LHCA6_ARATH
ID LHCA6_ARATH Reviewed; 270 AA.
AC Q8LCQ4; Q43382; Q84WT1; Q9LMB1;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Photosystem I chlorophyll a/b-binding protein 6, chloroplastic {ECO:0000303|PubMed:10366881};
DE AltName: Full=LHCI type III LHCA6 {ECO:0000305};
DE Flags: Precursor;
GN Name=LHCA6 {ECO:0000303|PubMed:10366881};
GN OrderedLocusNames=At1g19150 {ECO:0000312|Araport:AT1G19150};
GN ORFNames=T29M8.2 {ECO:0000312|EMBL:AAF82226.1};
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:AAM63464.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8049378; DOI=10.1007/bf00043883;
RA Zhang H., Wang J., Goodman H.M.;
RT "Differential expression in Arabidopsis of Lhca2, a PSI cab gene.";
RL Plant Mol. Biol. 25:551-557(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].
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=19903870; DOI=10.1105/tpc.109.068791;
RA Peng L., Fukao Y., Fujiwara M., Takami T., Shikanai T.;
RT "Efficient operation of NAD(P)H dehydrogenase requires supercomplex
RT formation with photosystem I via minor LHCI in Arabidopsis.";
RL Plant Cell 21:3623-3640(2009).
RN [9]
RP REVIEW ON NDH-PSI SUPERCOMPLEX.
RX PubMed=21785130; DOI=10.1093/pcp/pcr098;
RA Ifuku K., Endo T., Shikanai T., Aro E.M.;
RT "Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature
RT for nuclear-encoded subunits.";
RL Plant Cell Physiol. 52:1560-1568(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21278308; DOI=10.1104/pp.110.171264;
RA Peng L., Shikanai T.;
RT "Supercomplex formation with photosystem I is required for the
RT stabilization of the chloroplast NADH dehydrogenase-like complex in
RT Arabidopsis.";
RL Plant Physiol. 155:1629-1639(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. Seems involved in the function of
CC the photosystem I in low light conditions, when other LHCA proteins are
CC less abundant. Required, together with LHCA5, for the formation of a
CC full-size NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI)
CC that triggers cyclic and chlororespiratory electron transport in
CC chloroplast thylakoids, especially under stress conditions (e.g.
CC increased light intensity). {ECO:0000269|PubMed:19903870,
CC ECO:0000269|PubMed:21278308, ECO:0000305|PubMed:21785130}.
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:0000250|UniProtKB:Q9C639};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins
CC (PubMed:19903870). Homodimer. Binds pigments (By similarity). Element
CC of the NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI)
CC (PubMed:19903870). {ECO:0000250|UniProtKB:Q9C639,
CC ECO:0000269|PubMed:19903870}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250|UniProtKB:Q9C639}; Multi-pass membrane protein
CC {ECO:0000255}.
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 {ECO:0000250|UniProtKB:Q9C639}.
CC -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC residues. {ECO:0000250|UniProtKB:P12333}.
CC -!- DISRUPTION PHENOTYPE: Slightly lower NDH activity in immature leaves.
CC No chlorophyll fluorescence increase in mature leaves. Smaller version
CC of the NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI)
CC supercomplex (PubMed:19903870). In the double mutant lhca5 lhca6,
CC drastic reduction of NDH subunits accumulation upon increased light
CC intensity (PubMed:21278308). {ECO:0000269|PubMed:19903870,
CC ECO:0000269|PubMed:21278308}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF82226.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U03395; AAA57542.1; -; mRNA.
DR EMBL; AC069143; AAF82226.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29811.1; -; Genomic_DNA.
DR EMBL; BT002807; AAO22627.1; -; mRNA.
DR EMBL; BT020322; AAV85677.1; -; mRNA.
DR EMBL; BT020554; AAW70400.1; -; mRNA.
DR EMBL; AY086461; AAM63464.1; -; mRNA.
DR PIR; H86324; H86324.
DR PIR; S46295; S46295.
DR RefSeq; NP_173349.1; NM_101773.3.
DR PDB; 7WFD; EM; 3.25 A; A6=1-270.
DR PDB; 7WG5; EM; 3.89 A; A6=1-270.
DR PDBsum; 7WFD; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q8LCQ4; -.
DR SMR; Q8LCQ4; -.
DR STRING; 3702.AT1G19150.1; -.
DR iPTMnet; Q8LCQ4; -.
DR PaxDb; Q8LCQ4; -.
DR PRIDE; Q8LCQ4; -.
DR ProteomicsDB; 238491; -.
DR DNASU; 838498; -.
DR EnsemblPlants; AT1G19150.1; AT1G19150.1; AT1G19150.
DR GeneID; 838498; -.
DR Gramene; AT1G19150.1; AT1G19150.1; AT1G19150.
DR KEGG; ath:AT1G19150; -.
DR Araport; AT1G19150; -.
DR TAIR; locus:2202150; AT1G19150.
DR eggNOG; ENOG502QVPT; Eukaryota.
DR HOGENOM; CLU_057943_6_1_1; -.
DR InParanoid; Q8LCQ4; -.
DR OMA; YPHKVNP; -.
DR OrthoDB; 991539at2759; -.
DR PhylomeDB; Q8LCQ4; -.
DR PRO; PR:Q8LCQ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LCQ4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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..33
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT CHAIN 34..270
FT /note="Photosystem I chlorophyll a/b-binding protein 6,
FT chloroplastic"
FT /id="PRO_0000435450"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
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 88
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 107
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 112
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 165
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 168
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 221
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 222
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 225
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 227
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 239
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 254
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 21
FT /note="Q -> K (in Ref. 4; AAO22627)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="H -> HV (in Ref. 1; AAA57542)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..76
FT /note="LWFPGSSPPE -> YGSLVALHLN (in Ref. 1; AAA57542)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="L -> F (in Ref. 1; AAA57542)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> A (in Ref. 1; AAA57542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29939 MW; AFB9776316B8D5A6 CRC64;
MAFAIASALT STLTLSTSRV QNPTQRRPHV ASTSSTGGRL MRERLVVVRA GKEVSSVCEP
LPPDRPLWFP GSSPPEWLDG SLPGDFGFDP LGLGSDPDTL KWFAQAELIH SRWAMLAVTG
IIIPECLERL GFIENFSWYD AGSREYFADS TTLFVAQMVL MGWAEGRRWA DLIKPGSVDI
EPKYPHKVNP KPDVGYPGGL WFDFMMWGRG SPEPVMVLRT KEIKNGRLAM LAFLGFCFQA
TYTSQDPIEN LMAHLADPGH CNVFSAFTSH
