SR43C_ARATH
ID SR43C_ARATH Reviewed; 373 AA.
AC O22265; Q93V50; Q940I7; Q9SAU3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Signal recognition particle 43 kDa protein, chloroplastic;
DE AltName: Full=Chromo protein SRP43;
DE Short=CpSRP43;
DE Flags: Precursor;
GN Name=CAO; Synonyms=CPSRP43; OrderedLocusNames=At2g47450;
GN ORFNames=T30B22.25;
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], FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9878634; DOI=10.2307/3870840;
RA Klimyuk V.I., Persello-Cartieaux F., Havaux M., Contard-David P.,
RA Schuenemann D., Meiherhoff K., Gouet P., Jones J.D.G., Hoffman N.E.,
RA Nussaume L.;
RT "A chromodomain protein encoded by the arabidopsis CAO gene is a plant-
RT specific component of the chloroplast signal recognition particle pathway
RT that is involved in LHCP targeting.";
RL Plant Cell 11:87-99(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 FUNCTION, SUBUNIT, AND INTERACTION WITH FFC/CPSRP54.
RX PubMed=10480939; DOI=10.1074/jbc.274.38.27219;
RA Tu C.J., Schuenemann D., Hoffman N.E.;
RT "Chloroplast FtsY, chloroplast signal recognition particle, and GTP are
RT required to reconstitute the soluble phase of light-harvesting chlorophyll
RT protein transport into thylakoid membranes.";
RL J. Biol. Chem. 274:27219-27224(1999).
RN [6]
RP CHARACTERIZATION, SUBUNIT, AND BINDING TO LIGHT-HARVESTING CHLOROPHYLL
RP PROTEINS AND TO FFC/CPSRP54.
RX PubMed=11306572; DOI=10.1074/jbc.m100153200;
RA Jonas-Straube E., Hutin C., Hoffman N.E., Schuenemann D.;
RT "Functional analysis of the protein-interacting domains of chloroplast
RT SRP43.";
RL J. Biol. Chem. 276:24654-24660(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH FFC/CPSRP54.
RX PubMed=15292240; DOI=10.1074/jbc.m401600200;
RA Goforth R.L., Peterson E.C., Yuan J., Moore M.J., Kight A.D., Lohse M.B.,
RA Sakon J., Henry R.L.;
RT "Regulation of the GTPase cycle in post-translational signal recognition
RT particle-based protein targeting involves cpSRP43.";
RL J. Biol. Chem. 279:43077-43084(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16813577; DOI=10.1111/j.1365-313x.2006.02803.x;
RA Durrett T.P., Connolly E.L., Rogers E.E.;
RT "Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an
RT inability to increase iron deficiency-inducible root Fe(III) chelate
RT reductase activity.";
RL Plant J. 47:467-479(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH ALB3.
RX PubMed=17513500; DOI=10.1105/tpc.106.048959;
RA Tzvetkova-Chevolleau T., Hutin C., Noel L.D., Goforth R., Carde J.P.,
RA Caffarri S., Sinning I., Groves M., Teulon J.M., Hoffman N.E., Henry R.,
RA Havaux M., Nussaume L.;
RT "Canonical signal recognition particle components can be bypassed for
RT posttranslational protein targeting in chloroplasts.";
RL Plant Cell 19:1635-1648(2007).
RN [10]
RP INTERACTION WITH ALB3; FFC/CPSRP54; CPFTSY AND LHCP.
RX PubMed=20828566; DOI=10.1016/j.febslet.2010.08.053;
RA Bals T., Duenschede B., Funke S., Schuenemann D.;
RT "Interplay between the cpSRP pathway components, the substrate LHCP and the
RT translocase Alb3: an in vivo and in vitro study.";
RL FEBS Lett. 584:4138-4144(2010).
RN [11]
RP INTERACTION WITH ALB3 AND FFC/CPSRP54, AND MUTAGENESIS OF TYR-269; TRP-291
RP AND ASP-293.
RX PubMed=20018841; DOI=10.1074/jbc.m109.084996;
RA Falk S., Ravaud S., Koch J., Sinning I.;
RT "The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the
RT thylakoid membrane.";
RL J. Biol. Chem. 285:5954-5962(2010).
