CLPC1_ARATH
ID CLPC1_ARATH Reviewed; 929 AA.
AC Q9FI56; O48931;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Chaperone protein ClpC1, chloroplastic {ECO:0000303|PubMed:11299370};
DE AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC homolog 1;
DE AltName: Full=Casein lytic proteinase C1;
DE AltName: Full=Protein DE-REGULATED CAO ACCUMULATION 1;
DE AltName: Full=Protein IRON-RESCUED MUTANT 1;
DE Flags: Precursor;
GN Name=CLPC1 {ECO:0000303|PubMed:11299370};
GN Synonyms=DCA1, HSP93-V {ECO:0000303|PubMed:22353577}, IRM1;
GN OrderedLocusNames=At5g50920 {ECO:0000312|Araport:AT5G50920};
GN ORFNames=K3K7.7 {ECO:0000312|EMBL:BAB08738.1};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=11982939; DOI=10.1034/j.1399-3054.2002.1140113.x;
RA Zheng B., Halperin T., Hruskova-Heidingsfeldova O., Adam Z., Clarke A.K.;
RT "Characterization of chloroplast Clp proteins in Arabidopsis: localization,
RT tissue specificity and stress responses.";
RL Physiol. Plantarum 114:92-101(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11299370; DOI=10.1104/pp.125.4.1912;
RA Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
RA Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K.;
RT "Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
RT nomenclature.";
RL Plant Physiol. 125:1912-1918(2001).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14593120; DOI=10.1074/jbc.m309212200;
RA Peltier J.-B., Ripoll D.R., Friso G., Rudella A., Cai Y., Ytterberg J.,
RA Giacomelli L., Pillardy J., van Wijk K.J.;
RT "Clp protease complexes from photosynthetic and non-photosynthetic plastids
RT and mitochondria of plants, their predicted three-dimensional structures,
RT and functional implications.";
RL J. Biol. Chem. 279:4768-4781(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15516497; DOI=10.1104/pp.104.052928;
RA Constan D., Froehlich J.E., Rangarajan S., Keegstra K.;
RT "A stromal Hsp100 protein is required for normal chloroplast development
RT and function in Arabidopsis.";
RL Plant Physiol. 136:3605-3615(2004).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=15563614; DOI=10.1104/pp.104.053835;
RA Sjoegren L.L., MacDonald T.M., Sutinen S., Clarke A.K.;
RT "Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular
RT chaperone causes growth retardation, leaf chlorosis, lower photosynthetic
RT activity, and a specific reduction in photosystem content.";
RL Plant Physiol. 136:4114-4126(2004).
RN [10]
RP FUNCTION.
RX PubMed=15304652; DOI=10.1073/pnas.0402764101;
RA Park S., Rodermel S.R.;
RT "Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid
RT membrane biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12765-12770(2004).
RN [11]
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX DOI=10.1111/j.1399-3054.2005.00452.x;
RA Clarke A.K., MacDonald T.M., Sjoegren L.L.;
RT "The ATP-dependent Clp protease in chloroplasts of higher plants.";
RL Physiol. Plantarum 123:406-412(2005).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15659100; DOI=10.1111/j.1365-313x.2004.02307.x;
RA Kovacheva S., Bedard J., Patel R., Dudley P., Twell D., Rios G., Koncz C.,
RA Jarvis P.;
RT "In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast
RT protein import.";
RL Plant J. 41:412-428(2005).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17376159; DOI=10.1111/j.1365-313x.2007.03060.x;
RA Kovacheva S., Bedard J., Wardle A., Patel R., Jarvis P.;
RT "Further in vivo studies on the role of the molecular chaperone, Hsp93, in
RT plastid protein import.";
RL Plant J. 50:364-379(2007).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17291312; DOI=10.1111/j.1365-313x.2006.02996.x;
RA Nakagawara E., Sakuraba Y., Yamasato A., Tanaka R., Tanaka A.;
RT "Clp protease controls chlorophyll b synthesis by regulating the level of
RT chlorophyllide a oxygenase.";
RL Plant J. 49:800-809(2007).
