LHCA3_ARATH
ID LHCA3_ARATH Reviewed; 273 AA.
AC Q9SY97; Q0WR83; Q2V2R9; Q43381; Q8LCR7;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Photosystem I chlorophyll a/b-binding protein 3-1, chloroplastic {ECO:0000303|PubMed:8115553};
DE Short=Lhca3*1 {ECO:0000303|PubMed:8115553};
DE AltName: Full=LHCI type III LHCA3 {ECO:0000305};
DE Flags: Precursor;
GN Name=LHCA3 {ECO:0000303|PubMed:8115553};
GN OrderedLocusNames=At1g61520 {ECO:0000312|Araport:AT1G61520};
GN ORFNames=T25B24.12 {ECO:0000312|EMBL:AAD25555.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8115553; DOI=10.1104/pp.104.1.297;
RA Wang J., Zhang H., Goodman H.M.;
RT "An Arabidopsis cab gene homologous to Cab-8 of tomato.";
RL Plant Physiol. 104:297-297(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 INTERACTION WITH LHCA5, AND 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
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 [9]
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 [10]
RP DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=11553743; DOI=10.1104/pp.127.1.150;
RA Ganeteg U., Strand A., Gustafsson P., Jansson S.;
RT "The properties of the chlorophyll a/b-binding proteins Lhca2 and Lhca3
RT studied in vivo using antisense inhibition.";
RL Plant Physiol. 127:150-158(2001).
RN [11]
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 [12]
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 [13]
RP MUTAGENESIS OF GLU-100; ASN-103; ARG-105; GLU-159; GLU-167; ARG-170;
RP GLU-225; ASN-228; ARG-230; GLN-242 AND HIS-257.
RX PubMed=16950167; DOI=10.1016/j.bbabio.2006.06.018;
RA Mozzo M., Morosinotto T., Bassi R., Croce R.;
RT "Probing the structure of Lhca3 by mutation analysis.";
RL Biochim. Biophys. Acta 1757:1607-1613(2006).
RN [14]
RP INTERACTION WITH LHCA2.
RC STRAIN=cv. Columbia;
RX PubMed=17107674; DOI=10.1016/j.febslet.2006.10.063;
RA Lucinski R., Schmid V.H., Jansson S., Klimmek F.;
RT "Lhca5 interaction with plant photosystem I.";
RL FEBS Lett. 580:6485-6488(2006).
RN [15]
RP INTERACTION WITH CAROTENOIDS, AND COFACTOR.
RX PubMed=17326666; DOI=10.1021/bi602531k;
RA Croce R., Mozzo M., Morosinotto T., Romeo A., Hienerwadel R., Bassi R.;
RT "Singlet and triplet state transitions of carotenoids in the antenna
RT complexes of higher-plant photosystem I.";
RL Biochemistry 46:3846-3855(2007).
RN [16]
RP COFACTOR, AND SUBUNIT.
RX PubMed=19139095; DOI=10.1074/jbc.m808395200;
RA Wientjes E., Oostergetel G.T., Jansson S., Boekema E.J., Croce R.;
RT "The role of Lhca complexes in the supramolecular organization of higher
RT plant photosystem I.";
RL J. Biol. Chem. 284:7803-7810(2009).
RN [17]
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 [18]
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).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 95-259, SUBUNIT, AND COFACTOR.
RX PubMed=17476261; DOI=10.1038/nature05687;
RA Amunts A., Drory O., Nelson N.;
RT "The structure of a plant photosystem I supercomplex at 3.4 A resolution.";
RL Nature 447:58-63(2007).
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, here photosystem I.
CC {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:17326666,
CC ECO:0000269|PubMed:17476261, ECO:0000269|PubMed:19139095,
CC ECO:0000269|PubMed:21083539};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=~715 nm;
CC Note=Emission maxima at 735 nm. {ECO:0000269|PubMed:11553743};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins
CC (PubMed:19139095, PubMed:17476261). Red-emitting heterodimer with LHCA2
CC (PubMed:17107674, PubMed:21083539). Interacts with LHCA5
CC (PubMed:15356385). Binds to carotenoids (PubMed:17326666).
CC {ECO:0000269|PubMed:15356385, ECO:0000269|PubMed:17107674,
CC ECO:0000269|PubMed:17326666, ECO:0000269|PubMed:17476261,
CC ECO:0000269|PubMed:19139095, ECO:0000269|PubMed:21083539}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10818090}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SY97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SY97-2; Sequence=VSP_058097;
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. {ECO:0000305}.
CC -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC residues. {ECO:0000250|UniProtKB:P12333}.
CC -!- DISRUPTION PHENOTYPE: Slight decrease (30 percent) of LHCA2 levels (at
CC protein level). {ECO:0000269|PubMed:11553743}.
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; U01103; AAA18206.1; -; mRNA.
DR EMBL; AC005850; AAD25555.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33846.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33847.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33848.1; -; Genomic_DNA.
DR EMBL; AY059879; AAL24361.1; -; mRNA.
DR EMBL; AY093370; AAM13369.1; -; mRNA.
DR EMBL; AK228436; BAF00366.1; -; mRNA.
DR EMBL; AY086439; AAM63442.1; -; mRNA.
DR PIR; E96640; E96640.
DR RefSeq; NP_001031217.1; NM_001036140.1. [Q9SY97-2]
DR RefSeq; NP_001185280.1; NM_001198351.1. [Q9SY97-1]
DR RefSeq; NP_176347.1; NM_104833.3. [Q9SY97-1]
DR PDB; 2O01; X-ray; 3.40 A; 3=95-259.
