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Signal recognition particle 43 kDa protein, chloroplastic (Chromo protein SRP43) (CpSRP43)

 SR43C_ARATH             Reviewed;         373 AA.
O22265; Q93V50; Q940I7; Q9SAU3;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 2.
10-OCT-2018, entry version 153.
RecName: Full=Signal recognition particle 43 kDa protein, chloroplastic;
AltName: Full=Chromo protein SRP43;
Short=CpSRP43;
Flags: Precursor;
Name=CAO; Synonyms=CPSRP43; OrderedLocusNames=At2g47450;
ORFNames=T30B22.25;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta;
PubMed=9878634; DOI=10.1105/tpc.11.1.87;
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.;
"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.";
Plant Cell 11:87-99(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
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., 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.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, SUBUNIT, AND INTERACTION WITH FFC/CPSRP54.
PubMed=10480939; DOI=10.1074/jbc.274.38.27219;
Tu C.J., Schuenemann D., Hoffman N.E.;
"Chloroplast FtsY, chloroplast signal recognition particle, and GTP
are required to reconstitute the soluble phase of light-harvesting
chlorophyll protein transport into thylakoid membranes.";
J. Biol. Chem. 274:27219-27224(1999).
[6]
CHARACTERIZATION, SUBUNIT, AND BINDING TO LIGHT-HARVESTING CHLOROPHYLL
PROTEINS AND TO FFC/CPSRP54.
PubMed=11306572; DOI=10.1074/jbc.M100153200;
Jonas-Straube E., Hutin C., Hoffman N.E., Schuenemann D.;
"Functional analysis of the protein-interacting domains of chloroplast
SRP43.";
J. Biol. Chem. 276:24654-24660(2001).
[7]
FUNCTION, AND INTERACTION WITH FFC/CPSRP54.
PubMed=15292240; DOI=10.1074/jbc.M401600200;
Goforth R.L., Peterson E.C., Yuan J., Moore M.J., Kight A.D.,
Lohse M.B., Sakon J., Henry R.L.;
"Regulation of the GTPase cycle in post-translational signal
recognition particle-based protein targeting involves cpSRP43.";
J. Biol. Chem. 279:43077-43084(2004).
[8]
TISSUE SPECIFICITY.
PubMed=16813577; DOI=10.1111/j.1365-313X.2006.02803.x;
Durrett T.P., Connolly E.L., Rogers E.E.;
"Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an
inability to increase iron deficiency-inducible root Fe(III) chelate
reductase activity.";
Plant J. 47:467-479(2006).
[9]
FUNCTION, AND INTERACTION WITH ALB3.
PubMed=17513500; DOI=10.1105/tpc.106.048959;
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.;
"Canonical signal recognition particle components can be bypassed for
posttranslational protein targeting in chloroplasts.";
Plant Cell 19:1635-1648(2007).
[10]
INTERACTION WITH ALB3; FFC/CPSRP54; CPFTSY AND LHCP.
PubMed=20828566; DOI=10.1016/j.febslet.2010.08.053;
Bals T., Duenschede B., Funke S., Schuenemann D.;
"Interplay between the cpSRP pathway components, the substrate LHCP
and the translocase Alb3: an in vivo and in vitro study.";
FEBS Lett. 584:4138-4144(2010).
[11]
INTERACTION WITH ALB3 AND FFC/CPSRP54, AND MUTAGENESIS OF TYR-269;
TRP-291 AND ASP-293.
PubMed=20018841; DOI=10.1074/jbc.M109.084996;
Falk S., Ravaud S., Koch J., Sinning I.;
"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the
thylakoid membrane.";
J. Biol. Chem. 285:5954-5962(2010).
[12]
FUNCTION.
PubMed=20498370; DOI=10.1074/jbc.C110.132746;
Falk S., Sinning I.;
"cpSRP43 is a novel chaperone specific for light-harvesting
chlorophyll a,b-binding proteins.";
J. Biol. Chem. 285:21655-21661(2010).
[13]
INTERACTION WITH LTD.
