CA4_ARATH
ID CA4_ARATH Reviewed; 251 AA.
AC P27521;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Chlorophyll a-b binding protein 4, chloroplastic {ECO:0000303|PubMed:10366881};
DE AltName: Full=LHCI type III CAB-4;
DE Flags: Precursor;
GN Name=LHCA4 {ECO:0000303|PubMed:10366881}; Synonyms=CAB4;
GN OrderedLocusNames=At3g47470; ORFNames=F1P2.20;
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].
RC STRAIN=cv. Columbia;
RX PubMed=16668349; DOI=10.1104/pp.96.4.1387;
RA Zhang H., Hanley S., Goodman H.M.;
RT "Isolation, characterization and chromosomal location of a new cab gene
RT from Arabidopsis thaliana.";
RL Plant Physiol. 96:1387-1388(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10366881; DOI=10.1016/s1360-1385(99)01419-3;
RA Jansson S.;
RT "A guide to the Lhc genes and their relatives in Arabidopsis.";
RL Trends Plant Sci. 4:236-240(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10818090; DOI=10.1074/jbc.m000550200;
RA Jensen P.E., Gilpin M., Knoetzel J., Scheller H.V.;
RT "The PSI-K subunit of photosystem I is involved in the interaction between
RT light-harvesting complex I and the photosystem I reaction center core.";
RL J. Biol. Chem. 275:24701-24708(2000).
RN [8]
RP REVIEW ON PHOTOSYSTEM I ANTENNA.
RX PubMed=12324436; DOI=10.1016/s0006-3495(02)73979-9;
RA Ihalainen J.A., Jensen P.E., Haldrup A., van Stokkum I.H.M.,
RA van Grondelle R., Scheller H.V., Dekker J.P.;
RT "Pigment organization and energy transfer dynamics in isolated photosystem
RT I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K,
RT PSI-L, or PSI-N subunit.";
RL Biophys. J. 83:2190-2201(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [10]
RP INDUCTION BY LIGHT AND COLD.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=15356385; DOI=10.1023/b:plan.0000040813.05224.94;
RA Ganeteg U., Klimmek F., Jansson S.;
RT "Lhca5--an LHC-type protein associated with photosystem I.";
RL Plant Mol. Biol. 54:641-651(2004).
RN [11]
RP COFACTOR.
RX PubMed=15563470; DOI=10.1074/jbc.m411248200;
RA Storf S., Jansson S., Schmid V.H.R.;
RT "Pigment binding, fluorescence properties, and oligomerization behavior of
RT Lhca5, a novel light-harvesting protein.";
RL J. Biol. Chem. 280:5163-5168(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP 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).
RN [13]
RP SUBUNIT, AND COFACTOR.
RC STRAIN=cv. Columbia;
RX PubMed=21083539; DOI=10.1042/bj20101538;
RA Wientjes E., Croce R.;
RT "The light-harvesting complexes of higher-plant Photosystem I: Lhca1/4 and
RT Lhca2/3 form two red-emitting heterodimers.";
RL Biochem. J. 433:477-485(2011).
RN [14]
RP FUNCTION, AND MISCELLANEOUS.
RX PubMed=21806943; DOI=10.1016/j.bpj.2011.06.045;
RA Wientjes E., van Stokkum I.H.M., van Amerongen H., Croce R.;
RT "The role of the individual Lhcas in photosystem I excitation energy
RT trapping.";
RL Biophys. J. 101:745-754(2011).
CC -!- FUNCTION: The light-harvesting complex (LHC) functions as a light
CC receptor, it captures and delivers excitation energy to photosystems
CC with which it is closely associated. {ECO:0000269|PubMed:21806943}.
CC -!- COFACTOR:
CC Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
CC carotenoids such as lutein and neoxanthin.
CC {ECO:0000269|PubMed:15563470, ECO:0000269|PubMed:21083539};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC Red-emitting heterodimer with LHCA1 (PubMed:21083539).