RN [12]
RP FUNCTION.
RX PubMed=20498370; DOI=10.1074/jbc.c110.132746;
RA Falk S., Sinning I.;
RT "cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll
RT a,b-binding proteins.";
RL J. Biol. Chem. 285:21655-21661(2010).
RN [13]
RP INTERACTION WITH LTD.
RX PubMed=21505433; DOI=10.1038/ncomms1278;
RA Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.;
RT "LTD is a protein required for sorting light-harvesting chlorophyll-binding
RT proteins to the chloroplast SRP pathway.";
RL Nat. Commun. 2:277-277(2011).
RN [14]
RP STRUCTURE BY NMR OF 84-128 AND 265-373, AND INTERACTION WITH FFC/CPSRP54.
RX PubMed=16183644; DOI=10.1074/jbc.m507077200;
RA Sivaraja V., Kumar T.K.S., Leena P.S.T., Chang A.N., Vidya C.,
RA Goforth R.L., Rajalingam D., Arvind K., Ye J.-L., Chou J., Henry R., Yu C.;
RT "Three-dimensional solution structures of the chromodomains of cpSRP43.";
RL J. Biol. Chem. 280:41465-41471(2005).
RN [15]
RP STRUCTURE BY NMR OF 265-319.
RX PubMed=18586266; DOI=10.1016/j.jmb.2008.05.065;
RA Kathir K.M., Rajalingam D., Sivaraja V., Kight A., Goforth R.L., Yu C.,
RA Henry R., Kumar T.K.;
RT "Assembly of chloroplast signal recognition particle involves structural
RT rearrangement in cpSRP43.";
RL J. Mol. Biol. 381:49-60(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 85-267 IN COMPLEX WITH THE L18
RP DOMAIN OF LHCP, AND MUTAGENESIS OF ARG-161; ARG-192; TYR-204 AND ARG-226.
RX PubMed=18621669; DOI=10.1126/science.1158640;
RA Stengel K.F., Holdermann I., Cain P., Robinson C., Wild K., Sinning I.;
RT "Structural basis for specific substrate recognition by the chloroplast
RT signal recognition particle protein cpSRP43.";
RL Science 321:253-256(2008).
CC -!- FUNCTION: Component of the chloroplast signal recognition particle
CC pathway. Required for post-translational targeting of proteins into the
CC thylakoid membrane but seems to be dispensable for co-translational
CC targeting with a translating ribosome present. May be able to function
CC independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the
CC thylakoids. Acts as a highly specific chaperone for LHCPs, preventing
CC aggregation and being able to dissolve aggregates.
CC {ECO:0000269|PubMed:10480939, ECO:0000269|PubMed:15292240,
CC ECO:0000269|PubMed:17513500, ECO:0000269|PubMed:20498370,
CC ECO:0000269|PubMed:9878634}.
CC -!- SUBUNIT: Homodimer. Component of the cpSRP complex, composed of a
CC FFC/cpSRP54 monomer and a CAO/cpSRP43 dimer. Interacts (via chromo
CC domains 2 and 3) with ALB3 (via C-terminus), but not with ALB3L1/ALB4.
CC Can interact simultaneously with ALB3 and FFC/cpSRP54. Interacts with
CC LHCP and LTD. {ECO:0000269|PubMed:10480939,
CC ECO:0000269|PubMed:11306572, ECO:0000269|PubMed:15292240,
CC ECO:0000269|PubMed:16183644, ECO:0000269|PubMed:17513500,
CC ECO:0000269|PubMed:18621669, ECO:0000269|PubMed:20018841,
CC ECO:0000269|PubMed:20828566, ECO:0000269|PubMed:21505433}.
CC -!- INTERACTION:
CC O22265; Q8LBP4: ALB3; NbExp=10; IntAct=EBI-780656, EBI-1806831;
CC O22265; O22265: CAO; NbExp=5; IntAct=EBI-780656, EBI-780656;
CC O22265; P37107: FFC; NbExp=21; IntAct=EBI-780656, EBI-780642;
CC O22265; Q8H1G0: GATA28; NbExp=4; IntAct=EBI-780656, EBI-4435064;
CC O22265; P07371: AB80; Xeno; NbExp=7; IntAct=EBI-780656, EBI-2353186;
CC O22265; P27490: CAB8; Xeno; NbExp=4; IntAct=EBI-780656, EBI-8295162;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:9878634}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. Detected in roots.
