ARC3_ARATH
ID ARC3_ARATH Reviewed; 741 AA.
AC Q6F6B5; Q0WT28; Q9C9P7; Q9SSG9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3, chloroplastic {ECO:0000303|PubMed:15356321};
DE Flags: Precursor;
GN Name=ARC3 {ECO:0000303|PubMed:15356321};
GN OrderedLocusNames=At1g75010 {ECO:0000312|Araport:AT1G75010};
GN ORFNames=F25A4.3 {ECO:0000312|EMBL:AAD55276.1},
GN F9E10.14 {ECO:0000312|EMBL:AAG51935.1};
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], FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=15356321; DOI=10.1093/pcp/pch130;
RA Shimada H., Koizumi M., Kuroki K., Mochizuki M., Fujimoto H., Ohta H.,
RA Masuda T., Takamiya K.;
RT "ARC3, a chloroplast division factor, is a chimera of prokaryotic FtsZ and
RT part of eukaryotic phosphatidylinositol-4-phosphate 5-kinase.";
RL Plant Cell Physiol. 45:960-967(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] OF 280-741.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=10417716; DOI=10.1046/j.1365-313x.1999.00500.x;
RA Marrison J.L., Rutherford S.M., Robertson E.J., Lister C., Dean C.,
RA Leech R.M.;
RT "The distinctive roles of five different ARC genes in the chloroplast
RT division process in Arabidopsis.";
RL Plant J. 18:651-662(1999).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH FTSZ1; MIND1 AND MINE1,
RP SELF-INTERACTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17304239; DOI=10.1038/sj.embor.7400902;
RA Maple J., Vojta L., Soll J., Moeller S.G.;
RT "ARC3 is a stromal Z-ring accessory protein essential for plastid
RT division.";
RL EMBO Rep. 8:293-299(2007).
RN [7]
RP REVIEW.
RX PubMed=17451550; DOI=10.1111/j.1600-0854.2007.00545.x;
RA Glynn J.M., Miyagishima S.-Y., Yoder D.W., Osteryoung K.W., Vitha S.;
RT "Chloroplast division.";
RL Traffic 8:451-461(2007).
RN [8]
RP SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=18284374; DOI=10.1042/bj20071354;
RA McAndrew R.S., Olson B.J., Kadirjan-Kalbach D.K., Chi-Ham C.L., Vitha S.,
RA Froehlich J.E., Osteryoung K.W.;
RT "In vivo quantitative relationship between plastid division proteins FtsZ1
RT and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ complex.";
RL Biochem. J. 412:367-378(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=18764889; DOI=10.1111/j.1751-1097.2008.00437.x;
RA Holzinger A., Kwok E.Y., Hanson M.R.;
RT "Effects of arc3, arc5 and arc6 mutations on plastid morphology and
RT stromule formation in green and nongreen tissues of Arabidopsis thaliana.";
RL Photochem. Photobiol. 84:1324-1335(2008).
RN [10]
RP INTERACTION WITH CDP1, AND SELF-INTERACTION.
RX PubMed=19564892; DOI=10.1038/cr.2009.78;
RA Zhang M., Hu Y., Jia J., Li D., Zhang R., Gao H., He Y.;
RT "CDP1, a novel component of chloroplast division site positioning system in
RT Arabidopsis.";
RL Cell Res. 19:877-886(2009).
RN [11]
RP INTERACTION WITH CDP1.
RX PubMed=19453460; DOI=10.1111/j.1365-313x.2009.03905.x;
RA Glynn J.M., Yang Y., Vitha S., Schmitz A.J., Hemmes M., Miyagishima S.-Y.,
RA Osteryoung K.W.;
RT "PARC6, a novel chloroplast division factor, influences FtsZ assembly and
RT is required for recruitment of PDV1 during chloroplast division in
RT Arabidopsis.";
RL Plant J. 59:700-711(2009).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=23936263; DOI=10.1371/journal.pone.0071190;
RA Wang P., Zhang J., Su J., Wang P., Liu J., Liu B., Feng D., Wang J.,
RA Wang H.;
RT "The chloroplast min system functions differentially in two specific
RT nongreen plastids in Arabidopsis thaliana.";
RL PLoS ONE 8:e71190-e71190(2013).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=25731613; DOI=10.1017/s1431927615000082;
RA Johnson C.B., Shaik R., Abdallah R., Vitha S., Holzenburg A.;
RT "FtsZ1/FtsZ2 turnover in chloroplasts and the role of ARC3.";
RL Microsc. Microanal. 21:313-323(2015).