RN [15]
RP INDUCTION.
RX PubMed=17144892; DOI=10.1111/j.1365-313x.2006.02940.x;
RA Lee U., Rioflorido I., Hong S.W., Larkindale J., Waters E.R., Vierling E.;
RT "The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and
RT chloroplast development.";
RL Plant J. 49:115-127(2007).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-773.
RX PubMed=20382967; DOI=10.1093/aob/mcq051;
RA Wu H., Ji Y., Du J., Kong D., Liang H., Ling H.Q.;
RT "ClpC1, an ATP-dependent Clp protease in plastids, is involved in iron
RT homeostasis in Arabidopsis leaves.";
RL Ann. Bot. 105:823-833(2010).
RN [17]
RP FUNCTION, AND DOMAIN.
RX PubMed=22353577; DOI=10.1104/pp.112.193300;
RA Chu C.C., Li H.M.;
RT "The amino-terminal domain of chloroplast Hsp93 is important for its
RT membrane association and functions in vivo.";
RL Plant Physiol. 158:1656-1665(2012).
RN [18]
RP REVIEW.
RX PubMed=22085372; DOI=10.1111/j.1399-3054.2011.01541.x;
RA Clarke A.K.;
RT "The chloroplast ATP-dependent Clp protease in vascular plants - new
RT dimensions and future challenges.";
RL Physiol. Plantarum 145:235-244(2012).
RN [19]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CLPS1.
RX PubMed=23898032; DOI=10.1105/tpc.113.112557;
RA Nishimura K., Asakura Y., Friso G., Kim J., Oh S.H., Rutschow H.,
RA Ponnala L., van Wijk K.J.;
RT "ClpS1 is a conserved substrate selector for the chloroplast Clp protease
RT system in Arabidopsis.";
RL Plant Cell 25:2276-2301(2013).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24599948; DOI=10.1074/jbc.m113.534552;
RA Sjoegren L.L., Tanabe N., Lymperopoulos P., Khan N.Z., Rodermel S.R.,
RA Aronsson H., Clarke A.K.;
RT "Quantitative analysis of the chloroplast molecular chaperone ClpC/Hsp93 in
RT Arabidopsis reveals new insights into its localization, interaction with
RT the Clp proteolytic core, and functional importance.";
RL J. Biol. Chem. 289:11318-11330(2014).
RN [21]
RP INTERACTION WITH CLPF.
RX PubMed=26419670; DOI=10.1105/tpc.15.00574;
RA Nishimura K., Apitz J., Friso G., Kim J., Ponnala L., Grimm B.,
RA van Wijk K.J.;
RT "Discovery of a unique Clp Component, ClpF, in chloroplasts: A proposed
RT binary ClpF-ClpS1 adaptor complex functions in substrate recognition and
RT delivery.";
RL Plant Cell 27:2677-2691(2015).
CC -!- FUNCTION: Molecular chaperone that hydrolyzes ATP and is associated
CC with the chloroplast protein import apparatus. May function as the
CC motor for chloroplast protein translocation, as translocation requires
CC ATP hydrolysis in the stroma. May interact with a ClpP-like protease
CC involved in degradation of denatured proteins in the chloroplast.
CC Involved in the regulation of chlorophyll b biosynthesis through the
CC destabilization of chlorophyllide a oxygenase (CAO) protein in response
CC to the accumulation of chlorophyll b. Involved in leaf iron
CC homeostasis. {ECO:0000269|PubMed:15304652, ECO:0000269|PubMed:15516497,
CC ECO:0000269|PubMed:15659100, ECO:0000269|PubMed:17291312,
CC ECO:0000269|PubMed:17376159, ECO:0000269|PubMed:20382967,
CC ECO:0000269|PubMed:22353577, ECO:0000269|PubMed:24599948}.
CC -!- SUBUNIT: Homodimer (PubMed:14593120). May form hexamer and interact
CC with Clp core (PubMed:14593120). Interacts (via N-terminus) with CLPS1
CC (PubMed:23898032). Interacts with CLPF (PubMed:26419670).
