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Chlorophyll a-b binding protein 2.2, chloroplastic (Photosystem II light harvesting complex gene 2.2) (Protein LIGHT-HARVESTING CHLOROPHYLL B-BINDING 2.2)

 CB22_ARATH              Reviewed;         265 AA.
Q9S7J7;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 139.
RecName: Full=Chlorophyll a-b binding protein 2.2, chloroplastic {ECO:0000303|PubMed:10366881};
AltName: Full=Photosystem II light harvesting complex gene 2.2 {ECO:0000303|PubMed:10366881};
AltName: Full=Protein LIGHT-HARVESTING CHLOROPHYLL B-BINDING 2.2 {ECO:0000303|PubMed:10366881};
Flags: Precursor;
Name=LHCB2.2 {ECO:0000303|PubMed:10366881};
OrderedLocusNames=At2g05070 {ECO:0000312|Araport:AT2G05070};
ORFNames=F1O13.20 {ECO:0000312|EMBL:AAD25595.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
PubMed=10366881; DOI=10.1016/S1360-1385(99)01419-3;
Jansson S.;
"A guide to the Lhc genes and their relatives in Arabidopsis.";
Trends Plant Sci. 4:236-240(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
DEPHOSPHORYLATION BY PPH1.
PubMed=20176943; DOI=10.1073/pnas.0913810107;
Shapiguzov A., Ingelsson B., Samol I., Andres C., Kessler F.,
Rochaix J.D., Vener A.V., Goldschmidt-Clermont M.;
"The PPH1 phosphatase is specifically involved in LHCII
dephosphorylation and state transitions in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 107:4782-4787(2010).
[6]
INDUCTION BY LOW LIGHT.
STRAIN=cv. Columbia;
PubMed=22236032; DOI=10.1186/1471-2229-12-6;
Mishra Y., Jaenkaenpaeae H.J., Kiss A.Z., Funk C., Schroeder W.P.,
Jansson S.;
"Arabidopsis plants grown in the field and climate chambers
significantly differ in leaf morphology and photosystem components.";
BMC Plant Biol. 12:6-6(2012).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=22143917; DOI=10.1093/jxb/err315;
Xu Y.-H., Liu R., Yan L., Liu Z.-Q., Jiang S.-C., Shen Y.-Y.,
Wang X.-F., Zhang D.-P.;
"Light-harvesting chlorophyll a/b-binding proteins are required for
stomatal response to abscisic acid in Arabidopsis.";
J. Exp. Bot. 63:1095-1106(2012).
[8]
REPRESSION BY DESICCATION; COLD AND HIGH IRRADIANCE.
STRAIN=cv. Columbia;
PubMed=23598180; DOI=10.1016/j.jplph.2013.03.008;
Lucinski R., Jackowski G.;
"AtFtsH heterocomplex-mediated degradation of apoproteins of the major
light harvesting complex of photosystem II (LHCII) in response to
stresses.";
J. Plant Physiol. 170:1082-1089(2013).
[9]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=23995216; DOI=10.1016/j.jphotobiol.2013.07.028;
Nellaepalli S., Kodru S., Malavath T., Subramanyam R.;
"Change in fast Chl a fluorescence transients, 2 dimensional protein
profile and pigment protein interactions during state transitions in
Arabidopsis thaliana.";
J. Photochem. Photobiol. B 128:27-34(2013).
[10]
FUNCTION, PHOSPHORYLATION AT THR-40 BY STN7, AND SUBUNIT.
PubMed=23888908; DOI=10.1111/tpj.12297;
Leoni C., Pietrzykowska M., Kiss A.Z., Suorsa M., Ceci L.R., Aro E.M.,
Jansson S.;
"Very rapid phosphorylation kinetics suggest a unique role for Lhcb2
during state transitions in Arabidopsis.";
Plant J. 76:236-246(2013).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
STRAIN=cv. Columbia;
PubMed=25194026; DOI=10.1105/tpc.114.127373;
Pietrzykowska M., Suorsa M., Semchonok D.A., Tikkanen M.,
Boekema E.J., Aro E.-M., Jansson S.;
"The light-harvesting chlorophyll a/b binding proteins Lhcb1 and Lhcb2
play complementary roles during state transitions in Arabidopsis.";
Plant Cell 26:3646-3660(2014).