CC {ECO:0000269|PubMed:21083539}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10818090, ECO:0000269|PubMed:12766230}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by low light (LL) but repressed by high light (HL).
CC Inhibited by cold. {ECO:0000269|PubMed:15356385}.
CC -!- DOMAIN: The N-terminus of the protein extends into the stroma where it
CC is involved with adhesion of granal membranes and post-translational
CC modifications; both are believed to mediate the distribution of
CC excitation energy between photosystems I and II.
CC -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC residues. {ECO:0000250}.
CC -!- MISCELLANEOUS: Light emission at 715-720 nm upon excitation at 440 and
CC 475 nm, and subsequent transfer of excitation energy to the photosystem
CC I core with a relative slow rate of 25 nsec(-1).
CC {ECO:0000269|PubMed:21806943}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; M63931; AAA32760.1; -; mRNA.
DR EMBL; AL132955; CAB61973.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78285.1; -; Genomic_DNA.
DR EMBL; AY093080; AAM13079.1; -; mRNA.
DR EMBL; BT000093; AAN15412.1; -; mRNA.
DR EMBL; AY086470; AAM63472.1; -; mRNA.
DR PIR; T45707; T45707.
DR RefSeq; NP_190331.3; NM_114615.4.
DR PDB; 7WFD; EM; 3.25 A; A4=1-251.
DR PDB; 7WG5; EM; 3.89 A; A4=1-251.
DR PDBsum; 7WFD; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; P27521; -.
DR SMR; P27521; -.
DR BioGRID; 9221; 38.
DR STRING; 3702.AT3G47470.1; -.
DR iPTMnet; P27521; -.
DR PaxDb; P27521; -.
DR PRIDE; P27521; -.
DR ProteomicsDB; 223854; -.
DR EnsemblPlants; AT3G47470.1; AT3G47470.1; AT3G47470.
DR GeneID; 823901; -.
DR Gramene; AT3G47470.1; AT3G47470.1; AT3G47470.
DR KEGG; ath:AT3G47470; -.
DR Araport; AT3G47470; -.
DR TAIR; locus:2079117; AT3G47470.
DR eggNOG; ENOG502QSBP; Eukaryota.
DR HOGENOM; CLU_057943_6_0_1; -.
DR InParanoid; P27521; -.
DR OMA; LPQHECG; -.
DR OrthoDB; 1055775at2759; -.
DR PhylomeDB; P27521; -.
DR PRO; PR:P27521; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P27521; baseline and differential.
DR Genevisible; P27521; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR GO; GO:0009645; P:response to low light intensity stimulus; IEP:UniProtKB.
DR InterPro; IPR001344; Chloro_AB-bd_pln.
DR InterPro; IPR022796; Chloroa_b-bind.
DR PANTHER; PTHR21649; PTHR21649; 1.
DR Pfam; PF00504; Chloroa_b-bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll; Chloroplast; Chromophore; Magnesium; Membrane;
KW Metal-binding; Phosphoprotein; Photosynthesis; Photosystem I; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..251
FT /note="Chlorophyll a-b binding protein 4, chloroplastic"
FT /id="PRO_0000003649"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 57
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="4"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 251 AA; 27734 MW; DC8B390C2AED9D22 CRC64;
MATVTTHASA SIFRPCTSKP RFLTGSSGRL NRDLSFTSIG SSAKTSSFKV EAKKGEWLPG
LASPDYLTGS LAGDNGFDPL GLAEDPENLK WFVQAELVNG RWAMLGVAGM LLPEVFTKIG
IINVPEWYDA GKEQYFASSS TLFVIEFILF HYVEIRRWQD IKNPGSVNQD PIFKQYSLPK
GEVGYPGGIF NPLNFAPTQE AKEKELANGR LAMLAFLGFV VQHNVTGKGP FENLLQHLSD
PWHNTIVQTF N