RN [14]
RP INTERACTION WITH CDP1/PARC6, AND DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=26527658; DOI=10.1104/pp.15.01460;
RA Zhang M., Chen C., Froehlich J.E., TerBush A.D., Osteryoung K.W.;
RT "Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division
RT Complex and Negative Regulation of FtsZ Assembly.";
RL Plant Physiol. 170:250-262(2016).
RN [15]
RP FUNCTION, DOMAIN, AND INTERACTION WITH FTSZ2-1 AND ARC6.
RX PubMed=29138260; DOI=10.1042/bcj20170697;
RA Shaik R.S., Sung M.W., Vitha S., Holzenburg A.;
RT "Chloroplast division protein ARC3 acts on FtsZ2 by preventing filament
RT bundling and enhancing GTPase activity.";
RL Biochem. J. 475:99-115(2018).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=29967285; DOI=10.1105/tpc.18.00189;
RA Chen L., Sun B., Gao W., Zhang Q.Y., Yuan H., Zhang M.;
RT "MCD1 associates with FtsZ filaments via the membrane-tethering protein
RT ARC6 to guide chloroplast division.";
RL Plant Cell 30:1807-1823(2018).
RN [17]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=30252596; DOI=10.1080/15592324.2018.1517075;
RA Abolhassani Rad S., Clayton E.J., Cornelius E.J., Howes T.R., Kohalmi S.E.;
RT "Moonlighting proteins: putting the spotlight on enzymes.";
RL Plant Signal. Behav. 13:e1517075-e1517075(2018).
RN [18]
RP FUNCTION, MUTAGENESIS OF GLY-632; GLY-641; GLY-643; GLY-655; GLY-664 AND
RP GLY-666, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP INTERACTION WITH FTSZ2-1 AND FTSZ1.
RC STRAIN=cv. Columbia;
RX PubMed=30824505; DOI=10.1105/tpc.18.00948;
RA Chen C., Cao L., Yang Y., Porter K.J., Osteryoung K.W.;
RT "ARC3 activation by PARC6 promotes FtsZ-ring remodeling at the chloroplast
RT division site.";
RL Plant Cell 31:862-885(2019).
CC -!- FUNCTION: Together with MIND1 and MCD1, regulates FtsZ ring positioning
CC in chloroplasts in an ARC6-dependent manner (PubMed:29967285). Z-ring
CC accessory protein involved in the initiation of plastid division and
CC division site placement (might functionally replace bacterial MinC)
CC (PubMed:23936263). Acts as a disassembly factor that accelerates
CC fragmentation and depolymerization of existing FtsZ2 filaments by
CC enhancing FTSZ2 GTPase activity, thus leading to the conversion of
CC FTSZ2 bound GTP into GDP, a process which triggers FtsZ2 filaments
CC destabilization (PubMed:29138260, PubMed:25731613). Prevents misplaced
CC Z-ring formation at chloroplast stroma nondivision sites
CC (PubMed:30824505). May control the rate of chloroplast expansion. Seems
CC to influence stromule (stroma-filled tubular extensions of the plastid
CC envelope membrane) length and frequency. {ECO:0000269|PubMed:10417716,
CC ECO:0000269|PubMed:15356321, ECO:0000269|PubMed:17304239,
CC ECO:0000269|PubMed:18764889, ECO:0000269|PubMed:23936263,
CC ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29138260,
CC ECO:0000269|PubMed:29967285, ECO:0000269|PubMed:30824505}.
CC -!- SUBUNIT: Self-interacts. Interacts with FTSZ, CDP1/PARC6 (via N-
CC terminus), MIND1 and MINE1 (PubMed:26527658, PubMed:30824505). Part of
CC a complex made of ARC3, ARC6, FTSZ1 and FTSZ2 (PubMed:30824505).
CC Recruited to the middle of the plastid by CDP1/PARC6 where subsequent
CC complex made of CDP1/PARC6, ARC3 and FtsZ proteins can form; this
CC complex enhances the dynamics of Z rings during chloroplast division
CC (PubMed:30824505). Binding to FTSZ2-1 is enabled by ARC6
CC (PubMed:29138260). {ECO:0000269|PubMed:17304239,
CC ECO:0000269|PubMed:18284374, ECO:0000269|PubMed:19453460,
CC ECO:0000269|PubMed:19564892, ECO:0000269|PubMed:26527658,
CC ECO:0000269|PubMed:29138260, ECO:0000269|PubMed:30824505}.
