ARR2_ARATH
ID ARR2_ARATH Reviewed; 664 AA.
AC Q9ZWJ9; C3PTB4; O23460; Q680A8; Q682I9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Two-component response regulator ARR2;
DE AltName: Full=Receiver-like protein 5;
GN Name=ARR2; Synonyms=ARP5; OrderedLocusNames=At4g16110;
GN ORFNames=dl4095w, FCAALL.297;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9891419; DOI=10.1093/oxfordjournals.pcp.a029325;
RA Sakai H., Aoyama T., Bono H., Oka A.;
RT "Two-component response regulators from Arabidopsis thaliana contain a
RT putative DNA-binding motif.";
RL Plant Cell Physiol. 39:1232-1239(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=11370868; DOI=10.1007/s004380000400;
RA Lohrmann J., Sweere U., Zabaleta E., Baeurle I., Keitel C.,
RA Kozma-Bognar L., Brennicke A., Schaefer E., Kudla J., Harter K.;
RT "The response regulator ARR2: a pollen-specific transcription factor
RT involved in the expression of nuclear genes for components of mitochondrial
RT complex I in Arabidopsis.";
RL Mol. Genet. Genomics 265:2-13(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS ILE-62; ILE-283; VAL-385
RP AND GLY-655, FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT ASP-80,
RP MUTAGENESIS OF ASP-80, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=15282545; DOI=10.1038/sj.emboj.7600337;
RA Hass C., Lohrmann J., Albrecht V., Sweere U., Hummel F., Yoo S.D.,
RA Hwang I., Zhu T., Schaefer E., Kudla J., Harter K.;
RT "The response regulator 2 mediates ethylene signalling and hormone signal
RT integration in Arabidopsis.";
RL EMBO J. 23:3290-3302(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
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 [7]
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP DNA-BINDING SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11135105; DOI=10.1046/j.1365-313x.2000.00909.x;
RA Sakai H., Aoyama T., Oka A.;
RT "Arabidopsis ARR1 and ARR2 response regulators operate as transcriptional
RT activators.";
RL Plant J. 24:703-711(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11574878; DOI=10.1038/35096500;
RA Hwang I., Sheen J.;
RT "Two-component circuitry in Arabidopsis cytokinin signal transduction.";
RL Nature 413:383-389(2001).
RN [10]
RP INTERACTION.
RX PubMed=14981318; DOI=10.1271/bbb.68.462;
RA Tanaka Y., Suzuki T., Yamashino T., Mizuno T.;
RT "Comparative studies of the AHP histidine-containing phosphotransmitters
RT implicated in His-to-Asp phosphorelay in Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 68:462-465(2004).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=15173562; DOI=10.1104/pp.103.038109;
RA Mason M.G., Li J., Mathews D.E., Kieber J.J., Schaller G.E.;
RT "Type-B response regulators display overlapping expression patterns in
RT Arabidopsis.";
RL Plant Physiol. 135:927-937(2004).
RN [12]
RP FUNCTION, MUTAGENESIS OF ASP-80, AND PHOSPHORYLATION AT ASP-80.
RX PubMed=16407152; DOI=10.1073/pnas.0505150103;
RA Kim H.J., Ryu H., Hong S.H., Woo H.R., Lim P.O., Lee I.C., Sheen J.,
RA Nam H.G., Hwang I.;
RT "Cytokinin-mediated control of leaf longevity by AHK3 through
RT phosphorylation of ARR2 in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:814-819(2006).
CC -!- FUNCTION: Transcriptional activator that binds specifically to the DNA
CC sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in
CC His-to-Asp phosphorelay signal transduction system. Phosphorylation of
CC the Asp residue in the receiver domain activates the ability of the
CC protein to promote the transcription of target genes. Could directly
CC activate some type-A response regulators in response to cytokinins.
CC Involved in the expression of nuclear genes for components of
CC mitochondrial complex I. Promotes cytokinin-mediated leaf longevity.
CC Involved in the ethylene signaling pathway in an ETR1-dependent manner
CC and in the cytokinin signaling pathway. {ECO:0000269|PubMed:11370868,
CC ECO:0000269|PubMed:11574878, ECO:0000269|PubMed:15282545,
CC ECO:0000269|PubMed:16407152}.
CC -!- SUBUNIT: Binds the target DNA as a monomer (By similarity). Interacts
CC with histidine-containing phosphotransfer proteins. {ECO:0000250,
CC ECO:0000269|PubMed:11370868, ECO:0000269|PubMed:14981318}.
