(data stored in ACNUC13479 zone)

SWISSPROT: CB4A_ARATH

ID   CB4A_ARATH              Reviewed;         290 AA.
AC   Q07473; Q8RWN1; Q94AD5; Q94K17;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   30-AUG-2017, entry version 136.
DE   RecName: Full=Chlorophyll a-b binding protein CP29.1, chloroplastic;
DE   AltName: Full=LHCB4.1;
DE   AltName: Full=LHCII protein 4.1;
DE   Flags: Precursor;
GN   Name=LHCB4.1; OrderedLocusNames=At5g01530; ORFNames=F7A7_50;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=8290636; DOI=10.1104/pp.103.4.1451;
RA   Green B.R., Pichersky E.;
RT   "Nucleotide sequence of an Arabidopsis thaliana Lhcb4 gene.";
RL   Plant Physiol. 103:1451-1452(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
RA   Andreasson E., Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from
RT   Arabidopsis thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112 AND THR-114, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: The light-harvesting complex (LHC) functions as a light
CC       receptor, it captures and delivers excitation energy to
CC       photosystems with which it is closely associated.
CC   -!- COFACTOR:
CC       Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
CC       carotenoids such as lutein and neoxanthin. {ECO:0000250};
CC   -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Multi-pass membrane protein.
CC   -!- DOMAIN: The N-terminus of the protein extends into the stroma
CC       where it is involved with adhesion of granal membranes and post-
CC       translational modifications; both are believed to mediate the
CC       distribution of excitation energy between photosystems I and II.
CC   -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC       residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-
CC       binding (LHC) protein family. {ECO:0000305}.
DR   EMBL; X71878; CAA50712.1; -; Genomic_DNA.
DR   EMBL; AL161946; CAB82269.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90357.1; -; Genomic_DNA.
DR   EMBL; AF370474; AAK43851.1; -; mRNA.
DR   EMBL; AY048262; AAK82524.1; -; mRNA.
DR   EMBL; AY048300; AAK82562.1; -; mRNA.
DR   EMBL; AY057641; AAL15272.1; -; mRNA.
DR   EMBL; AY059861; AAL24343.1; -; mRNA.
DR   EMBL; AY081680; AAM10242.1; -; mRNA.
DR   EMBL; AY092980; AAM12979.1; -; mRNA.
DR   EMBL; AY133566; AAM91396.1; -; mRNA.
DR   EMBL; BT000363; AAN15682.1; -; mRNA.
DR   PIR; S33443; S33443.
DR   RefSeq; NP_195773.1; NM_120231.4.
DR   UniGene; At.23015; -.
DR   UniGene; At.23659; -.
DR   UniGene; At.23691; -.
DR   UniGene; At.24017; -.
DR   UniGene; At.75201; -.
DR   PDB; 5MDX; EM; 5.30 A; R/r=41-290.
DR   PDBsum; 5MDX; -.
DR   ProteinModelPortal; Q07473; -.
DR   BioGrid; 15604; 6.
DR   IntAct; Q07473; 1.
DR   STRING; 3702.AT5G01530.1; -.
DR   iPTMnet; Q07473; -.
DR   PaxDb; Q07473; -.
DR   PRIDE; Q07473; -.
DR   EnsemblPlants; AT5G01530.1; AT5G01530.1; AT5G01530.
DR   GeneID; 830325; -.
DR   Gramene; AT5G01530.1; AT5G01530.1; AT5G01530.
DR   KEGG; ath:AT5G01530; -.
DR   Araport; AT5G01530; -.
DR   TAIR; locus:2149765; AT5G01530.
DR   eggNOG; ENOG410IEXD; Eukaryota.
DR   eggNOG; ENOG410YYUX; LUCA.
DR   HOGENOM; HOG000238033; -.
DR   InParanoid; Q07473; -.
DR   KO; K08915; -.
DR   OMA; TDRPLWY; -.
DR   OrthoDB; EOG09360J56; -.
DR   PhylomeDB; Q07473; -.
DR   PRO; PR:Q07473; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q07473; baseline and differential.
DR   Genevisible; Q07473; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IBA:GO_Central.
DR   GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0010287; C:plastoglobule; IDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR   GO; GO:0016168; F:chlorophyll binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031409; F:pigment binding; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR   GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0009637; P:response to blue light; IEP:TAIR.