CC -!- INTERACTION:
CC Q6F6B5; Q8VY16: CDP1; NbExp=4; IntAct=EBI-2367605, EBI-2349234;
CC Q6F6B5; Q9C4Z7: MINE1; NbExp=3; IntAct=EBI-2367605, EBI-2119860;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:15356321}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15356321}; Cytoplasmic side
CC {ECO:0000269|PubMed:15356321}. Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:17304239}. Note=Distributed in two pools, a first
CC one throughout the stroma, probably to inhibits Z-ring assembly at
CC nondivision sites, and a second one localized to a midplastid ring-like
CC structure (PubMed:30824505). Located at the site of chloroplast
CC division on the outer surface in a ring-shaped structure at the early
CC and middle stages of the process according to PubMed:15356321. Forms
CC ring-like structures, short filaments and discrete foci in the
CC chloroplast stroma according to PubMed:17304239 (PubMed:17304239,
CC PubMed:15356321). {ECO:0000269|PubMed:15356321,
CC ECO:0000269|PubMed:17304239, ECO:0000269|PubMed:30824505}.
CC -!- DOMAIN: MORN domains promote interaction with ARC6 and CDP1/PARC6 but
CC prevent binding to FTSZ1, FTSZ2, MIND and MINE proteins.
CC {ECO:0000269|PubMed:26527658, ECO:0000269|PubMed:30824505,
CC ECO:0000303|PubMed:29138260}.
CC -!- DISRUPTION PHENOTYPE: Small number of abnormally large and
CC heterogeneous chloroplasts sometimes exhibiting alteration in stromule
CC length and frequency in non-green tissues (e.g. slightly increased
CC stromule frequency in hypocotyl epidermal cells) (PubMed:30824505,
CC PubMed:23936263). Normal shape and number of etioplasts in cotyledons
CC (PubMed:23936263). Misexpression and mislocalization of ADT2
CC (PubMed:30252596). Formation of multiple MCD1 and MIND1-containing ring
CC structures in dividing chloroplasts, instead of single ring
CC (PubMed:29967285). Slow trunover of FtsZ ring subunits (e.g. FTSZ2-1,
CC FTSZ2-2 and FTSZ1) in contractile rings at the chloroplast midpoint
CC (PubMed:25731613). {ECO:0000269|PubMed:10417716,
CC ECO:0000269|PubMed:15356321, ECO:0000269|PubMed:17304239,
CC ECO:0000269|PubMed:18764889, ECO:0000269|PubMed:23936263,
CC ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29967285,
CC ECO:0000269|PubMed:30252596, ECO:0000269|PubMed:30824505}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55276.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51935.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE99720.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB094044; BAD26731.1; -; mRNA.
DR EMBL; AC008263; AAD55276.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013258; AAG51935.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35661.1; -; Genomic_DNA.
DR EMBL; AK227735; BAE99720.1; ALT_SEQ; mRNA.
DR PIR; A96780; A96780.
DR RefSeq; NP_177638.2; NM_106158.5.
DR AlphaFoldDB; Q6F6B5; -.
DR SMR; Q6F6B5; -.
DR BioGRID; 29058; 3.
DR IntAct; Q6F6B5; 5.
DR MINT; Q6F6B5; -.
DR STRING; 3702.AT1G75010.1; -.
DR PaxDb; Q6F6B5; -.
DR PRIDE; Q6F6B5; -.
DR ProteomicsDB; 244457; -.
DR EnsemblPlants; AT1G75010.1; AT1G75010.1; AT1G75010.
DR GeneID; 843839; -.
DR Gramene; AT1G75010.1; AT1G75010.1; AT1G75010.
DR KEGG; ath:AT1G75010; -.
DR Araport; AT1G75010; -.
DR TAIR; locus:2027242; AT1G75010.
DR eggNOG; KOG0231; Eukaryota.
DR HOGENOM; CLU_382379_0_0_1; -.
DR InParanoid; Q6F6B5; -.
DR OMA; IYRGRCQ; -.
DR OrthoDB; 376216at2759; -.
DR PhylomeDB; Q6F6B5; -.