DR PDB; 7WFD; EM; 3.25 A; A3=1-273.
DR PDB; 7WFE; EM; 3.25 A; B3=1-273.
DR PDB; 7WG5; EM; 3.89 A; A3/B3=1-273.
DR PDBsum; 2O01; -.
DR PDBsum; 7WFD; -.
DR PDBsum; 7WFE; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9SY97; -.
DR SMR; Q9SY97; -.
DR STRING; 3702.AT1G61520.1; -.
DR TCDB; 5.B.4.1.1; the plant photosystem i supercomplex (psi) family.
DR iPTMnet; Q9SY97; -.
DR PaxDb; Q9SY97; -.
DR PRIDE; Q9SY97; -.
DR ProMEX; Q9SY97; -.
DR ProteomicsDB; 238466; -. [Q9SY97-1]
DR EnsemblPlants; AT1G61520.1; AT1G61520.1; AT1G61520. [Q9SY97-1]
DR EnsemblPlants; AT1G61520.2; AT1G61520.2; AT1G61520. [Q9SY97-2]
DR EnsemblPlants; AT1G61520.3; AT1G61520.3; AT1G61520. [Q9SY97-1]
DR GeneID; 842446; -.
DR Gramene; AT1G61520.1; AT1G61520.1; AT1G61520. [Q9SY97-1]
DR Gramene; AT1G61520.2; AT1G61520.2; AT1G61520. [Q9SY97-2]
DR Gramene; AT1G61520.3; AT1G61520.3; AT1G61520. [Q9SY97-1]
DR KEGG; ath:AT1G61520; -.
DR Araport; AT1G61520; -.
DR TAIR; locus:2200868; AT1G61520.
DR eggNOG; ENOG502QT09; Eukaryota.
DR InParanoid; Q9SY97; -.
DR OMA; WLAYSEV; -.
DR PhylomeDB; Q9SY97; -.
DR PRO; PR:Q9SY97; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY97; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
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; Alternative splicing; Chlorophyll; Chloroplast; Chromophore;
KW Magnesium; Membrane; Metal-binding; Phosphoprotein; Photosynthesis;
KW Photosystem I; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT CHAIN 40..273
FT /note="Photosystem I chlorophyll a/b-binding protein 3-1,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435448"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 56
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|UniProtKB:P12333"
FT BINDING 76
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 82
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 100
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|UniProtKB:P12333"
FT BINDING 105
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 140
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|UniProtKB:P12333"
FT BINDING 167
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|UniProtKB:P12333"
FT BINDING 170
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 224
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 225
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|UniProtKB:P12333"
FT BINDING 228
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|UniProtKB:P12333"
FT BINDING 230
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 242
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|UniProtKB:P12333"
FT BINDING 257
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|UniProtKB:P12333"
FT BINDING 272
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT VAR_SEQ 1..68
FT /note="MAAQALVSSSLTSSVQTARQIFGSKPVASASQKKSSFVVKAAATPPVKQGAN
FT RPLWFASSQSLSYLDG -> MMFKIWRCSDSSC (in isoform 2)"
FT /id="VSP_058097"
FT MUTAGEN 100
FT /note="E->V: Impaired complex formation with chlorophyll;
FT when associated with L-230."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 103
FT /note="N->F: Reduced chlorophyll-b content in pigment
FT complex."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 105
FT /note="R->L: Impaired complex formation with chlorophyll;
FT when associated with V-225."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 159
FT /note="E->V: Reduced chlorophyll-a content in pigment
FT complex."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 167
FT /note="E->V: Reduced chlorophyll-a and chlorophyll-b
FT content in pigment complex; when associated with L-170."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 170
FT /note="R->L: Reduced chlorophyll-a and chlorophyll-b
FT content in pigment complex; when associated with V-167."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 225
FT /note="E->V: Impaired complex formation with chlorophyll;
FT when associated with L-105."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 228
FT /note="N->V: Reduced chlorophyll-a content in pigment
FT complex."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 230
FT /note="R->L: Impaired complex formation with chlorophyll;
FT when associated with V-100."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 242
FT /note="Q->L: Impaired complex formation with chlorophyll."
FT /evidence="ECO:0000269|PubMed:16950167"
FT MUTAGEN 257
FT /note="H->F: Reduced chlorophyll-a content in pigment
FT complex."
FT /evidence="ECO:0000269|PubMed:16950167"
FT CONFLICT 44
FT /note="T -> A (in Ref. 1; AAA18206)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="F -> V (in Ref. 1; AAA18206)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> G (in Ref. 6; BAF00366)"
FT /evidence="ECO:0000305"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:2O01"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2O01"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:2O01"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:2O01"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2O01"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:2O01"
FT TURN 242..246
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2O01"
SQ SEQUENCE 273 AA; 29181 MW; C7EE634D155274F4 CRC64;
MAAQALVSSS LTSSVQTARQ IFGSKPVASA SQKKSSFVVK AAATPPVKQG ANRPLWFASS
QSLSYLDGSL PGDYGFDPLG LSDPEGTGGF IEPRWLAYGE IINGRFAMLG AAGAIAPEIL
GKAGLIPAET ALPWFQTGVI PPAGTYTYWA DNYTLFVLEM ALMGFAEHRR LQDWYNPGSM
GKQYFLGLEK GLAGSGNPAY PGGPFFNPLG FGKDEKSLKE LKLKEVKNGR LAMLAILGYF
IQGLVTGVGP YQNLLDHLAD PVNNNVLTSL KFH
