Q01667 (CAB6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chlorophyll a-b binding protein 6, chloroplastic

Alternative name(s):
LHCI-730
LHCII type III CAB-6
Light-harvesting complex protein Lhca1

Gene names

Name:	LHCA1
Synonyms:	CAB6
Ordered Locus Names:	At3g54890
ORF Names:	F28P10.130

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Cofactor	Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin By similarity.
Subunit structure	The LHC complex consists of chlorophyll a-b binding proteins. Heterodimer with LHCA4.
Subcellular location	Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein.
Domain	The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Post-translational modification	Photoregulated by reversible phosphorylation of its threonine residues By similarity.
Sequence similarities	Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.

Ontologies

Keywords
Biological process	Photosynthesis
Cellular component	Chloroplast Membrane Photosystem I Photosystem II Plastid Thylakoid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	Chlorophyll Chromophore Magnesium Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	photosynthesis, light harvesting in photosystem I Inferred from mutant phenotype PubMed 16098971. Source: TAIR protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW response to blue light Inferred from expression pattern PubMed 18820083. Source: TAIR response to far red light Inferred from expression pattern PubMed 18820083. Source: TAIR response to red light Inferred from expression pattern PubMed 18820083. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR chloroplast envelope Inferred from direct assay PubMed 12766230. Source: TAIR chloroplast thylakoid Inferred from direct assay PubMed 20061580. Source: TAIR chloroplast thylakoid membrane Inferred from direct assay PubMed 14729914PubMed 15322131. Source: TAIR integral component of membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay PubMed 17432890. Source: TAIR photosystem I Inferred from electronic annotation. Source: UniProtKB-KW photosystem II Inferred from electronic annotation. Source: UniProtKB-KW plastoglobule Inferred from direct assay PubMed 16414959. Source: TAIR thylakoid Inferred from direct assay PubMed 18633119. Source: TAIR
Molecular_function	chlorophyll binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q01667-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

35

Chloroplast Potential

Chain

36 – 241

206

Chlorophyll a-b binding protein 6, chloroplastic

PRO_0000401362

Regions

Transmembrane

93 – 113

21

Helical; Potential

Transmembrane

132 – 152

21

Helical; Potential

Transmembrane

197 – 217

21

Helical; Potential

Sites

Metal binding

48

1

Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygen By similarity

Metal binding

87

1

Magnesium (chlorophyll-a 1 axial ligand) By similarity

Metal binding

90

1

Magnesium (chlorophyll-a 2 axial ligand) By similarity

Metal binding

133

1

Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygen By similarity

Metal binding

153

1

Magnesium (chlorophyll-b 3 axial ligand) By similarity

Metal binding

191

1

Magnesium (chlorophyll-a 3 axial ligand) By similarity

Metal binding

194

1

Magnesium (chlorophyll-a 4 axial ligand) By similarity

Metal binding

208

1

Magnesium (chlorophyll-a 5 axial ligand) By similarity

Metal binding

224

1

Magnesium (chlorophyll-a 6 axial ligand) By similarity

Binding site

68

1

Chlorophyll-a 1; via amide nitrogen By similarity

Binding site

92

1

Chlorophyll-b 2 By similarity

Binding site

129

1

Chlorophyll-a 3; via amide nitrogen By similarity

Binding site

156

1

Chlorophyll-b 4 By similarity

Binding site

190

1

Chlorophyll-a 5 By similarity

Binding site

196

1

Chlorophyll-a 1 By similarity

Experimental info

Sequence conflict

11

1

I → K in AAG40043. Ref.4

Sequence conflict

43

1

R → K in AAG40043. Ref.4

Secondary structure

1

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241

Helix Strand Turn

Details...

