CB3_ARATH
ID CB3_ARATH Reviewed; 265 AA.
AC Q9S7M0; C0Z239; Q42016;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Chlorophyll a-b binding protein 3, chloroplastic;
DE AltName: Full=Light-harvesting chlorophyll B-binding protein 3 {ECO:0000312|EMBL:AED96477.1};
DE Short=LHCB3*1 {ECO:0000303|PubMed:11245797};
DE Short=Lhcb3 {ECO:0000303|PubMed:11245797};
DE Flags: Precursor;
GN Name=LHCB3 {ECO:0000303|PubMed:11245797};
GN OrderedLocusNames=At5g54270 {ECO:0000312|Araport:AT5G54270};
GN ORFNames=MDK4.9 {ECO:0000312|EMBL:BAB10750.1};
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:AAD37362.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Benedetti C.E., Arruda P.;
RT "Isolation of an Arabidopsis type III chlorophyll a/b binding protein gene
RT (Lhcb3*1).";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-104 (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Protoplast;
RA Berthomieu P., Guerrier D., Giraudat J.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=11245797; DOI=10.1016/s0005-2728(00)00262-0;
RA Jackowski G., Kacprzak K., Jansson S.;
RT "Identification of Lhcb1/Lhcb2/Lhcb3 heterotrimers of the main light-
RT harvesting chlorophyll a/b-protein complex of Photosystem II (LHC II).";
RL Biochim. Biophys. Acta 1504:340-345(2001).
RN [9]
RP INTERACTION WITH LHCB1 AND LHCB2.
RX PubMed=15208324; DOI=10.1074/jbc.m402348200;
RA Standfuss J., Kuehlbrandt W.;
RT "The three isoforms of the light-harvesting complex II: spectroscopic
RT features, trimer formation, and functional roles.";
RL J. Biol. Chem. 279:36884-36891(2004).
RN [10]
RP INDUCTION BY LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=16170635; DOI=10.1007/s11120-005-6807-z;
RA Tanaka R., Tanaka A.;
RT "Effects of chlorophyllide a oxygenase overexpression on light acclimation
RT in Arabidopsis thaliana.";
RL Photosyn. Res. 85:327-340(2005).
RN [11]
RP SUBUNIT, INTERACTION WITH LHCB5, AND SUBCELLULAR LOCATION.
RX PubMed=16551629; DOI=10.1074/jbc.m511415200;
RA Ruban A.V., Solovieva S., Lee P.J., Ilioaia C., Wentworth M., Ganeteg U.,
RA Klimmek F., Chow W.S., Anderson J.M., Jansson S., Horton P.;
RT "Plasticity in the composition of the light harvesting antenna of higher
RT plants preserves structural integrity and biological function.";
RL J. Biol. Chem. 281:14981-14990(2006).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19880802; DOI=10.1105/tpc.108.064006;
RA Damkjaer J.T., Kereiche S., Johnson M.P., Kovacs L., Kiss A.Z.,
RA Boekema E.J., Ruban A.V., Horton P., Jansson S.;
RT "The photosystem II light-harvesting protein Lhcb3 affects the
RT macrostructure of photosystem II and the rate of state transitions in
RT Arabidopsis.";
RL Plant Cell 21:3245-3256(2009).
RN [13]
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 [14]
RP INDUCTION BY HIGH LIGHT, AND SUBUNIT.
RX PubMed=23274453; DOI=10.1016/j.bbabio.2012.12.003;
RA Kouril R., Wientjes E., Bultema J.B., Croce R., Boekema E.J.;
RT "High-light vs. low-light: effect of light acclimation on photosystem II
RT composition and organization in Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1827:411-419(2013).
RN [15]
RP INDUCTION BY HIGH LIGHT.
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 [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26562806; DOI=10.1016/j.jphotobiol.2015.11.002;
RA Adamiec M., Gibasiewicz K., Lucinski R., Giera W., Chelminiak P.,
RA Szewczyk S., Sipinska W., van Grondelle R., Jackowski G.;
RT "Excitation energy transfer and charge separation are affected in
RT Arabidopsis thaliana mutants lacking light-harvesting chlorophyll a/b
RT binding protein Lhcb3.";
RL J. Photochem. Photobiol. B 153:423-428(2015).
RN [17]
RP REGULATION BY BROMACIL.
RX PubMed=26802342; DOI=10.1016/j.scitotenv.2016.01.046;
RA Chen Z., Zou Y., Wang J., Li M., Wen Y.;
RT "Phytotoxicity of chiral herbicide bromacil: Enantioselectivity of
RT photosynthesis in Arabidopsis thaliana.";
RL Sci. Total Environ. 548:139-147(2016).
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 (PubMed:26562806). Modulates the
CC rate of photosystem II (PSII) state transitions and influences PSII
CC macrostructure (PubMed:19880802). Involved in PSII excitation energy
CC transfer and charge separation during photosynthesis in thylakoids
CC (PubMed:26562806). {ECO:0000269|PubMed:19880802,
CC ECO:0000269|PubMed:26562806}.