CC {ECO:0000269|PubMed:14593120, ECO:0000269|PubMed:23898032,
CC ECO:0000269|PubMed:26419670}.
CC -!- INTERACTION:
CC Q9FI56; Q8LPR9: TIC110; NbExp=4; IntAct=EBI-2297694, EBI-639092;
CC Q9FI56; Q9FMD5: TIC40; NbExp=3; IntAct=EBI-2297694, EBI-639157;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:14593120,
CC ECO:0000269|PubMed:20382967, ECO:0000269|PubMed:24599948}. Plastid,
CC chloroplast membrane {ECO:0000269|PubMed:24599948}. Note=The membrane
CC association is important for the in vivo functions.
CC {ECO:0000269|PubMed:24599948}.
CC -!- TISSUE SPECIFICITY: Highly expressed in rosette leaves. Expressed in
CC roots, stems and inflorescences (PubMed:11982939, PubMed:15659100,
CC PubMed:20382967). Expressed in photosynthetic green tissues with high
CC levels in young, developing leaf tissues (PubMed:23898032).
CC {ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:15659100,
CC ECO:0000269|PubMed:20382967, ECO:0000269|PubMed:23898032}.
CC -!- INDUCTION: By cold and salt stresses. Not induced by heat stress.
CC {ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:17144892}.
CC -!- DOMAIN: The Clp repeat (R) domain is important for membrane association
CC and is essential for the in vivo functions, but not for the ATPase
CC activity. {ECO:0000269|PubMed:22353577}.
CC -!- DISRUPTION PHENOTYPE: Small plants with chlorotic leaves, aberrant
CC chloroplast biogenesis and inefficient chloroplast import of both
CC photosynthetic and non-photosynthetic preproteins (PubMed:15516497,
CC PubMed:15563614, Ref.11, PubMed:15659100, PubMed:17376159,
CC PubMed:17291312, PubMed:20382967). Clpc1 and clpc2 double mutants are
CC embryo lethal when homozygous (PubMed:17376159).
CC {ECO:0000269|PubMed:15516497, ECO:0000269|PubMed:15563614,
CC ECO:0000269|PubMed:15659100, ECO:0000269|PubMed:17291312,
CC ECO:0000269|PubMed:17376159, ECO:0000269|PubMed:20382967,
CC ECO:0000269|Ref.11}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC {ECO:0000305}.
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DR EMBL; AF022909; AAC04687.1; -; mRNA.
DR EMBL; AB017063; BAB08738.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96011.1; -; Genomic_DNA.
DR EMBL; AY102125; AAM26692.1; -; mRNA.
DR EMBL; AK227173; BAE99213.1; -; mRNA.
DR PIR; T52292; T52292.
DR RefSeq; NP_568746.1; NM_124471.4.
DR PDB; 5GUI; X-ray; 1.20 A; A=94-238.
DR PDBsum; 5GUI; -.
DR AlphaFoldDB; Q9FI56; -.
DR SMR; Q9FI56; -.
DR BioGRID; 20411; 3.
DR IntAct; Q9FI56; 5.
DR STRING; 3702.AT5G50920.1; -.
DR TCDB; 3.A.9.1.2; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR MetOSite; Q9FI56; -.
DR PaxDb; Q9FI56; -.
DR PRIDE; Q9FI56; -.
DR ProteomicsDB; 246585; -.
DR EnsemblPlants; AT5G50920.1; AT5G50920.1; AT5G50920.
DR GeneID; 835165; -.
DR Gramene; AT5G50920.1; AT5G50920.1; AT5G50920.
DR KEGG; ath:AT5G50920; -.
DR Araport; AT5G50920; -.
DR TAIR; locus:2157383; AT5G50920.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_1_1; -.
DR InParanoid; Q9FI56; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 611758at2759; -.
DR PhylomeDB; Q9FI56; -.
DR BRENDA; 7.4.2.4; 399.