CC {ECO:0000269|PubMed:16813577, ECO:0000269|PubMed:9878634}.
CC -!- DOMAIN: The binding to LHCP occurs through the first ankyrin repeat and
CC the L18 domain of LHCP.
CC -!- DOMAIN: Homodimerization occurs through both the third and the fourth
CC ankyrin repeats.
CC -!- DOMAIN: Chromo domain 1 may act as a negative regulator of GTP
CC hydrolysis by FFC/cpSRP54. It is unnecessary for targeting complex
CC formation but is required for integration into the thylakoid membrane.
CC -!- DOMAIN: Chromo domain 2 is involved in binding to the M domain of
CC FFC/cpSRP54.
CC -!- DISRUPTION PHENOTYPE: Plants show a reduced level of the major light-
CC harvesting chlorophyll a/b-binding proteins (LHCPs).
CC {ECO:0000269|PubMed:9878634}.
CC -!- MISCELLANEOUS: Unlike eukaryotic or prokaryotic signal recognition
CC particle (SRP), the chloroplast SRP from higher plants lacks an SRP-RNA
CC component. It targets both chloroplast-encoded and nucleus-encoded
CC substrates to the thylakoid membrane, post-translationally for the
CC nucleus-encoded proteins and co-translationally for the chloroplast-
CC encoded proteins.
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DR EMBL; AF013115; AAD01509.1; -; Genomic_DNA.
DR EMBL; AC002535; AAC62865.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10842.1; -; Genomic_DNA.
DR EMBL; AY050442; AAK91457.1; -; mRNA.
DR EMBL; AY054584; AAK96775.1; -; mRNA.
DR EMBL; AY057532; AAL09772.1; -; mRNA.
DR EMBL; AY133540; AAM91370.1; -; mRNA.
DR EMBL; BT002191; AAN72202.1; -; mRNA.
DR PIR; T00439; T00439.
DR RefSeq; NP_566101.1; NM_130313.3.
DR PDB; 1X32; NMR; -; A=84-128.
DR PDB; 1X3P; NMR; -; A=320-373.
DR PDB; 1X3Q; NMR; -; A=265-319.
DR PDB; 2HUG; NMR; -; A=265-319.
DR PDB; 2N88; NMR; -; A=316-373.
DR PDB; 3DEO; X-ray; 1.50 A; A=85-267.
DR PDB; 3DEP; X-ray; 2.70 A; A=85-267.
DR PDB; 3UI2; X-ray; 3.18 A; A=84-327.
DR PDB; 5E4W; X-ray; 2.80 A; C/D=265-369.
DR PDB; 5E4X; X-ray; 2.75 A; A=319-368.
DR PDBsum; 1X32; -.
DR PDBsum; 1X3P; -.
DR PDBsum; 1X3Q; -.
DR PDBsum; 2HUG; -.
DR PDBsum; 2N88; -.
DR PDBsum; 3DEO; -.
DR PDBsum; 3DEP; -.
DR PDBsum; 3UI2; -.
DR PDBsum; 5E4W; -.
DR PDBsum; 5E4X; -.
DR AlphaFoldDB; O22265; -.
DR BMRB; O22265; -.
DR SMR; O22265; -.
DR BioGRID; 4693; 17.
DR DIP; DIP-37639N; -.
DR IntAct; O22265; 22.
DR MINT; O22265; -.
DR STRING; 3702.AT2G47450.1; -.
DR TCDB; 3.A.5.1.2; the general secretory pathway (sec) family.
DR PaxDb; O22265; -.
DR PRIDE; O22265; -.
DR ProteomicsDB; 226859; -.
DR EnsemblPlants; AT2G47450.1; AT2G47450.1; AT2G47450.
DR GeneID; 819358; -.
DR Gramene; AT2G47450.1; AT2G47450.1; AT2G47450.
DR KEGG; ath:AT2G47450; -.
DR Araport; AT2G47450; -.
DR TAIR; locus:2062046; AT2G47450.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_712464_0_0_1; -.
DR OMA; DGHAPSW; -.