PubMed=21505433; DOI=10.1038/ncomms1278;
Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C.,
Zhang L.;
"LTD is a protein required for sorting light-harvesting chlorophyll-
binding proteins to the chloroplast SRP pathway.";
Nat. Commun. 2:277-277(2011).
[14]
STRUCTURE BY NMR OF 84-128 AND 265-373, AND INTERACTION WITH
FFC/CPSRP54.
PubMed=16183644; DOI=10.1074/jbc.M507077200;
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.;
"Three-dimensional solution structures of the chromodomains of
cpSRP43.";
J. Biol. Chem. 280:41465-41471(2005).
[15]
STRUCTURE BY NMR OF 265-319.
PubMed=18586266; DOI=10.1016/j.jmb.2008.05.065;
Kathir K.M., Rajalingam D., Sivaraja V., Kight A., Goforth R.L.,
Yu C., Henry R., Kumar T.K.;
"Assembly of chloroplast signal recognition particle involves
structural rearrangement in cpSRP43.";
J. Mol. Biol. 381:49-60(2008).
[16]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 85-267 IN COMPLEX WITH THE
L18 DOMAIN OF LHCP, AND MUTAGENESIS OF ARG-161; ARG-192; TYR-204 AND
ARG-226.
PubMed=18621669; DOI=10.1126/science.1158640;
Stengel K.F., Holdermann I., Cain P., Robinson C., Wild K.,
Sinning I.;
"Structural basis for specific substrate recognition by the
chloroplast signal recognition particle protein cpSRP43.";
Science 321:253-256(2008).
-!- FUNCTION: Component of the chloroplast signal recognition particle
pathway. Required for post-translational targeting of proteins
into the thylakoid 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. {ECO:0000269|PubMed:10480939,
ECO:0000269|PubMed:15292240, ECO:0000269|PubMed:17513500,
ECO:0000269|PubMed:20498370, ECO:0000269|PubMed:9878634}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:10480939, ECO:0000269|PubMed:11306572,
ECO:0000269|PubMed:15292240, ECO:0000269|PubMed:16183644,
ECO:0000269|PubMed:17513500, ECO:0000269|PubMed:18621669,
ECO:0000269|PubMed:20018841, ECO:0000269|PubMed:20828566,
ECO:0000269|PubMed:21505433}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-780656, EBI-780656;
P07371:AB80 (xeno); NbExp=7; IntAct=EBI-780656, EBI-2353186;
Q8LBP4:ALB3; NbExp=10; IntAct=EBI-780656, EBI-1806831;
P27490:CAB8 (xeno); NbExp=4; IntAct=EBI-780656, EBI-8295162;
P37107:FFC; NbExp=21; IntAct=EBI-780656, EBI-780642;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:9878634}.
-!- TISSUE SPECIFICITY: Expressed in leaves. Detected in roots.
{ECO:0000269|PubMed:16813577, ECO:0000269|PubMed:9878634}.
-!- DOMAIN: The binding to LHCP occurs through the first ankyrin
repeat and the L18 domain of LHCP.
-!- DOMAIN: Homodimerization occurs through both the third and the
fourth ankyrin repeats.
-!- DOMAIN: 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.
-!- DOMAIN: Chromo domain 2 is involved in binding to the M domain of
FFC/cpSRP54.
-!- DISRUPTION PHENOTYPE: Plants show a reduced level of the major
light-harvesting chlorophyll a/b-binding proteins (LHCPs).
{ECO:0000269|PubMed:9878634}.
-!- 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.
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EMBL; AF013115; AAD01509.1; -; Genomic_DNA.
EMBL; AC002535; AAC62865.2; -; Genomic_DNA.
EMBL; CP002685; AEC10842.1; -; Genomic_DNA.
EMBL; AY050442; AAK91457.1; -; mRNA.
EMBL; AY054584; AAK96775.1; -; mRNA.
EMBL; AY057532; AAL09772.1; -; mRNA.
EMBL; AY133540; AAM91370.1; -; mRNA.
EMBL; BT002191; AAN72202.1; -; mRNA.
PIR; T00439; T00439.
RefSeq; NP_566101.1; NM_130313.3.
