encoded substrates to the thylakoid membrane, post-translationally for the nucleus-encoded proteins and co-translationally for the chloroplast-encoded proteins.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3