CB24_ARATH
ID CB24_ARATH Reviewed; 266 AA.
AC Q9XF87; C0Z391;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Chlorophyll a-b binding protein 2.4, chloroplastic {ECO:0000303|PubMed:10366881};
DE AltName: Full=Photosystem II light harvesting complex gene 2.4 {ECO:0000303|PubMed:10366881};
DE AltName: Full=Protein LIGHT-HARVESTING CHLOROPHYLL B-BINDING 2.4 {ECO:0000303|PubMed:10366881};
DE Flags: Precursor;
GN Name=LHCB2.4 {ECO:0000303|PubMed:10366881};
GN OrderedLocusNames=At3g27690 {ECO:0000312|Araport:AT3G27690};
GN ORFNames=MGF10.9 {ECO:0000312|EMBL:BAB02693.1};
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] (ISOFORM 1), 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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
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 [7]
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 [8]
RP INDUCTION BY BZIP68 AND GBF1.
RC STRAIN=cv. Columbia;
RX PubMed=22718771; DOI=10.1074/jbc.m112.361394;
RA Shaikhali J., Noren L., de Dios Barajas-Lopez J., Srivastava V., Koenig J.,
RA Sauer U.H., Wingsle G., Dietz K.J., Strand A.;
RT "Redox-mediated mechanisms regulate DNA binding activity of the G-group of
RT basic region leucine zipper (bZIP) transcription factors in Arabidopsis.";
RL J. Biol. Chem. 287:27510-27525(2012).
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 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 [11]
RP FUNCTION, PHOSPHORYLATION AT THR-41 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 [12]
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 [13]
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 (By similarity).
CC {ECO:0000250|UniProtKB:P27521, ECO:0000250|UniProtKB:Q9S7J7,
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XF87-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XF87-2; Sequence=VSP_058661;
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). Activated by
CC BZIP68 and GBF1 but repressed by BZIP16 (PubMed:22718771).
CC {ECO:0000269|PubMed:22236032, ECO:0000269|PubMed:22718771,
CC 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. {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; AF134125; AAD28772.1; -; mRNA.
DR EMBL; AB018114; BAB02693.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77352.1; -; Genomic_DNA.
DR EMBL; AF370557; AAK48984.1; -; mRNA.
DR EMBL; BT006298; AAP13406.1; -; mRNA.
DR EMBL; AK319055; BAH57170.1; -; mRNA.
DR PIR; T52322; T52322.
DR RefSeq; NP_189406.1; NM_113685.4. [Q9XF87-1]
DR AlphaFoldDB; Q9XF87; -.
DR SMR; Q9XF87; -.
DR STRING; 3702.AT3G27690.1; -.
DR iPTMnet; Q9XF87; -.
DR PaxDb; Q9XF87; -.
DR PRIDE; Q9XF87; -.
DR ProteomicsDB; 222788; -. [Q9XF87-1]
DR EnsemblPlants; AT3G27690.1; AT3G27690.1; AT3G27690. [Q9XF87-1]
DR GeneID; 822391; -.
DR Gramene; AT3G27690.1; AT3G27690.1; AT3G27690. [Q9XF87-1]
DR KEGG; ath:AT3G27690; -.
DR Araport; AT3G27690; -.
DR TAIR; locus:2089139; AT3G27690.
DR eggNOG; ENOG502QPU1; Eukaryota.
DR HOGENOM; CLU_057943_2_0_1; -.
DR InParanoid; Q9XF87; -.
DR PhylomeDB; Q9XF87; -.
DR PRO; PR:Q9XF87; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9XF87; baseline and differential.
DR GO; GO:0009941; C:chloroplast envelope; 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; IDA:UniProtKB.
DR GO; GO:0009523; C:photosystem II; IDA:UniProtKB.
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; ISS: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; ISS:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; ISS: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; ISS: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 Alternative splicing; Chlorophyll; Chloroplast; Chromophore; Magnesium;
KW Membrane; Metal-binding; Phosphoprotein; Photosynthesis; Photosystem I;
KW Photosystem II; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT CHAIN 39..266
FT /note="Chlorophyll a-b binding protein 2.4, chloroplastic"
FT /id="PRO_0000438439"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 58
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 80
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 86
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 99
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 102
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 104
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 137
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 147
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 153
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 157
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 165
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 165
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 173
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 176
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 182
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 213
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 214
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 217
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 219
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 231
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 246
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 255
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 262
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT MOD_RES 41
FT /note="Phosphothreonine; by STN7"
FT /evidence="ECO:0000269|PubMed:23888908"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /id="VSP_058661"
SQ SEQUENCE 266 AA; 28803 MW; 9BAE36EDA70FD3ED CRC64;
MATSAIQHSS FAGQTTLKPS NDLLRKIGAS NGGGRIIMRR TVKSTPQSIW YGPDRPKYLG
PFSENTPSYL TGEYPGDYGW DTAGLSADPE TFAKNRELEV IHSRWAMLGA LGCTFPEILS
KNGVKFGEAV WFKAGSQIFS EGGLDYLGNP NLIHAQSILA IWACQVVLMG FIEGYRIGGG
PLGEGLDPLY PGGAFDPLNL AEDPEAFSEL KVKELKNGRL AMFSMFGFFV QAIVTGKGPI
ENLFDHIADP VANNAWAYAT NFVPGK