UniGene; At.19748; -.
UniGene; At.72297; -.
PDB; 1X32; NMR; -; A=84-128.
PDB; 1X3P; NMR; -; A=320-373.
PDB; 1X3Q; NMR; -; A=265-319.
PDB; 2HUG; NMR; -; A=265-319.
PDB; 2N88; NMR; -; A=316-373.
PDB; 3DEO; X-ray; 1.50 A; A=85-267.
PDB; 3DEP; X-ray; 2.70 A; A=85-267.
PDB; 3UI2; X-ray; 3.18 A; A=84-327.
PDB; 5E4W; X-ray; 2.80 A; C/D=265-369.
PDB; 5E4X; X-ray; 2.75 A; A=319-368.
PDBsum; 1X32; -.
PDBsum; 1X3P; -.
PDBsum; 1X3Q; -.
PDBsum; 2HUG; -.
PDBsum; 2N88; -.
PDBsum; 3DEO; -.
PDBsum; 3DEP; -.
PDBsum; 3UI2; -.
PDBsum; 5E4W; -.
PDBsum; 5E4X; -.
ProteinModelPortal; O22265; -.
SMR; O22265; -.
BioGrid; 4693; 17.
DIP; DIP-37639N; -.
IntAct; O22265; 22.
MINT; O22265; -.
STRING; 3702.AT2G47450.1; -.
TCDB; 3.A.5.1.2; the general secretory pathway (sec) family.
PaxDb; O22265; -.
PRIDE; O22265; -.
EnsemblPlants; AT2G47450.1; AT2G47450.1; AT2G47450.
GeneID; 819358; -.
Gramene; AT2G47450.1; AT2G47450.1; AT2G47450.
KEGG; ath:AT2G47450; -.
Araport; AT2G47450; -.
TAIR; locus:2062046; AT2G47450.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
HOGENOM; HOG000239692; -.
KO; K12271; -.
OMA; DGHAPSW; -.
OrthoDB; EOG09360GNA; -.
PhylomeDB; O22265; -.
EvolutionaryTrace; O22265; -.
PRO; PR:O22265; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O22265; baseline and differential.
Genevisible; O22265; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0080085; C:signal recognition particle, chloroplast targeting; IEA:InterPro.
GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; IPI:CAFA.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0070208; P:protein heterotrimerization; IMP:CAFA.
GO; GO:0045038; P:protein import into chloroplast thylakoid membrane; TAS:TAIR.
GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
CDD; cd00204; ANK; 1.
CDD; cd00024; CHROMO; 2.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR030300; CPSRP43.
PANTHER; PTHR24128:SF11; PTHR24128:SF11; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00385; Chromo; 1.
SMART; SM00248; ANK; 3.
SMART; SM00298; CHROMO; 3.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF54160; SSF54160; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
PROSITE; PS50013; CHROMO_2; 1.
1: Evidence at protein level;
3D-structure; ANK repeat; Chloroplast; Coiled coil; Complete proteome;
Metal-binding; Plastid; Reference proteome; Repeat; Ribonucleoprotein;
Signal recognition particle; Transit peptide.
TRANSIT 1 56 Chloroplast. {ECO:0000255}.
CHAIN 57 373 Signal recognition particle 43 kDa
protein, chloroplastic.
/FTId=PRO_0000238461.
DOMAIN 84 135 Chromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
REPEAT 136 158 ANK 1.
REPEAT 159 188 ANK 2.
REPEAT 193 222 ANK 3.
REPEAT 242 269 ANK 4.
DOMAIN 270 320 Chromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 321 373 Chromo 3. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
COILED 57 79 {ECO:0000255}.
COMPBIAS 79 82 Poly-Ser.
COMPBIAS 366 369 Poly-Gln.
METAL 232 232 Magnesium.
MUTAGEN 161 161 R->A: Decreased interaction with LHCP.
{ECO:0000269|PubMed:18621669}.
MUTAGEN 192 192 R->A: Decreased interaction with LHCP.
{ECO:0000269|PubMed:18621669}.
MUTAGEN 204 204 Y->A: Loss of interaction with LHCP.
