ID CLPC2_ARATH Reviewed; 952 AA.
AC Q9SXJ7; A0A1I9LLC3; Q93ZM4; Q9M2Z6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 155.
DE RecName: Full=Chaperone protein ClpC2, chloroplastic {ECO:0000303|PubMed:11299370};
DE EC=3.6.1.- {ECO:0000269|PubMed:21737456};
DE AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC homolog 2;
DE AltName: Full=AtClpC;
DE AltName: Full=Casein lytic proteinase C2;
DE Flags: Precursor;
GN Name=CLPC2 {ECO:0000303|PubMed:11299370};
GN Synonyms=HSP93-III {ECO:0000303|PubMed:17376159};
GN OrderedLocusNames=At3g48870 {ECO:0000312|Araport:AT3G48870};
GN ORFNames=T21J18.140 {ECO:0000312|EMBL:CAB87915.1};
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, AND INDUCTION BY
RP SENESCENCE.
RC STRAIN=cv. Columbia;
RX PubMed=10427773; DOI=10.1093/oxfordjournals.pcp.a029571;
RA Nakabayashi K., Ito M., Kiyosue T., Shinozaki K., Watanabe A.;
RT "Identification of clp genes expressed in senescing Arabidopsis leaves.";
RL Plant Cell Physiol. 40:504-514(1999).
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 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 [6]
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 [7]
RP NOMENCLATURE.
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 [8]
RP TISSUE SPECIFICITY.
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 [9]
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 [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21737456; DOI=10.1074/jbc.m110.211946;
RA Rosano G.L., Bruch E.M., Ceccarelli E.A.;
RT "Insights into the Clp/HSP100 chaperone system from chloroplasts of
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 286:29671-29680(2011).
RN [12]
RP FUNCTION.
RX PubMed=22545953; DOI=10.1186/1471-2229-12-57;
RA Bruch E.M., Rosano G.L., Ceccarelli E.A.;
RT "Chloroplastic Hsp100 chaperones ClpC2 and ClpD interact in vitro with a
RT transit peptide only when it is located at the N-terminus of a protein.";
RL BMC Plant Biol. 12:57-57(2012).
RN [13]
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 [14]
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 [15]
RP INTERACTION WITH CLPT1.
RX PubMed=25149061; DOI=10.1186/s12870-014-0228-0;
RA Colombo C.V., Ceccarelli E.A., Rosano G.L.;
RT "Characterization of the accessory protein ClpT1 from Arabidopsis thaliana:
RT oligomerization status and interaction with Hsp100 chaperones.";
RL BMC Plant Biol. 14:228-228(2014).
RN [16]
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 [17]
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 (PubMed:15304652, PubMed:21737456,
CC PubMed:24599948). May act as a suppressor of FtsH-mediated thylakoid
CC membrane biogenesis and may enhance photoinhibition (PubMed:15304652).
CC Seems not involved in chloroplastic protein import (PubMed:15304652).
CC Probable component of the TIC-associated stromal import motor involved
CC in inner membrane translocation (PubMed:17376159). Has an ATPase
CC activity, but no ADPase activity (PubMed:21737456). Interacts with
CC transit peptides with a positional preference (PubMed:21737456,
CC PubMed:22545953). Localization of the signal sequence at the N-terminal
CC end of a protein seems mandatory for interaction to take place
CC (PubMed:22545953). {ECO:0000269|PubMed:15304652,
CC ECO:0000269|PubMed:17376159, ECO:0000269|PubMed:21737456,
CC ECO:0000269|PubMed:22545953, ECO:0000269|PubMed:24599948}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:21737456};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21737456};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.42 mM for ATP {ECO:0000269|PubMed:21737456};
CC Vmax=0.62 nmol/min/ug enzyme {ECO:0000269|PubMed:21737456};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:21737456};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:21737456};
CC -!- SUBUNIT: Homodimer and homohexamer (PubMed:21737456). Hexamerization
CC upon addition of ATP (PubMed:21737456). Interacts with CLPT1
CC (PubMed:25149061). Interacts with CLPS1 (PubMed:23898032). Stably
CC associated with the import machinery (PubMed:21737456). Interacts with
CC CLPF (PubMed:26419670). {ECO:0000269|PubMed:21737456,
CC ECO:0000269|PubMed:23898032, ECO:0000269|PubMed:25149061,
CC ECO:0000269|PubMed:26419670}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:10427773, ECO:0000269|PubMed:21737456,
CC ECO:0000269|PubMed:24599948}. Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:21737456, ECO:0000269|PubMed:24599948}.
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=Q9SXJ7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots and inflorescences
CC (PubMed:15659100). Expressed at very low levels in rosette leaves
CC (PubMed:15659100). Expressed in photosynthetic green tissues with high
CC levels in young, developing leaf tissues (PubMed:23898032).
CC {ECO:0000269|PubMed:15659100, ECO:0000269|PubMed:23898032}.
CC -!- INDUCTION: By senescence. Not induced by heat stress.
CC {ECO:0000269|PubMed:10427773, ECO:0000269|PubMed:17144892}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:17376159). Clpc1 and
CC clpc2 double mutants are embryo lethal when homozygous
CC (PubMed:17376159). {ECO:0000269|PubMed:17376159}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL10478.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB022324; BAA82062.1; -; mRNA.
DR EMBL; AL132963; CAB87915.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78466.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63380.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63381.1; -; Genomic_DNA.