[12]
FUNCTION, SUBUNIT, PHOSPHORYLATION BY STN7, AND DEPHOSPHORYLATION BY
PPH1.
STRAIN=cv. Columbia;
PubMed=26392145; DOI=10.1016/j.bbabio.2015.09.005;
Crepin A., Caffarri S.;
"The specific localizations of phosphorylated Lhcb1 and Lhcb2 isoforms
reveal the role of Lhcb2 in the formation of the PSI-LHCII
supercomplex in Arabidopsis during state transitions.";
Biochim. Biophys. Acta 1847:1539-1548(2015).
-!- 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 (By similarity).
Mediates rapid phosphorylation and migration of LHCII-PSII to
photosystem I (PSI) after transition to state 2 (red) light
conditions, thus leading to the formation of PSI-PSII-LHCII and
PSI-LHCII supercomplex to balance the relative excitation of PSI
and PSII (PubMed:23995216, PubMed:23888908, PubMed:25194026,
PubMed:26392145). Involved in the production of reactive oxygen
species (ROS) and stomatal closure upon abscisic acid (ABA)
treatment. Required to prevent water loss (PubMed:22143917).
{ECO:0000250|UniProtKB:P27521, ECO:0000269|PubMed:22143917,
ECO:0000269|PubMed:23888908, ECO:0000269|PubMed:23995216,
ECO:0000269|PubMed:25194026, ECO:0000269|PubMed:26392145}.
-!- COFACTOR:
Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
carotenoids such as lutein and neoxanthin.
{ECO:0000250|UniProtKB:P12333};
-!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding
proteins (By similarity). Component of LHCII trimers made of
LHCB1, LHCB2 and LHCB3 subunits (PubMed:23888908, PubMed:23995216,
PubMed:25194026). Associated with super- (PSI-LHCII and PSII-
LHCII) and mega-complexes (PSI-PSII-LHCII) containing LHCII and
both photosystem (PS)I and PSII, in state 2 (red) light conditions
(PubMed:23995216, PubMed:23888908, PubMed:25194026,
PubMed:26392145). {ECO:0000250|UniProtKB:P12333,
ECO:0000269|PubMed:23888908, ECO:0000269|PubMed:23995216,
ECO:0000269|PubMed:25194026, ECO:0000269|PubMed:26392145}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000269|PubMed:23995216}; Multi-pass membrane protein
{ECO:0000255}.
-!- INDUCTION: Accumulates at stronger levels in low light than in
normal or high light; more expressed in growth chamber conditions
than when grown in the field (PubMed:22236032). Repressed in
leaves exposed to desiccation, cold and high irradiance via a
metalloprotease-dependent proteolytic process (at protein level)
(PubMed:23598180). {ECO:0000269|PubMed:22236032,
ECO:0000269|PubMed:23598180}.
-!- PTM: Photoregulated by reversible but rapid phosphorylation by
STN7 of its threonine residues under state 2 (red) light
conditions (PubMed:23995216, PubMed:23888908, PubMed:26392145).
Dephosphorylated by PPH1 in state 1 (far red) light conditions
(PubMed:20176943, PubMed:23995216, PubMed:23888908,
PubMed:26392145). Phosphorylation triggers the formation of the
PSI-LHCII supercomplex (PubMed:26392145).
{ECO:0000269|PubMed:20176943, ECO:0000269|PubMed:23888908,
ECO:0000269|PubMed:23995216, ECO:0000269|PubMed:26392145}.