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: Present in M heterotrimers (PubMed:23274453). Forms
CC heterotrimers with LHCB1, LHCB2, and LHCB5 proteins (PubMed:16551629,
CC PubMed:15208324). The LHC complex consists of chlorophyll a-b binding
CC proteins (PubMed:11245797). {ECO:0000269|PubMed:11245797,
CC ECO:0000269|PubMed:15208324, ECO:0000269|PubMed:16551629,
CC ECO:0000269|PubMed:23274453}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:16551629}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9S7M0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S7M0-2; Sequence=VSP_058349;
CC -!- INDUCTION: Repressed by high-light (HL) in a CAO-dependent manner (at
CC protein level) (PubMed:16170635, PubMed:23598180). Reduced levels
CC relative to CP43 during high light acclimation, thus helping
CC photosystem II (PSII) structural re-arrangement (PubMed:23274453).
CC Repressed by the herbicide bromacil (BRO) (PubMed:26802342).
CC {ECO:0000269|PubMed:16170635, ECO:0000269|PubMed:23274453,
CC ECO:0000269|PubMed:23598180, ECO:0000269|PubMed:26802342}.
CC -!- DISRUPTION PHENOTYPE: In koLhcb3, accumulation of LHCB1 and LHCB2
CC apoproteins to adjust photosystem II (PSII) (PubMed:19880802,
CC PubMed:26562806). However, altered macrostructural arrangement of the
CC LHCII antenna and increased rate of PSII transition from state 1 to
CC state 2. Increased phosphorylation level of LHCII (PubMed:19880802).
CC Reduced responsiveness of stomatal movement to abscisic acid (ABA),
CC therefore resulting in a decrease in tolerance to drought stress
CC (PubMed:22143917). Deceleration of the fast phase of excitation
CC dynamics in grana cores (PubMed:26562806).
CC {ECO:0000269|PubMed:19880802, ECO:0000269|PubMed:22143917,
CC ECO:0000269|PubMed:26562806}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; AF143691; AAD37362.1; -; mRNA.
DR EMBL; AF134126; AAD28773.1; -; mRNA.
DR EMBL; AB010695; BAB10750.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96477.1; -; Genomic_DNA.
DR EMBL; AF361858; AAK32870.1; -; mRNA.
DR EMBL; AF372917; AAK49633.1; -; mRNA.
DR EMBL; AY057735; AAL15365.1; -; mRNA.
DR EMBL; AK318653; BAH56768.1; -; mRNA.
DR EMBL; Z18479; CAA79201.1; -; mRNA.
DR PIR; T52318; T52318.
DR RefSeq; NP_200238.1; NM_124807.4. [Q9S7M0-1]
DR PDB; 7OUI; EM; 2.79 A; 2/6=23-265.
DR PDBsum; 7OUI; -.
DR AlphaFoldDB; Q9S7M0; -.
DR SMR; Q9S7M0; -.
DR STRING; 3702.AT5G54270.1; -.
DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family.
DR iPTMnet; Q9S7M0; -.
DR PaxDb; Q9S7M0; -.
DR PRIDE; Q9S7M0; -.
DR ProteomicsDB; 239183; -. [Q9S7M0-1]
DR EnsemblPlants; AT5G54270.1; AT5G54270.1; AT5G54270. [Q9S7M0-1]
DR GeneID; 835515; -.
DR Gramene; AT5G54270.1; AT5G54270.1; AT5G54270. [Q9S7M0-1]
DR KEGG; ath:AT5G54270; -.
DR Araport; AT5G54270; -.
DR TAIR; locus:2162540; AT5G54270.
DR eggNOG; ENOG502QQ3N; Eukaryota.
DR HOGENOM; CLU_057943_2_0_1; -.
DR InParanoid; Q9S7M0; -.
DR OMA; PMGTGKY; -.
DR PhylomeDB; Q9S7M0; -.
DR PRO; PR:Q9S7M0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7M0; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
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:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009517; C:PSII associated light-harvesting complex II; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0042651; C:thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR GO; GO:0009769; P:photosynthesis, light harvesting in photosystem II; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009635; P:response to herbicide; IEP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IEP: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; Alternative splicing; Chlorophyll; Chloroplast; Chromophore;
KW Magnesium; Membrane; Metal-binding; Photosynthesis; Photosystem I;
KW Photosystem II; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..22
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 23..265
FT /note="Chlorophyll a-b binding protein 3, chloroplastic"
FT /id="PRO_0000436333"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 55
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 77
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 96
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 99
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 101
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 151
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 155
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 171
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 174
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
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"
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"
FT BINDING 261
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /id="VSP_058349"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 86..118
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 155..175
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 202..232
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:7OUI"
SQ SEQUENCE 265 AA; 28707 MW; 75593036C6AFBE25 CRC64;
MASTFTSSSS VLTPTTFLGQ TKASSFNPLR DVVSLGSPKY TMGNDLWYGP DRVKYLGPFS
VQTPSYLTGE FPGDYGWDTA GLSADPEAFA KNRALEVIHG RWAMLGAFGC ITPEVLQKWV
RVDFKEPVWF KAGSQIFSEG GLDYLGNPNL VHAQSILAVL GFQVILMGLV EGFRINGLDG
VGEGNDLYPG GQYFDPLGLA DDPVTFAELK VKEIKNGRLA MFSMFGFFVQ AIVTGKGPLE
NLLDHLDNPV ANNAWAFATK FAPGA