Beta strand

51 – 53

3

Beta strand

67 – 69

3

Turn

71 – 78

8

Helix

79 – 82

4

Helix

84 – 94

11

Turn

95 – 97

3

Helix

98 – 100

3

Beta strand

101 – 103

3

Beta strand

119 – 121

3

Beta strand

129 – 131

3

Beta strand

133 – 137

5

Helix

138 – 148

11

Helix

150 – 156

7

Beta strand

160 – 163

4

Beta strand

165 – 167

3

Beta strand

174 – 176

3

Beta strand

180 – 183

4

Helix

191 – 203

13

Helix

205 – 209

5

Beta strand

210 – 212

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 2F5EE06B55A979CE	FASTA	241	25,996
	10 20 30 40 50 60 MASNSLMSCG IAAVYPSLLS SSKSKFVSAG VPLPNAGNVG RIRMAAHWMP GEPRPAYLDG 70 80 90 100 110 120 SAPGDFGFDP LGLGEVPANL ERYKESELIH CRWAMLAVPG ILVPEALGYG NWVKAQEWAA 130 140 150 160 170 180 LPGGQATYLG NPVPWGTLPT ILAIEFLAIA FVEHQRSMEK DPEKKKYPGG AFDPLGYSKD 190 200 210 220 230 240 PKKLEELKVK EIKNGRLALL AFVGFCVQQS AYPGTGPLEN LATHLADPWH NNIGDIVIPF N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a single-copy gene encoding a type I chlorophyll a/b-binding polypeptide of photosystem I in Arabidopsis thaliana." Jensen P.E., Kristensen M., Lehmbeck J., Hoff T., Stummann B.M., Henningsen K.W. Physiol. Plantarum 84:561-567(1992) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-241. Strain: cv. Columbia.
[6]	"The structure of a plant photosystem I supercomplex at 3.4 A resolution." Amunts A., Drory O., Nelson N. Nature 447:58-63(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 49-235.
[7]	"Structure determination and improved model of plant photosystem I." Amunts A., Toporik H., Borovikova A., Nelson N. J. Biol. Chem. 285:3478-3486(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85150 Genomic DNA. Translation: AAA32759.1.
X56062 mRNA. Translation: CAA39534.1.
AL049655 Genomic DNA. Translation: CAB41095.1.
CP002686 Genomic DNA. Translation: AEE79306.1.
AF324692 mRNA. Translation: AAG40043.2.
AF325016 mRNA. Translation: AAG40368.1.
AF326866 mRNA. Translation: AAG41448.1.
AF339688 mRNA. Translation: AAK00370.1.
AF361847 mRNA. Translation: AAK32859.1.
AY070473 mRNA. Translation: AAL49939.1.
AY094437 mRNA. Translation: AAM19809.1.
BT000852 mRNA. Translation: AAN38689.1.
AK317555 mRNA. Translation: BAH20219.1.

PIR

S25435.

RefSeq

NP_191049.1. NM_115346.3. [Q01667-1]

UniGene

At.23982.
At.67867.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O01	X-ray	3.40	1	49-235	[»]
2WSC	X-ray	3.30	1	1-241	[»]
2WSE	X-ray	3.49	1	1-241	[»]
2WSF	X-ray	3.48	1	1-241	[»]

ProteinModelPortal

Q01667.

SMR

Q01667. Positions 61-230.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

DIP

DIP-59003N.

STRING

3702.AT3G54890.1-P.

Proteomic databases

PaxDb

Q01667.

PRIDE

Q01667.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G54890.1; AT3G54890.1; AT3G54890. [Q01667-1]

GeneID

824654.

KEGG

ath:AT3G54890.

Organism-specific databases

TAIR

AT3G54890.

Phylogenomic databases

eggNOG

NOG263751.

HOGENOM

HOG000238033.

InParanoid

Q01667.

KO

K08907.

OMA

MASNSLM.

PhylomeDB

Q01667.

Gene expression databases

ArrayExpress

Q01667.

Genevestigator

Q01667.

Family and domain databases

Gene3D

1.10.3460.10. 1 hit.

InterPro

IPR001344. Chloro_AB-bd_pln.
IPR022796. Chloroa_b-bind.
IPR023329. Chlorophyll_a/b-bd_dom.
[Graphical view]

PANTHER

PTHR21649. PTHR21649. 1 hit.

Pfam

PF00504. Chloroa_b-bind. 1 hit.
[Graphical view]

SUPFAM

SSF103511. SSF103511. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q01667.

Entry information

Entry name

CAB6_ARATH

Accession

Primary (citable) accession number: Q01667
Secondary accession number(s): B9DHK2, Q9C5R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 30, 2010
Last sequence update:	November 1, 1996
Last modified:	May 14, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program