DR PRO; PR:Q6F6B5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6F6B5; baseline and differential.
DR Genevisible; Q6F6B5; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0035452; C:extrinsic component of plastid membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR045013; ARC3.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR43215:SF11; PTHR43215:SF11; 1.
DR Pfam; PF02493; MORN; 3.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00698; MORN; 2.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Plastid outer membrane; Reference proteome;
KW Repeat; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..741
FT /note="Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS
FT 3, chloroplastic"
FT /id="PRO_0000406230"
FT REPEAT 612..628
FT /note="MORN 1"
FT /evidence="ECO:0000255"
FT REPEAT 630..652
FT /note="MORN 2"
FT /evidence="ECO:0000255"
FT REPEAT 653..675
FT /note="MORN 3"
FT /evidence="ECO:0000255"
FT REGION 444..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 632
FT /note="G->A: Impaired interaction with CDP1/PARC6; when
FT associated with A-641; A-643; A-655; A-664 and A-666."
FT /evidence="ECO:0000269|PubMed:30824505"
FT MUTAGEN 641
FT /note="G->A: Impaired interaction with CDP1/PARC6; when
FT associated with A-632; A-643; A-655; A-664 and A-666."
FT /evidence="ECO:0000269|PubMed:30824505"
FT MUTAGEN 643
FT /note="G->A: Impaired interaction with CDP1/PARC6; when
FT associated with A-632; A-641; A-655; A-664 and A-666."
FT /evidence="ECO:0000269|PubMed:30824505"
FT MUTAGEN 655
FT /note="G->A: Impaired interaction with CDP1/PARC6; when
FT associated with A-632; A-641; A-643; A-664 and A-666."
FT /evidence="ECO:0000269|PubMed:30824505"
FT MUTAGEN 664
FT /note="G->A: Impaired interaction with CDP1/PARC6; when
FT associated with A-632; A-641; A-643; A-655 and A-666."
FT /evidence="ECO:0000269|PubMed:30824505"
FT MUTAGEN 666
FT /note="G->A: Impaired interaction with CDP1/PARC6; when
FT associated with A-632; A-641; A-643; A-655 and A-664."
FT /evidence="ECO:0000269|PubMed:30824505"
FT CONFLICT 129
FT /note="L -> S (in Ref. 1; BAD26731)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="V -> E (in Ref. 1; BAD26731)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="V -> I (in Ref. 1; BAD26731)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="I -> V (in Ref. 1; BAD26731)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="F -> L (in Ref. 1; BAD26731)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="V -> A (in Ref. 4; BAE99720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 82583 MW; 3CA934BB03EB9DEF CRC64;
MPISMELPVF STLRVPLFSR LALLPTFGVP FSSLGATTRL NCTSRKARRI CVMCLVRDSA
PIETCERAGE DGSDEFIEVL VIGSRKESIM DSCLDSPFPS LPLRFWSISK DSSGGLVLQQ
RLNHQDNALK TMNPIELLQS RPRAFILVAS AGYGSDQVEA INILSAVRSG GNLAVAVLLK
PFSFEGRKRL EEVNELARKL QQHTNFCIDI DIEVLLQKDL VTLDEALRNA NNAVSMAINA
ASALISGMHG NFIDVMHKDL KELEGSEVKT ILESYKEAKV GFGVGHNLKT SILRAIYDCP
FFRPGLKDLN AIICIVASSV PLQKKDVKTI LRTFRQTMEY TGDIIVSTVH EPDLEPKVRV
TTFFILSSSE VETSNKGNIF SGLVPFVLNI FTRYRSQLQK ETNIGLGETP VSIKDSADST
DVKTSNQNIE EFEIDSEDLL EVSENGDDSE YPLKEGEPSR NSRLDLKDEN VEDFGAIQRE
PIANWSMDQG YQIEQKWQAD SGDTAVLSLG IVNLPVGVRP SKKLNSNLSV ASQLSRKADS
REESFFNPNG STKDSSDTAS TLLSEKYADF TKQRNLSARA SSMLEAERDS SKRWSPILEM
QYRGGLFKGR CQGGLPEGKG RLVLGDGSIY DGMWHNGKRS GLGTFYFKNG DVFQGTWRED
LIHGKGWFYF HKGDRWFANF WKGKASGEGR FYSKSGEIFF GHFKDGWRHG QFLCIDLDGT
RYSETWDDGV LIDRKQVDAG D
