CAB6_ARATH
ID CAB6_ARATH Reviewed; 241 AA.
AC Q01667; B9DHK2; Q9C5R7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chlorophyll a-b binding protein 6, chloroplastic;
DE AltName: Full=LHCI-730;
DE AltName: Full=LHCII type III CAB-6;
DE AltName: Full=Light-harvesting complex protein Lhca1 {ECO:0000303|PubMed:10366881};
DE Flags: Precursor;
GN Name=LHCA1 {ECO:0000303|PubMed:10366881}; Synonyms=CAB6;
GN OrderedLocusNames=At3g54890; ORFNames=F28P10.130;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RA Jensen P.E., Kristensen M., Lehmbeck J., Hoff T., Stummann B.M.,
RA Henningsen K.W.;
RT "Identification of a single-copy gene encoding a type I chlorophyll a/b-
RT binding polypeptide of photosystem I in Arabidopsis thaliana.";
RL Physiol. Plantarum 84:561-567(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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] OF 83-241.
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 [6]
RP 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 [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10818090; DOI=10.1074/jbc.m000550200;
RA Jensen P.E., Gilpin M., Knoetzel J., Scheller H.V.;
RT "The PSI-K subunit of photosystem I is involved in the interaction between
RT light-harvesting complex I and the photosystem I reaction center core.";
RL J. Biol. Chem. 275:24701-24708(2000).
RN [8]
RP REVIEW ON PHOTOSYSTEM I ANTENNA.
RX PubMed=12324436; DOI=10.1016/s0006-3495(02)73979-9;
RA Ihalainen J.A., Jensen P.E., Haldrup A., van Stokkum I.H.M.,
RA van Grondelle R., Scheller H.V., Dekker J.P.;
RT "Pigment organization and energy transfer dynamics in isolated photosystem
RT I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K,
RT PSI-L, or PSI-N subunit.";
RL Biophys. J. 83:2190-2201(2002).
RN [9]
RP INDUCTION BY LIGHT AND COLD.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=15356385; DOI=10.1023/b:plan.0000040813.05224.94;
RA Ganeteg U., Klimmek F., Jansson S.;
RT "Lhca5--an LHC-type protein associated with photosystem I.";
RL Plant Mol. Biol. 54:641-651(2004).
RN [10]
RP INTERACTION WITH LHCA5, MISCELLANEOUS, AND COFACTOR.
RX PubMed=15563470; DOI=10.1074/jbc.m411248200;
RA Storf S., Jansson S., Schmid V.H.R.;
RT "Pigment binding, fluorescence properties, and oligomerization behavior of
RT Lhca5, a novel light-harvesting protein.";
RL J. Biol. Chem. 280:5163-5168(2005).
RN [11]
RP SUBUNIT, AND COFACTOR.
RC STRAIN=cv. Columbia;
RX PubMed=21083539; DOI=10.1042/bj20101538;
RA Wientjes E., Croce R.;
RT "The light-harvesting complexes of higher-plant Photosystem I: Lhca1/4 and
RT Lhca2/3 form two red-emitting heterodimers.";
RL Biochem. J. 433:477-485(2011).
RN [12]
RP INTERACTION WITH LHCA5, AND FUNCTION.
RX PubMed=21806943; DOI=10.1016/j.bpj.2011.06.045;
RA Wientjes E., van Stokkum I.H.M., van Amerongen H., Croce R.;
RT "The role of the individual Lhcas in photosystem I excitation energy
RT trapping.";
RL Biophys. J. 101:745-754(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 49-235.
RX PubMed=17476261; DOI=10.1038/nature05687;
RA Amunts A., Drory O., Nelson N.;
RT "The structure of a plant photosystem I supercomplex at 3.4 A resolution.";
RL Nature 447:58-63(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=19923216; DOI=10.1074/jbc.m109.072645;
RA Amunts A., Toporik H., Borovikova A., Nelson N.;
RT "Structure determination and improved model of plant photosystem I.";
RL J. Biol. Chem. 285:3478-3486(2010).
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. {ECO:0000269|PubMed:21806943}.
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:0000269|PubMed:15563470, ECO:0000269|PubMed:21083539};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC Red-emitting heterodimer with LHCA4 (PubMed:21083539). Interacts with
CC LHCA5 (PubMed:21806943, PubMed:15563470). {ECO:0000269|PubMed:15563470,
CC ECO:0000269|PubMed:21083539, ECO:0000269|PubMed:21806943}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10818090}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q01667-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by low light (LL) but repressed by high light (HL).
CC Inhibited by cold. {ECO:0000269|PubMed:15356385}.
CC -!- DOMAIN: The N-terminus of the protein extends into the stroma where it
CC is involved with adhesion of granal membranes and post-translational
CC modifications; both are believed to mediate the distribution of
CC excitation energy between photosystems I and II.
CC -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC residues. {ECO:0000250}.
CC -!- MISCELLANEOUS: Light emission at 684 nm upon excitation at 410 and 470
CC nm. {ECO:0000269|PubMed:15563470}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; M85150; AAA32759.1; -; Genomic_DNA.
DR EMBL; X56062; CAA39534.1; -; mRNA.