DR OrthoDB; 683197at2759; -.
DR PhylomeDB; O22265; -.
DR BRENDA; 3.6.5.4; 399.
DR EvolutionaryTrace; O22265; -.
DR PRO; PR:O22265; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22265; baseline and differential.
DR Genevisible; O22265; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0080085; C:signal recognition particle, chloroplast targeting; IEA:InterPro.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0030674; F:protein-macromolecule adaptor activity; IPI:CAFA.
DR GO; GO:0070208; P:protein heterotrimerization; IMP:CAFA.
DR GO; GO:0045038; P:protein import into chloroplast thylakoid membrane; TAS:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR030300; CPSRP43.
DR PANTHER; PTHR24128:SF43; PTHR24128:SF43; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00298; CHROMO; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54160; SSF54160; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Chloroplast; Coiled coil; Magnesium;
KW Metal-binding; Plastid; Reference proteome; Repeat; Ribonucleoprotein;
KW Signal recognition particle; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..373
FT /note="Signal recognition particle 43 kDa protein,
FT chloroplastic"
FT /id="PRO_0000238461"
FT DOMAIN 84..135
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REPEAT 136..158
FT /note="ANK 1"
FT REPEAT 159..188
FT /note="ANK 2"
FT REPEAT 193..222
FT /note="ANK 3"
FT REPEAT 242..269
FT /note="ANK 4"
FT DOMAIN 270..320
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 321..373
FT /note="Chromo 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 65..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..79
FT /evidence="ECO:0000255"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 161
FT /note="R->A: Decreased interaction with LHCP."
FT /evidence="ECO:0000269|PubMed:18621669"
FT MUTAGEN 192
FT /note="R->A: Decreased interaction with LHCP."
FT /evidence="ECO:0000269|PubMed:18621669"
FT MUTAGEN 204
FT /note="Y->A: Loss of interaction with LHCP."
FT /evidence="ECO:0000269|PubMed:18621669"
FT MUTAGEN 226
FT /note="R->A: Decreased interaction with LHCP."
FT /evidence="ECO:0000269|PubMed:18621669"
FT MUTAGEN 269
FT /note="Y->A: Decreased interaction with ALB3."
FT /evidence="ECO:0000269|PubMed:20018841"
FT MUTAGEN 291
FT /note="W->A: Decreased interaction with ALB3."
FT /evidence="ECO:0000269|PubMed:20018841"
FT MUTAGEN 293
FT /note="D->A: Decreased interaction with ALB3."
FT /evidence="ECO:0000269|PubMed:20018841"
FT CONFLICT 35
FT /note="S -> SSSS (in Ref. 1; AAD01509)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> V (in Ref. 4; AAK96775/AAN72202)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="R -> K (in Ref. 1; AAD01509)"
FT /evidence="ECO:0000305"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:3DEO"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3DEO"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:3DEO"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:1X32"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:3DEO"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:3DEO"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:3DEO"
FT HELIX 246..263
FT /evidence="ECO:0007829|PDB:3DEO"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5E4W"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:5E4W"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:5E4W"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:5E4W"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5E4W"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:5E4W"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5E4W"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:5E4X"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1X3P"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:5E4X"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:1X3P"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:5E4W"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:5E4X"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:5E4X"
SQ SEQUENCE 373 AA; 41279 MW; F75ED9C7046A1441 CRC64;
MQKVFLAMDT CALVIHQSLS RIKLSPPKSS SSSSSAFSPE SLPIRRIELC FRGAICAAVQ
RNYEETTSSV EEAEEDDESS SSYGEVNKII GSRTAGEGAM EYLIEWKDGH SPSWVPSSYI
AADVVSEYET PWWTAARKAD EQALSQLLED RDVDAVDENG RTALLFVAGL GSDKCVRLLA
EAGADLDHRD MRGGLTALHM AAGYVRPEVV EALVELGADI EVEDERGLTA LELAREILKT
TPKGNPMQFG RRIGLEKVIN VLEGQVFEYA EVDEIVEKRG KGKDVEYLVR WKDGGDCEWV
KGVHVAEDVA KDYEDGLEYA VAESVIGKRV GDDGKTIEYL VKWTDMSDAT WEPQDNVDST
LVLLYQQQQP MNE
