CB22_ARATH
ID CB22_ARATH Reviewed; 265 AA.
AC Q9S7J7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Chlorophyll a-b binding protein 2.2, chloroplastic {ECO:0000303|PubMed:10366881};
DE AltName: Full=Photosystem II light harvesting complex gene 2.2 {ECO:0000303|PubMed:10366881};
DE AltName: Full=Protein LIGHT-HARVESTING CHLOROPHYLL B-BINDING 2.2 {ECO:0000303|PubMed:10366881};
DE Flags: Precursor;
GN Name=LHCB2.2 {ECO:0000303|PubMed:10366881};
GN OrderedLocusNames=At2g05070 {ECO:0000312|Araport:AT2G05070};
GN ORFNames=F1O13.20 {ECO:0000312|EMBL:AAD25595.1};
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], 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 DEPHOSPHORYLATION BY PPH1.
RX PubMed=20176943; DOI=10.1073/pnas.0913810107;
RA Shapiguzov A., Ingelsson B., Samol I., Andres C., Kessler F., Rochaix J.D.,
RA Vener A.V., Goldschmidt-Clermont M.;
RT "The PPH1 phosphatase is specifically involved in LHCII dephosphorylation
RT and state transitions in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4782-4787(2010).
RN [6]
RP INDUCTION BY LOW LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=22236032; DOI=10.1186/1471-2229-12-6;
RA Mishra Y., Jaenkaenpaeae H.J., Kiss A.Z., Funk C., Schroeder W.P.,
RA Jansson S.;
RT "Arabidopsis plants grown in the field and climate chambers significantly
RT differ in leaf morphology and photosystem components.";
RL BMC Plant Biol. 12:6-6(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22143917; DOI=10.1093/jxb/err315;
RA Xu Y.-H., Liu R., Yan L., Liu Z.-Q., Jiang S.-C., Shen Y.-Y., Wang X.-F.,
RA Zhang D.-P.;
RT "Light-harvesting chlorophyll a/b-binding proteins are required for
RT stomatal response to abscisic acid in Arabidopsis.";
RL J. Exp. Bot. 63:1095-1106(2012).
RN [8]
RP REPRESSION BY DESICCATION; COLD AND HIGH IRRADIANCE.
RC STRAIN=cv. Columbia;
RX PubMed=23598180; DOI=10.1016/j.jplph.2013.03.008;
RA Lucinski R., Jackowski G.;
RT "AtFtsH heterocomplex-mediated degradation of apoproteins of the major
RT light harvesting complex of photosystem II (LHCII) in response to
RT stresses.";
RL J. Plant Physiol. 170:1082-1089(2013).
RN [9]
RP FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23995216; DOI=10.1016/j.jphotobiol.2013.07.028;
RA Nellaepalli S., Kodru S., Malavath T., Subramanyam R.;
RT "Change in fast Chl a fluorescence transients, 2 dimensional protein
RT profile and pigment protein interactions during state transitions in
RT Arabidopsis thaliana.";
RL J. Photochem. Photobiol. B 128:27-34(2013).
RN [10]
RP FUNCTION, PHOSPHORYLATION AT THR-40 BY STN7, AND SUBUNIT.
RX PubMed=23888908; DOI=10.1111/tpj.12297;
RA Leoni C., Pietrzykowska M., Kiss A.Z., Suorsa M., Ceci L.R., Aro E.M.,
RA Jansson S.;
RT "Very rapid phosphorylation kinetics suggest a unique role for Lhcb2 during
RT state transitions in Arabidopsis.";
RL Plant J. 76:236-246(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=25194026; DOI=10.1105/tpc.114.127373;
RA Pietrzykowska M., Suorsa M., Semchonok D.A., Tikkanen M., Boekema E.J.,
RA Aro E.-M., Jansson S.;
RT "The light-harvesting chlorophyll a/b binding proteins Lhcb1 and Lhcb2 play
RT complementary roles during state transitions in Arabidopsis.";
RL Plant Cell 26:3646-3660(2014).
RN [12]
RP FUNCTION, SUBUNIT, PHOSPHORYLATION BY STN7, AND DEPHOSPHORYLATION BY PPH1.
RC STRAIN=cv. Columbia;
RX PubMed=26392145; DOI=10.1016/j.bbabio.2015.09.005;
RA Crepin A., Caffarri S.;
RT "The specific localizations of phosphorylated Lhcb1 and Lhcb2 isoforms
RT reveal the role of Lhcb2 in the formation of the PSI-LHCII supercomplex in
RT Arabidopsis during state transitions.";
RL Biochim. Biophys. Acta 1847:1539-1548(2015).
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 (By similarity). Mediates rapid
CC phosphorylation and migration of LHCII-PSII to photosystem I (PSI)
CC after transition to state 2 (red) light conditions, thus leading to the
CC formation of PSI-PSII-LHCII and PSI-LHCII supercomplex to balance the
CC relative excitation of PSI and PSII (PubMed:23995216, PubMed:23888908,
CC PubMed:25194026, PubMed:26392145). Involved in the production of
CC reactive oxygen species (ROS) and stomatal closure upon abscisic acid
CC (ABA) treatment. Required to prevent water loss (PubMed:22143917).
CC {ECO:0000250|UniProtKB:P27521, ECO:0000269|PubMed:22143917,
CC ECO:0000269|PubMed:23888908, ECO:0000269|PubMed:23995216,
CC ECO:0000269|PubMed:25194026, ECO:0000269|PubMed:26392145}.