DR   GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR   GO; GO:0010114; P:response to red light; IEP:TAIR.
DR   Gene3D; 1.10.3460.10; -; 1.
DR   InterPro; IPR001344; Chloro_AB-bd_pln.
DR   InterPro; IPR022796; Chloroa_b-bind.
DR   InterPro; IPR023329; Chlorophyll_a/b-bd_dom.
DR   PANTHER; PTHR21649; PTHR21649; 1.
DR   Pfam; PF00504; Chloroa_b-bind; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q07473.
DR   SWISS-2DPAGE; Q07473.
KW   3D-structure; Chlorophyll; Chloroplast; Chromophore;
KW   Complete proteome; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW   Photosynthesis; Photosystem I; Photosystem II; Plastid;
KW   Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT       1     40       Chloroplast. {ECO:0000255}.
FT   CHAIN        41    290       Chlorophyll a-b binding protein CP29.1,
FT                                chloroplastic.
FT                                /FTId=PRO_0000003651.
FT   TRANSMEM    146    166       Helical. {ECO:0000255}.
FT   TRANSMEM    184    204       Helical. {ECO:0000255}.
FT   TRANSMEM    248    268       Helical. {ECO:0000255}.
FT   METAL        58     58       Magnesium (chlorophyll-b 1 axial ligand);
FT                                via carbonyl oxygen. {ECO:0000250}.
FT   METAL       140    140       Magnesium (chlorophyll-a 1 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       143    143       Magnesium (chlorophyll-a 2 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       203    203       Magnesium (chlorophyll-b 3 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       242    242       Magnesium (chlorophyll-a 3 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       245    245       Magnesium (chlorophyll-a 4 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       259    259       Magnesium (chlorophyll-a 5 axial ligand).
FT                                {ECO:0000250}.
FT   METAL       274    274       Magnesium (chlorophyll-a 6 axial ligand).
FT                                {ECO:0000250}.
FT   BINDING      78     78       Chlorophyll-a 1; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     180    180       Chlorophyll-a 3; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     206    206       Chlorophyll-b 4. {ECO:0000250}.
FT   BINDING     247    247       Chlorophyll-a 1. {ECO:0000250}.
FT   MOD_RES     112    112       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19376835}.
FT   MOD_RES     114    114       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19376835}.
FT   CONFLICT     10     12       AAS -> DAA (in Ref. 4; AAK82524).
FT                                {ECO:0000305}.
FT   CONFLICT     34     34       F -> V (in Ref. 4; AAK82524).
FT                                {ECO:0000305}.
FT   CONFLICT     57     57       L -> V (in Ref. 4; AAM12979).
FT                                {ECO:0000305}.
FT   CONFLICT    227    227       G -> S (in Ref. 4; AAK43851/AAN15682).
FT                                {ECO:0000305}.
FT   CONFLICT    268    270       LNN -> RNY (in Ref. 4; AAK82524).
FT                                {ECO:0000305}.
SQ   SEQUENCE   290 AA;  31139 MW;  991C69CF3B773C79 CRC64;
     MAATSAAAAA ASSIMGTRVA PGIHPGSGRF TAVFGFGKKK AAPKKSAKKT VTTDRPLWYP
     GAISPDWLDG SLVGDYGFDP FGLGKPAEYL QFDIDSLDQN LAKNLAGDVI GTRTEAADAK
     STPFQPYSEV FGIQRFRECE LIHGRWAMLA TLGALSVEWL TGVTWQDAGK VELVDGSSYL
     GQPLPFSIST LIWIEVLVIG YIEFQRNAEL DSEKRLYPGG KFFDPLGLAA DPEKTAQLQL
     AEIKHARLAM VAFLGFAVQA AATGKGPLNN WATHLSDPLH TTIIDTFSSS
//

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