{ECO:0000269|PubMed:18621669}.
MUTAGEN 226 226 R->A: Decreased interaction with LHCP.
{ECO:0000269|PubMed:18621669}.
MUTAGEN 269 269 Y->A: Decreased interaction with ALB3.
{ECO:0000269|PubMed:20018841}.
MUTAGEN 291 291 W->A: Decreased interaction with ALB3.
{ECO:0000269|PubMed:20018841}.
MUTAGEN 293 293 D->A: Decreased interaction with ALB3.
{ECO:0000269|PubMed:20018841}.
CONFLICT 35 35 S -> SSSS (in Ref. 1; AAD01509).
{ECO:0000305}.
CONFLICT 73 73 A -> V (in Ref. 4; AAK96775/AAN72202).
{ECO:0000305}.
CONFLICT 137 137 R -> K (in Ref. 1; AAD01509).
{ECO:0000305}.
STRAND 86 95 {ECO:0000244|PDB:3DEO}.
TURN 96 98 {ECO:0000244|PDB:3DEO}.
STRAND 99 106 {ECO:0000244|PDB:3DEO}.
TURN 107 110 {ECO:0000244|PDB:1X32}.
STRAND 113 116 {ECO:0000244|PDB:3DEO}.
HELIX 117 119 {ECO:0000244|PDB:3DEO}.
HELIX 122 137 {ECO:0000244|PDB:3DEO}.
HELIX 141 147 {ECO:0000244|PDB:3DEO}.
TURN 148 150 {ECO:0000244|PDB:3DEO}.
HELIX 163 170 {ECO:0000244|PDB:3DEO}.
HELIX 173 181 {ECO:0000244|PDB:3DEO}.
STRAND 191 194 {ECO:0000244|PDB:3DEO}.
HELIX 197 203 {ECO:0000244|PDB:3DEO}.
HELIX 207 216 {ECO:0000244|PDB:3DEO}.
HELIX 230 239 {ECO:0000244|PDB:3DEO}.
HELIX 246 263 {ECO:0000244|PDB:3DEO}.
STRAND 268 270 {ECO:0000244|PDB:5E4W}.
STRAND 272 281 {ECO:0000244|PDB:5E4W}.
STRAND 284 294 {ECO:0000244|PDB:5E4W}.
STRAND 297 301 {ECO:0000244|PDB:5E4W}.
HELIX 302 304 {ECO:0000244|PDB:5E4W}.
HELIX 307 314 {ECO:0000244|PDB:5E4W}.
STRAND 317 320 {ECO:0000244|PDB:5E4W}.
STRAND 322 330 {ECO:0000244|PDB:5E4X}.
STRAND 332 334 {ECO:0000244|PDB:1X3P}.
STRAND 337 343 {ECO:0000244|PDB:5E4X}.
STRAND 344 348 {ECO:0000244|PDB:1X3P}.
STRAND 350 353 {ECO:0000244|PDB:5E4W}.
TURN 354 356 {ECO:0000244|PDB:5E4X}.
HELIX 359 367 {ECO:0000244|PDB:5E4X}.
SEQUENCE 373 AA; 41279 MW; F75ED9C7046A1441 CRC64;
MQKVFLAMDT CALVIHQSLS RIKLSPPKSS SSSSSAFSPE SLPIRRIELC FRGAICAAVQ
RNYEETTSSV EEAEEDDESS SSYGEVNKII GSRTAGEGAM EYLIEWKDGH SPSWVPSSYI
AADVVSEYET PWWTAARKAD EQALSQLLED RDVDAVDENG RTALLFVAGL GSDKCVRLLA
EAGADLDHRD MRGGLTALHM AAGYVRPEVV EALVELGADI EVEDERGLTA LELAREILKT
TPKGNPMQFG RRIGLEKVIN VLEGQVFEYA EVDEIVEKRG KGKDVEYLVR WKDGGDCEWV
KGVHVAEDVA KDYEDGLEYA VAESVIGKRV GDDGKTIEYL VKWTDMSDAT WEPQDNVDST
LVLLYQQQQP MNE


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