DR EMBL; AL049655; CAB41095.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79306.1; -; Genomic_DNA.
DR EMBL; AF324692; AAG40043.2; -; mRNA.
DR EMBL; AF325016; AAG40368.1; -; mRNA.
DR EMBL; AF326866; AAG41448.1; -; mRNA.
DR EMBL; AF339688; AAK00370.1; -; mRNA.
DR EMBL; AF361847; AAK32859.1; -; mRNA.
DR EMBL; AY070473; AAL49939.1; -; mRNA.
DR EMBL; AY094437; AAM19809.1; -; mRNA.
DR EMBL; BT000852; AAN38689.1; -; mRNA.
DR EMBL; AK317555; BAH20219.1; -; mRNA.
DR PIR; S25435; S25435.
DR RefSeq; NP_191049.1; NM_115346.4. [Q01667-1]
DR PDB; 2O01; X-ray; 3.40 A; 1=49-235.
DR PDB; 2WSC; X-ray; 3.30 A; 1=1-241.
DR PDB; 2WSE; X-ray; 3.49 A; 1=1-241.
DR PDB; 2WSF; X-ray; 3.48 A; 1=1-241.
DR PDB; 4XK8; X-ray; 2.80 A; 1/6=46-240.
DR PDB; 6ZOO; EM; 2.74 A; 1=47-239.
DR PDB; 7WFD; EM; 3.25 A; A1=1-241.
DR PDB; 7WFE; EM; 3.25 A; B1=1-241.
DR PDB; 7WG5; EM; 3.89 A; A1/B1=1-241.
DR PDBsum; 2O01; -.
DR PDBsum; 2WSC; -.
DR PDBsum; 2WSE; -.
DR PDBsum; 2WSF; -.
DR PDBsum; 4XK8; -.
DR PDBsum; 6ZOO; -.
DR PDBsum; 7WFD; -.
DR PDBsum; 7WFE; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q01667; -.
DR SMR; Q01667; -.
DR BioGRID; 9970; 15.
DR DIP; DIP-59003N; -.
DR IntAct; Q01667; 1.
DR STRING; 3702.AT3G54890.1; -.
DR PaxDb; Q01667; -.
DR PRIDE; Q01667; -.
DR ProteomicsDB; 223859; -. [Q01667-1]
DR EnsemblPlants; AT3G54890.1; AT3G54890.1; AT3G54890. [Q01667-1]
DR GeneID; 824654; -.
DR Gramene; AT3G54890.1; AT3G54890.1; AT3G54890. [Q01667-1]
DR KEGG; ath:AT3G54890; -.
DR Araport; AT3G54890; -.
DR TAIR; locus:2082717; AT3G54890.
DR eggNOG; ENOG502QTYF; Eukaryota.
DR HOGENOM; CLU_057943_5_0_1; -.
DR InParanoid; Q01667; -.
DR OMA; LKEITHC; -.
DR PhylomeDB; Q01667; -.
DR EvolutionaryTrace; Q01667; -.
DR PRO; PR:Q01667; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q01667; baseline and differential.
DR Genevisible; Q01667; AT.
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:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
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:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; 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 GO; GO:0009645; P:response to low light intensity stimulus; IEP: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 3D-structure; Alternative splicing; Chlorophyll; Chloroplast; Chromophore;
KW Magnesium; Membrane; Metal-binding; Phosphoprotein; Photosynthesis;
KW Photosystem I; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..241
FT /note="Chlorophyll a-b binding protein 6, chloroplastic"
FT /id="PRO_0000401362"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 48
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"
FT BINDING 68
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
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"
FT BINDING 90
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"
FT BINDING 92
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 133
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"
FT BINDING 153
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"
FT BINDING 156
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 191
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"
FT BINDING 194
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"
FT BINDING 196
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 208
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"
FT BINDING 224
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"
FT CONFLICT 11
FT /note="I -> K (in Ref. 4; AAG40043)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="R -> K (in Ref. 4; AAG40043)"
FT /evidence="ECO:0000305"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2O01"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4XK8"
FT HELIX 77..106
FT /evidence="ECO:0007829|PDB:6ZOO"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6ZOO"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6ZOO"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2WSC"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2WSC"
FT HELIX 138..157
FT /evidence="ECO:0007829|PDB:6ZOO"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2O01"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6ZOO"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6ZOO"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2WSC"
FT HELIX 181..211
FT /evidence="ECO:0007829|PDB:6ZOO"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:6ZOO"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6ZOO"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:6ZOO"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6ZOO"
SQ SEQUENCE 241 AA; 25996 MW; 2F5EE06B55A979CE CRC64;
MASNSLMSCG IAAVYPSLLS SSKSKFVSAG VPLPNAGNVG RIRMAAHWMP GEPRPAYLDG
SAPGDFGFDP LGLGEVPANL ERYKESELIH CRWAMLAVPG ILVPEALGYG NWVKAQEWAA
LPGGQATYLG NPVPWGTLPT ILAIEFLAIA FVEHQRSMEK DPEKKKYPGG AFDPLGYSKD
PKKLEELKVK EIKNGRLALL AFVGFCVQQS AYPGTGPLEN LATHLADPWH NNIGDIVIPF
N
