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   27-MAR-2024, entry version 160.
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   PDB; 8J6Z; EM; 2.79 A; 1=1-241.
DR   PDB; 8J7A; EM; 3.06 A; 1=1-241.
DR   PDB; 8J7B; EM; 3.22 A; 1=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   PDBsum; 8J6Z; -.
DR   PDBsum; 8J7A; -.
DR   PDBsum; 8J7B; -.
DR   AlphaFoldDB; Q01667; -.
DR   EMDB; EMD-11326; -.
DR   EMDB; EMD-32462; -.
DR   EMDB; EMD-32463; -.
DR   EMDB; EMD-32477; -.
DR   EMDB; EMD-36021; -.
DR   EMDB; EMD-36036; -.
DR   EMDB; EMD-36037; -.
DR   SMR; Q01667; -.
DR   BioGRID; 9970; 15.
DR   DIP; DIP-59003N; -.
DR   IntAct; Q01667; 2.
DR   STRING; 3702.Q01667; -.
DR   PaxDb; 3702-AT3G54890-1; -.
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; AT3G54890; LHCA1.
DR   eggNOG; ENOG502QTYF; Eukaryota.
DR   HOGENOM; CLU_057943_5_0_1; -.
DR   InParanoid; Q01667; -.
DR   OMA; MTSDWMP; -.
DR   OrthoDB; 444860at2759; -.
DR   PhylomeDB; Q01667; -.
DR   EvolutionaryTrace; Q01667; -.
DR   PRO; PR:Q01667; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q01667; 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: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:0009645; P:response to low light intensity stimulus; IEP:UniProtKB.
DR   Gene3D; 1.10.3460.10; Chlorophyll a/b binding protein domain; 1.
DR   InterPro; IPR001344; Chloro_AB-bd_pln.
DR   InterPro; IPR022796; Chloroa_b-bind.
DR   PANTHER; PTHR21649:SF89; CHLOROPHYLL A-B BINDING PROTEIN 6, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21649; CHLOROPHYLL A/B BINDING PROTEIN; 1.
DR   Pfam; PF00504; Chloroa_b-bind; 1.
DR   SUPFAM; SSF103511; Chlorophyll a-b binding protein; 1.
DR   Genevisible; Q01667; AT.
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
//