DR EMBL; AY056787; AAL10478.1; ALT_FRAME; mRNA.
DR PIR; T49283; T49283.
DR PIR; T52456; T52456.
DR RefSeq; NP_001325472.1; NM_001339385.1. [Q9SXJ7-1]
DR RefSeq; NP_001325473.1; NM_001339386.1. [Q9SXJ7-1]
DR RefSeq; NP_566912.2; NM_114746.5. [Q9SXJ7-1]
DR AlphaFoldDB; Q9SXJ7; -.
DR SMR; Q9SXJ7; -.
DR BioGRID; 9366; 3.
DR IntAct; Q9SXJ7; 3.
DR MINT; Q9SXJ7; -.
DR STRING; 3702.Q9SXJ7; -.
DR TCDB; 3.A.9.1.2; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR MetOSite; Q9SXJ7; -.
DR SwissPalm; Q9SXJ7; -.
DR PaxDb; 3702-AT3G48870-1; -.
DR EnsemblPlants; AT3G48870.1; AT3G48870.1; AT3G48870. [Q9SXJ7-1]
DR EnsemblPlants; AT3G48870.3; AT3G48870.3; AT3G48870. [Q9SXJ7-1]
DR EnsemblPlants; AT3G48870.4; AT3G48870.4; AT3G48870. [Q9SXJ7-1]
DR GeneID; 824048; -.
DR Gramene; AT3G48870.1; AT3G48870.1; AT3G48870. [Q9SXJ7-1]
DR Gramene; AT3G48870.3; AT3G48870.3; AT3G48870. [Q9SXJ7-1]
DR Gramene; AT3G48870.4; AT3G48870.4; AT3G48870. [Q9SXJ7-1]
DR KEGG; ath:AT3G48870; -.
DR Araport; AT3G48870; -.
DR TAIR; AT3G48870; HSP93-III.
DR eggNOG; KOG1051; Eukaryota.
DR InParanoid; Q9SXJ7; -.
DR OrthoDB; 275944at2759; -.
DR PhylomeDB; Q9SXJ7; -.
DR BRENDA; 7.4.2.4; 399.
DR PRO; PR:Q9SXJ7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SXJ7; baseline and differential.
DR Genevisible; Q9SXJ7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; ISS:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; ISS:TAIR.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 1.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 Alternative splicing; ATP-binding; Chaperone; Chloroplast; Hydrolase;
KW Membrane; Nucleotide-binding; Plastid; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..952
FT /note="Chaperone protein ClpC2, chloroplastic"
FT /id="PRO_0000412576"
FT DOMAIN 115..257
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT DOMAIN 532..567
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 118..183
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 193..257
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 278..525
FT /note="I"
FT /evidence="ECO:0000250"
FT REGION 592..783
FT /note="II"
FT /evidence="ECO:0000250"
FT BINDING 323..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 666..673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 307
FT /note="V -> M (in Ref. 2; CAB87915)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="E -> G (in Ref. 4; AAL10478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 952 AA; 105739 MW; F6BD9C64FE6A6F87 CRC64;
MAWSIALLTP PFFGPGRHVQ AKEYREPRGC VMKMSSLKAP VLRIQATEYR EPRGRVKMMS
SLQAPLLTIQ SFSGLRAPSA LDYLGRPSPG FLVKYKLAKS SGREKASRCV PKAMFERFTE
KAIKVIMLSQ EEARRLGHNF VGTEQILLGL IGEGTGIAAK VLKSMGINLK DSRVEVEKII
GRGSGFVAVE IPFTPRAKRV LELSLEEARQ LGHNYIGSEH LLLGLLREGE GVAARVLENL
GADPSNIRTQ VIRMVGENNE VTASVGGGSS GNSKMPTLEE YGTNLTKLAE EGKLDPVVGR
QPQIERVVQI LARRTKNNPC LIGEPGVGKT AIAEGLAQRI ASGDVPETIE GKTVITLDMG
LLVAGTKYRG EFEERLKKLM EEIRQSDEII LFIDEVHTLI GAGAAEGAID AANILKPALA
RGELQCIGAT TIDEYRKHIE KDPALERRFQ PVKVPEPTVE EAIQILQGLR ERYEIHHKLR
YTDEALVAAA QLSHQYISDR FLPDKAIDLI DEAGSRVRLR HAQLPEEARE LEKQLRQITK
EKNEAVRSQD FEMAGSHRDR EIELKAEIAN VLSRGKEVAK AENEAEEGGP TVTESDIQHI
VATWTGIPVE KVSSDESSRL LQMEQTLHTR VIGQDEAVKA ISRAIRRARV GLKNPNRPIA
SFIFSGPTGV GKSELAKALA AYYFGSEEAM IRLDMSEFME RHTVSKLIGS PPGYVGYTEG
GQLTEAVRRR PYTLVLFDEI EKAHPDVFNM MLQILEDGRL TDSKGRTVDF KNTLLIMTSN
VGSSVIEKGG RRIGFDLDHD EKDSSYNRIK SLVTEELKQY FRPEFLNRLD EMIVFRQLTK
LEVKEIADIM LKEVVARLEV KEIELQVTER FKERVVDEGF DPSYGARPLR RAIMRLLEDS
MAEKMLSRDI KEGDSVIVDV DAEGSVVVLS GTTGRVGGFA AEEAMEDPIP IL
//