-!- DISRUPTION PHENOTYPE: In plants silenced with microRNAs,
functional LHCII thylakoid protein complexes where LHCB2 is
replaced by LHCB1. However these LHCII complexes are impaired in
light state transitions, leading to stunted growth in high light
(PubMed:25194026). Reduced reactive oxygen species (ROS)
production in leaves and impaired stomatal closure in response to
abscisic acid (ABA). Increased water loss and reduced resistance
to drought, probably due to open stomata. Altered expression of
other LHCB members (PubMed:22143917).
{ECO:0000269|PubMed:22143917, ECO:0000269|PubMed:25194026}.
-!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-
binding (LHC) protein family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF134123; AAD28770.1; -; mRNA.
EMBL; AC007211; AAD25595.1; -; Genomic_DNA.
EMBL; CP002685; AEC05893.1; -; Genomic_DNA.
EMBL; AY054218; AAL06878.1; -; mRNA.
EMBL; AY062563; AAL32641.1; -; mRNA.
EMBL; AY066036; AAL47403.1; -; mRNA.
EMBL; AY093372; AAM13371.1; -; mRNA.
PIR; T52324; T52324.
RefSeq; NP_178582.1; NM_126537.4.
UniGene; At.48420; -.
UniGene; At.63397; -.
UniGene; At.72525; -.
ProteinModelPortal; Q9S7J7; -.
SMR; Q9S7J7; -.
IntAct; Q9S7J7; 1.
STRING; 3702.AT2G05070.1; -.
iPTMnet; Q9S7J7; -.
PaxDb; Q9S7J7; -.
PRIDE; Q9S7J7; -.
EnsemblPlants; AT2G05070.1; AT2G05070.1; AT2G05070.
GeneID; 815055; -.
Gramene; AT2G05070.1; AT2G05070.1; AT2G05070.
KEGG; ath:AT2G05070; -.
Araport; AT2G05070; -.
TAIR; locus:2044988; AT2G05070.
eggNOG; ENOG410IU0X; Eukaryota.
eggNOG; ENOG410ZHBU; LUCA.
HOGENOM; HOG000238032; -.
KO; K08913; -.
OMA; GEAIWFK; -.
OrthoDB; EOG09360I0J; -.
PhylomeDB; Q9S7J7; -.
PRO; PR:Q9S7J7; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9S7J7; baseline and differential.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009522; C:photosystem I; IDA:UniProtKB.
GO; GO:0009523; C:photosystem II; IDA:UniProtKB.
GO; GO:0010287; C:plastoglobule; IDA:TAIR.
GO; GO:0009517; C:PSII associated light-harvesting complex II; IDA:UniProtKB.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0016168; F:chlorophyll binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031409; F:pigment binding; IBA:GO_Central.
GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IDA:UniProtKB.
GO; GO:0009769; P:photosynthesis, light harvesting in photosystem II; IDA:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
GO; GO:0009409; P:response to cold; IEP:UniProtKB.
GO; GO:0009269; P:response to desiccation; IEP:UniProtKB.
GO; GO:0010218; P:response to far red light; IDA:UniProtKB.
GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB.
GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
GO; GO:0009645; P:response to low light intensity stimulus; IEP:UniProtKB.
GO; GO:0010114; P:response to red light; IDA:UniProtKB.
GO; GO:0030104; P:water homeostasis; IMP:UniProtKB.
Gene3D; 1.10.3460.10; -; 1.
InterPro; IPR001344; Chloro_AB-bd_pln.
InterPro; IPR022796; Chloroa_b-bind.
InterPro; IPR023329; Chlorophyll_a/b-bd_dom_sf.
PANTHER; PTHR21649; PTHR21649; 1.
Pfam; PF00504; Chloroa_b-bind; 1.
1: Evidence at protein level;
Chlorophyll; Chloroplast; Chromophore; Complete proteome; Magnesium;
Membrane; Metal-binding; Phosphoprotein; Photosynthesis;
Photosystem I; Photosystem II; Plastid; Reference proteome; Thylakoid;
Transit peptide; Transmembrane; Transmembrane helix.
TRANSIT 1 37 Chloroplast.