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:P12333};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins
CC (By similarity). Component of LHCII trimers made of LHCB1, LHCB2 and
CC LHCB3 subunits (PubMed:23888908, PubMed:23995216, PubMed:25194026).
CC Associated with super- (PSI-LHCII and PSII-LHCII) and mega-complexes
CC (PSI-PSII-LHCII) containing LHCII and both photosystem (PS)I and PSII,
CC in state 2 (red) light conditions (PubMed:23995216, PubMed:23888908,
CC PubMed:25194026, PubMed:26392145). {ECO:0000250|UniProtKB:P12333,
CC ECO:0000269|PubMed:23888908, ECO:0000269|PubMed:23995216,
CC ECO:0000269|PubMed:25194026, ECO:0000269|PubMed:26392145}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:23995216}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Accumulates at stronger levels in low light than in normal
CC or high light; more expressed in growth chamber conditions than when
CC grown in the field (PubMed:22236032). Repressed in leaves exposed to
CC desiccation, cold and high irradiance via a metalloprotease-dependent
CC proteolytic process (at protein level) (PubMed:23598180).
CC {ECO:0000269|PubMed:22236032, ECO:0000269|PubMed:23598180}.
CC -!- PTM: Photoregulated by reversible but rapid phosphorylation by STN7 of
CC its threonine residues under state 2 (red) light conditions
CC (PubMed:23995216, PubMed:23888908, PubMed:26392145). Dephosphorylated
CC by PPH1 in state 1 (far red) light conditions (PubMed:20176943,
CC PubMed:23995216, PubMed:23888908, PubMed:26392145). Phosphorylation
CC triggers the formation of the PSI-LHCII supercomplex (PubMed:26392145).
CC {ECO:0000269|PubMed:20176943, ECO:0000269|PubMed:23888908,
CC ECO:0000269|PubMed:23995216, ECO:0000269|PubMed:26392145}.
CC -!- DISRUPTION PHENOTYPE: In plants silenced with microRNAs, functional
CC LHCII thylakoid protein complexes where LHCB2 is replaced by LHCB1.
CC However these LHCII complexes are impaired in light state transitions,
CC leading to stunted growth in high light (PubMed:25194026). Reduced
CC reactive oxygen species (ROS) production in leaves and impaired
CC stomatal closure in response to abscisic acid (ABA). Increased water
CC loss and reduced resistance to drought, probably due to open stomata.
CC Altered expression of other LHCB members (PubMed:22143917).
CC {ECO:0000269|PubMed:22143917, ECO:0000269|PubMed:25194026}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; AF134123; AAD28770.1; -; mRNA.
DR EMBL; AC007211; AAD25595.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05893.1; -; Genomic_DNA.
DR EMBL; AY054218; AAL06878.1; -; mRNA.
DR EMBL; AY062563; AAL32641.1; -; mRNA.
DR EMBL; AY066036; AAL47403.1; -; mRNA.
DR EMBL; AY093372; AAM13371.1; -; mRNA.
DR PIR; T52324; T52324.
DR RefSeq; NP_178582.1; NM_126537.4.
DR AlphaFoldDB; Q9S7J7; -.
DR SMR; Q9S7J7; -.
DR IntAct; Q9S7J7; 1.
DR STRING; 3702.AT2G05070.1; -.
DR iPTMnet; Q9S7J7; -.
DR PaxDb; Q9S7J7; -.
DR PRIDE; Q9S7J7; -.
DR ProteomicsDB; 239151; -.
DR EnsemblPlants; AT2G05070.1; AT2G05070.1; AT2G05070.
DR GeneID; 815055; -.
DR Gramene; AT2G05070.1; AT2G05070.1; AT2G05070.
DR KEGG; ath:AT2G05070; -.
DR Araport; AT2G05070; -.
DR TAIR; locus:2044988; AT2G05070.
DR eggNOG; ENOG502QPU1; Eukaryota.
DR HOGENOM; CLU_057943_2_0_1; -.
DR InParanoid; Q9S7J7; -.
DR OMA; XSFLSAV; -.
DR OrthoDB; 1476770at2759; -.
DR PhylomeDB; Q9S7J7; -.
DR PRO; PR:Q9S7J7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9S7J7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; 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:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009522; C:photosystem I; IDA:UniProtKB.
DR GO; GO:0009523; C:photosystem II; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0009517; C:PSII associated light-harvesting complex II; IDA:UniProtKB.
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:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IDA:UniProtKB.
DR GO; GO:0009769; P:photosynthesis, light harvesting in photosystem II; IDA:UniProtKB.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009269; P:response to desiccation; IEP:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IDA:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR GO; GO:0009645; P:response to low light intensity stimulus; IEP:UniProtKB.
DR GO; GO:0010114; P:response to red light; IDA:UniProtKB.
DR GO; GO:0030104; P:water homeostasis; IMP: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 Chlorophyll; Chloroplast; Chromophore; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Photosynthesis; Photosystem I; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT CHAIN 38..265
FT /note="Chlorophyll a-b binding protein 2.2, chloroplastic"
FT /id="PRO_0000438438"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 57
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 79
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 85
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 98
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 101
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
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 103
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 136
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 146
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 152
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 156
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 164
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 164
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 172
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 175
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 181
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 212
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 213
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 216
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 218
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 230
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 245
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 254
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 261
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT MOD_RES 40
FT /note="Phosphothreonine; by STN7"
FT /evidence="ECO:0000269|PubMed:23888908"
SQ 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
