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O22265 (SR43C_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal recognition particle 43 kDa protein, chloroplastic
Alternative name(s):
Chromo protein SRP43
Short name=CpSRP43
Gene names
Name:CAO
Synonyms:CPSRP43
Ordered Locus Names:At2g47450
ORF Names:T30B22.25
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.7 Ref.9 Ref.12

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14

Subcellular location

Plastidchloroplast stroma Ref.1.

Tissue specificity

Expressed in leaves. Detected in roots. Ref.1 Ref.8

Domain

The binding to LHCP occurs through the first ankyrin repeat and the L18 domain of LHCP. Ref.16

Homodimerization occurs through both the third and the fourth ankyrin repeats. Ref.16

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. Ref.16

Chromo domain 2 is involved in binding to the M domain of FFC/cpSRP54. Ref.16

Disruption phenotype

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

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.

Sequence similarities

Contains 4 ANK repeats.

Contains 3 chromo domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Chloroplast Potential
Chain57 – 373317Signal recognition particle 43 kDa protein, chloroplastic
PRO_0000238461

Regions

Domain84 – 13552Chromo 1
Repeat136 – 15823ANK 1
Repeat159 – 18830ANK 2
Repeat193 – 22230ANK 3
Repeat242 – 26928ANK 4
Domain270 – 32051Chromo 2
Domain321 – 37353Chromo 3
Coiled coil57 – 7923 Potential
Compositional bias79 – 824Poly-Ser
Compositional bias366 – 3694Poly-Gln

Sites

Metal binding2321Magnesium

Experimental info

Mutagenesis1611R → A: Decreased interaction with LHCP. Ref.16
Mutagenesis1921R → A: Decreased interaction with LHCP. Ref.16
Mutagenesis2041Y → A: Loss of interaction with LHCP. Ref.16
Mutagenesis2261R → A: Decreased interaction with LHCP. Ref.16
Mutagenesis2691Y → A: Decreased interaction with ALB3. Ref.11
Mutagenesis2911W → A: Decreased interaction with ALB3. Ref.11
Mutagenesis2931D → A: Decreased interaction with ALB3. Ref.11
Sequence conflict351S → SSSS in AAD01509. Ref.1
Sequence conflict731A → V in AAK96775. Ref.4
Sequence conflict731A → V in AAN72202. Ref.4
Sequence conflict1371R → K in AAD01509. Ref.1

Secondary structure

.............................................. 373
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O22265 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: F75ED9C7046A1441

FASTA37341,279
        10         20         30         40         50         60 
MQKVFLAMDT CALVIHQSLS RIKLSPPKSS SSSSSAFSPE SLPIRRIELC FRGAICAAVQ 

        70         80         90        100        110        120 
RNYEETTSSV EEAEEDDESS SSYGEVNKII GSRTAGEGAM EYLIEWKDGH SPSWVPSSYI 

       130        140        150        160        170        180 
AADVVSEYET PWWTAARKAD EQALSQLLED RDVDAVDENG RTALLFVAGL GSDKCVRLLA 

       190        200        210        220        230        240 
EAGADLDHRD MRGGLTALHM AAGYVRPEVV EALVELGADI EVEDERGLTA LELAREILKT 

       250        260        270        280        290        300 
TPKGNPMQFG RRIGLEKVIN VLEGQVFEYA EVDEIVEKRG KGKDVEYLVR WKDGGDCEWV 

       310        320        330        340        350        360 
KGVHVAEDVA KDYEDGLEYA VAESVIGKRV GDDGKTIEYL VKWTDMSDAT WEPQDNVDST 

       370 
LVLLYQQQQP MNE 

« Hide

References

« Hide 'large scale' references
[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]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Three-dimensional solution structures of the chromodomains of cpSRP43."
Sivaraja V., Kumar T.K.S., Leena P.S.T., Chang A.N., Vidya C., Goforth R.L., Rajalingam D., Arvind K., Ye J.-L., Chou J., Henry R., Yu C.
J. Biol. Chem. 280:41465-41471(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT00439.
RefSeqNP_566101.1. NM_130313.2.
UniGeneAt.19748.
At.72297.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO22265.
SMRO22265. Positions 31-318, 320-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4693. 13 interactions.
DIPDIP-37639N.
IntActO22265. 19 interactions.
MINTMINT-126461.

Protein family/group databases

TCDB3.A.5.1.2. the general secretory pathway (sec) family.

Proteomic databases

PaxDbO22265.
PRIDEO22265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G47450.1; AT2G47450.1; AT2G47450.
GeneID819358.
KEGGath:AT2G47450.

Organism-specific databases

GeneFarm2589. 230.
TAIRAT2G47450.

Phylogenomic databases

eggNOGNOG268128.
HOGENOMHOG000239692.
InParanoidO22265.
KOK12271.
OMAMEYLIEW.
PhylomeDBO22265.

Gene expression databases

GenevestigatorO22265.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
[Graphical view]
PfamPF00023. Ank. 2 hits.
PF00385. Chromo. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 3 hits.
SM00298. CHROMO. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF54160. SSF54160. 3 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50013. CHROMO_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO22265.

Entry information

Entry nameSR43C_ARATH
AccessionPrimary (citable) accession number: O22265
Secondary accession number(s): Q93V50, Q940I7, Q9SAU3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names