LHCA2_ARATH
ID LHCA2_ARATH Reviewed; 257 AA.
AC Q9SYW8; Q9M320;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Photosystem I chlorophyll a/b-binding protein 2, chloroplastic {ECO:0000303|PubMed:10366881};
DE Short=Lhca2 {ECO:0000303|PubMed:10366881};
DE AltName: Full=LHCI type III LHCA2 {ECO:0000305};
DE Flags: Precursor;
GN Name=LHCA2 {ECO:0000303|PubMed:10366881};
GN OrderedLocusNames=At3g61470 {ECO:0000312|Araport:AT3G61470};
GN ORFNames=F2A19.70 {ECO:0000312|EMBL:CAB71077.1};
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 {ECO:0000312|EMBL:AAD28767.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [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 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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP INTERACTION WITH LHCA3 AND LHCA5.
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 [11]
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 [12]
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 [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.
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, 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:19139095, ECO:0000269|PubMed:21083539};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=~695 nm;
CC Note=Emission maxima at 702 nm. {ECO:0000269|PubMed:11553743};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins
CC (PubMed:19139095). Red-emitting heterodimers with LHCA3 and LHCA5
CC (PubMed:17107674, PubMed:21083539, PubMed:15356385). Binds to
CC carotenoids (PubMed:17326666). {ECO:0000269|PubMed:15356385,
CC ECO:0000269|PubMed:17107674, ECO:0000269|PubMed:17326666,
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 -!- 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: Depletion of LHCA3 levels (at protein level).
CC {ECO:0000269|PubMed:11553743}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; AF134120; AAD28767.1; -; mRNA.
DR EMBL; AL132962; CAB71077.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80209.1; -; Genomic_DNA.
DR EMBL; AY054670; AAK96861.1; -; mRNA.
DR EMBL; AY065429; AAL38870.1; -; mRNA.
DR EMBL; AY072483; AAL66898.1; -; mRNA.
DR EMBL; BT002070; AAN72081.1; -; mRNA.
DR PIR; T47939; T47939.
DR PIR; T50550; T50550.
DR RefSeq; NP_191706.2; NM_116012.5.
DR PDB; 7WFE; EM; 3.25 A; B2=1-257.
DR PDB; 7WG5; EM; 3.89 A; B2=1-257.
DR PDBsum; 7WFE; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9SYW8; -.
DR SMR; Q9SYW8; -.
DR STRING; 3702.AT3G61470.1; -.
DR TCDB; 5.B.4.1.1; the plant photosystem i supercomplex (psi) family.
DR iPTMnet; Q9SYW8; -.
DR PaxDb; Q9SYW8; -.
DR PRIDE; Q9SYW8; -.
DR ProteomicsDB; 238465; -.
DR EnsemblPlants; AT3G61470.1; AT3G61470.1; AT3G61470.
DR GeneID; 825320; -.
DR Gramene; AT3G61470.1; AT3G61470.1; AT3G61470.
DR KEGG; ath:AT3G61470; -.
DR Araport; AT3G61470; -.
DR TAIR; locus:2082767; AT3G61470.
DR eggNOG; ENOG502SBWS; Eukaryota.
DR HOGENOM; CLU_057943_6_0_1; -.
DR InParanoid; Q9SYW8; -.
DR OMA; CEMATAK; -.
DR OrthoDB; 991539at2759; -.
DR PhylomeDB; Q9SYW8; -.
DR PRO; PR:Q9SYW8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SYW8; 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: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; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Photosynthesis; Photosystem I; Plastid; Reference proteome;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT CHAIN 44..257
FT /note="Photosystem I chlorophyll a/b-binding protein 2,
FT chloroplastic"
FT /id="PRO_0000435447"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 55
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 75
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 81
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 94
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 99
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 152
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 155
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 208
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 209
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 212
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 214
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 226
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 241
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 CONFLICT 39
FT /note="P -> Q (in Ref. 2; CAB71077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 27755 MW; 208A86988298428E CRC64;
MASSLCASSA IAAISSPSFL GGKKLRLKKK LTVPAVSRPD ASVRAVAADP DRPIWFPGST
PPEWLDGSLP GDFGFDPLGL SSDPDSLKWN VQAEIVHCRW AMLGAAGIFI PEFLTKIGIL
NTPSWYTAGE QEYFTDKTTL FVVELILIGW AEGRRWADII KPGSVNTDPV FPNNKLTGTD
VGYPGGLWFD PLGWGSGSPA KLKELRTKEI KNGRLAMLAV MGAWFQHIYT GTGPIDNLFA
HLADPGHATI FAAFTPK