{ECO:0000250|UniProtKB:P12333}.
CHAIN 38 265 Chlorophyll a-b binding protein 2.2,
chloroplastic.
/FTId=PRO_0000438438.
TRANSMEM 151 171 Helical. {ECO:0000255}.
TRANSMEM 219 239 Helical. {ECO:0000255}.
METAL 57 57 Magnesium (chlorophyll-b 1 axial ligand);
via carbonyl oxygen.
{ECO:0000250|UniProtKB:P12333}.
METAL 98 98 Magnesium (chlorophyll-a 1 axial ligand).
{ECO:0000250|UniProtKB:P12333}.
METAL 101 101 Magnesium (chlorophyll-a 2 axial ligand).
{ECO:0000250|UniProtKB:P12333}.
METAL 152 152 Magnesium (chlorophyll-b 2 axial ligand);
via carbonyl oxygen.
{ECO:0000250|UniProtKB:P12333}.
METAL 172 172 Magnesium (chlorophyll-b 3 axial ligand).
{ECO:0000250|UniProtKB:P12333}.
METAL 213 213 Magnesium (chlorophyll-a 3 axial ligand).
{ECO:0000250|UniProtKB:P12333}.
METAL 216 216 Magnesium (chlorophyll-a 4 axial ligand).
{ECO:0000250|UniProtKB:P12333}.
METAL 230 230 Magnesium (chlorophyll-a 5 axial ligand).
{ECO:0000250|UniProtKB:P12333}.
METAL 245 245 Magnesium (chlorophyll-a 6 axial ligand).
{ECO:0000250|UniProtKB:P12333}.
BINDING 79 79 Chlorophyll-a 1; via amide nitrogen.
{ECO:0000250|UniProtKB:P07371}.
BINDING 85 85 Chlorophyll-a 1.
{ECO:0000250|UniProtKB:P07371}.
BINDING 103 103 Chlorophyll-b 2.
{ECO:0000250|UniProtKB:P07371}.
BINDING 136 136 Chlorophyll-a 3.
{ECO:0000250|UniProtKB:P07371}.
BINDING 146 146 Chlorophyll-a 3; via amide nitrogen.
{ECO:0000250|UniProtKB:P07371}.
BINDING 156 156 Chlorophyll-b 3.
{ECO:0000250|UniProtKB:P07371}.
BINDING 164 164 Chlorophyll-b 4 or chlorophyll-b 5.
{ECO:0000250|UniProtKB:P07371}.
BINDING 175 175 Chlorophyll-b 4.
{ECO:0000250|UniProtKB:P07371}.
BINDING 181 181 Chlorophyll-b 2; via amide nitrogen.
{ECO:0000250|UniProtKB:P07371}.
BINDING 212 212 Chlorophyll-a 5.
{ECO:0000250|UniProtKB:P07371}.
BINDING 218 218 Chlorophyll-a 1.
{ECO:0000250|UniProtKB:P07371}.
BINDING 254 254 Chlorophyll-a 6; via amide nitrogen.
{ECO:0000250|UniProtKB:P07371}.
BINDING 261 261 Chlorophyll-b 5; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P07371}.
MOD_RES 40 40 Phosphothreonine; by STN7.
{ECO:0000269|PubMed:23888908}.
SEQUENCE 265 AA; 28621 MW; 7F780F4E62B45547 CRC64;
MATSAIQQSS FAGQTALKPS SDLIQKVGVL GGGRVTMRRT VKSTPQSIWY GPDRPKYLGP
FSENTPSYLT GEYPGDYGWD TAGLSADPET FAKNRELEVI HSRWAMLGAL GCTFPEILSK
NGVKFGEAVW FKAGSQIFSE GGLDYLGNPN LIHAQSILAI WAVQVVLMGF IEGYRIGGGP
LGEGLDPLYP GGAFDPLNLA EDPEAFSELK VKELKNGRLA MFSMFGFFVQ AIVTGKGPIE
NLFDHLADPV ANNAWSYATN FVPGK


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