DR PRO; PR:Q9FI56; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI56; baseline and differential.
DR Genevisible; Q9FI56; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0031897; C:Tic complex; TAS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
DR GO; GO:0045036; P:protein targeting to chloroplast; IMP:TAIR.
DR GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:TAIR.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Chloroplast; Membrane;
KW Nucleotide-binding; Plastid; Protein transport; Reference proteome; Repeat;
KW Transit peptide; Transport.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..929
FT /note="Chaperone protein ClpC1, chloroplastic"
FT /id="PRO_0000412575"
FT DOMAIN 95..237
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT DOMAIN 511..546
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 98..163
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 173..237
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 257..504
FT /note="I"
FT /evidence="ECO:0000250"
FT REGION 552..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..762
FT /note="II"
FT /evidence="ECO:0000250"
FT REGION 908..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 645..652
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 773
FT /note="G->R: In irm1; iron deficiency chlorosis."
FT /evidence="ECO:0000269|PubMed:20382967"
FT CONFLICT 40..48
FT /note="SQLQVSGLR -> IIFNVWLP (in Ref. 1; AAC04687)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..188
FT /note="EA -> AT (in Ref. 1; AAC04687)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="A -> V (in Ref. 1; AAC04687)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="K -> T (in Ref. 1; AAC04687)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="P -> L (in Ref. 1; AAC04687)"
FT /evidence="ECO:0000305"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:5GUI"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:5GUI"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:5GUI"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:5GUI"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:5GUI"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5GUI"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:5GUI"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:5GUI"
FT HELIX 224..237
FT /evidence="ECO:0007829|PDB:5GUI"
SQ SEQUENCE 929 AA; 103453 MW; 438DEA514125F0BF CRC64;
MAMATRVLAQ STPPSLACYQ RNVPSRGSGR SRRSVKMMCS QLQVSGLRMQ GFMGLRGNNA
LDTLGKSRQD FHSKVRQAMN VPKGKASRFT VKAMFERFTE KAIKVIMLAQ EEARRLGHNF
VGTEQILLGL IGEGTGIAAK VLKSMGINLK DARVEVEKII GRGSGFVAVE IPFTPRAKRV
LELSLEEARQ LGHNYIGSEH LLLGLLREGE GVAARVLENL GADPSNIRTQ VIRMVGENNE
VTANVGGGSS SNKMPTLEEY GTNLTKLAEE GKLDPVVGRQ PQIERVVQIL GRRTKNNPCL
IGEPGVGKTA IAEGLAQRIA SGDVPETIEG KKVITLDMGL LVAGTKYRGE FEERLKKLME
EIRQSDEIIL FIDEVHTLIG AGAAEGAIDA ANILKPALAR GELQCIGATT LDEYRKHIEK
DPALERRFQP VKVPEPTVDE TIQILKGLRE RYEIHHKLRY TDESLVAAAQ LSYQYISDRF
LPDKAIDLID EAGSRVRLRH AQVPEEAREL EKELRQITKE KNEAVRGQDF EKAGTLRDRE
IELRAEVSAI QAKGKEMSKA ESETGEEGPM VTESDIQHIV SSWTGIPVEK VSTDESDRLL
KMEETLHKRI IGQDEAVKAI SRAIRRARVG LKNPNRPIAS FIFSGPTGVG KSELAKALAA
YYFGSEEAMI RLDMSEFMER HTVSKLIGSP PGYVGYTEGG QLTEAVRRRP YTVVLFDEIE
KAHPDVFNMM LQILEDGRLT DSKGRTVDFK NTLLIMTSNV GSSVIEKGGR RIGFDLDYDE
KDSSYNRIKS LVTEELKQYF RPEFLNRLDE MIVFRQLTKL EVKEIADILL KEVFERLKKK
EIELQVTERF KERVVDEGYN PSYGARPLRR AIMRLLEDSM AEKMLAREIK EGDSVIVDVD
AEGNVTVLNG GSGTPTTSLE EQEDSLPVA