CC -!- INTERACTION:
CC Q9ZWJ9; Q9ZNV9: AHP1; NbExp=4; IntAct=EBI-1101028, EBI-1100673;
CC Q9ZWJ9; Q9ZNV8: AHP2; NbExp=7; IntAct=EBI-1101028, EBI-1100687;
CC Q9ZWJ9; Q0WPF2: PCFS4; NbExp=3; IntAct=EBI-1101028, EBI-1775648;
CC Q9ZWJ9; Q9SLH3: RGA; NbExp=5; IntAct=EBI-1101028, EBI-963624;
CC Q9ZWJ9; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-1101028, EBI-4426144;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:11135105, ECO:0000269|PubMed:11574878,
CC ECO:0000269|PubMed:15282545}.
CC -!- TISSUE SPECIFICITY: Detected in the whole plant. Predominantly
CC expressed in pollen. {ECO:0000269|PubMed:11370868,
CC ECO:0000269|PubMed:15173562, ECO:0000269|PubMed:9891419}.
CC -!- PTM: Two-component system major event consists of a His-to-Asp
CC phosphorelay between a sensor histidine kinase (HK) and a response
CC regulator (RR). In plants, the His-to-Asp phosphorelay involves an
CC additional intermediate named Histidine-containing phosphotransfer
CC protein (HPt). This multistep phosphorelay consists of a His-Asp-His-
CC Asp sequential transfer of a phosphate group between first an His and
CC an Asp of the HK protein, followed by the transfer to a conserved His
CC of the HPt protein and finally the transfer to an Asp in the receiver
CC domain of the RR protein. Phosphorylated in response to cytokinin
CC mediated by AHK3. {ECO:0000269|PubMed:15282545,
CC ECO:0000269|PubMed:16407152}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth and development, and early
CC flowering. Reduced responses to ethylene and cytokinin.
CC {ECO:0000269|PubMed:15282545}.
CC -!- SIMILARITY: Belongs to the ARR family. Type-B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA06433.1; Type=Miscellaneous discrepancy; Note=Artifacts of PCR amplification.; Evidence={ECO:0000305};
CC Sequence=CAB10390.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78653.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016472; BAA74527.1; -; Genomic_DNA.
DR EMBL; AJ005196; CAA06433.1; ALT_SEQ; mRNA.
DR EMBL; DQ473518; ABF47278.1; -; Genomic_DNA.
DR EMBL; DQ473519; ABF47279.1; -; mRNA.
DR EMBL; DQ473520; ABF19058.1; -; Genomic_DNA.
DR EMBL; DQ473521; ABF19059.1; -; mRNA.
DR EMBL; Z97340; CAB10390.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161543; CAB78653.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83694.2; -; Genomic_DNA.
DR EMBL; AK175378; BAD43141.1; -; mRNA.
DR EMBL; AK175737; BAD43500.1; -; mRNA.
DR EMBL; AK175959; BAD43722.1; -; mRNA.
DR EMBL; AK176614; BAD44377.1; -; mRNA.
DR PIR; D71427; D71427.
DR PIR; T51247; T51247.
DR RefSeq; NP_193346.5; NM_117704.6.
DR AlphaFoldDB; Q9ZWJ9; -.
DR SMR; Q9ZWJ9; -.
DR BioGRID; 12591; 12.
DR IntAct; Q9ZWJ9; 11.
DR STRING; 3702.AT4G16110.1; -.
DR PaxDb; Q9ZWJ9; -.
DR PRIDE; Q9ZWJ9; -.
DR ProteomicsDB; 246936; -.
DR GeneID; 827297; -.
DR KEGG; ath:AT4G16110; -.
DR Araport; AT4G16110; -.
DR TAIR; locus:2130095; AT4G16110.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_413684_0_0_1; -.
DR InParanoid; Q9ZWJ9; -.
DR OrthoDB; 265576at2759; -.
DR PhylomeDB; Q9ZWJ9; -.
DR PRO; PR:Q9ZWJ9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZWJ9; baseline and differential.
DR Genevisible; Q9ZWJ9; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0000156; F:phosphorelay response regulator activity; ISS:TAIR.
DR GO; GO:0071368; P:cellular response to cytokinin stimulus; IMP:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:UniProtKB.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:TAIR.
DR GO; GO:0080113; P:regulation of seed growth; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IGI:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR InterPro; IPR045279; ARR-like.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR017053; Response_reg_B-typ_pln.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43874; PTHR43874; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF036392; RR_ARR_type-B; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Cytokinin signaling pathway; DNA-binding;
KW Ethylene signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..664
FT /note="Two-component response regulator ARR2"
FT /id="PRO_0000132294"
FT DOMAIN 29..144
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 218..268
FT /note="Myb-like GARP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 215..218
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 161..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:15282545, ECO:0000269|PubMed:16407152"
FT VARIANT 62
FT /note="S -> I (in strain: cv. Landsberg erecta)"
FT /evidence="ECO:0000269|PubMed:15282545"
FT VARIANT 283
FT /note="N -> I (in strain: cv. Landsberg erecta)"
FT /evidence="ECO:0000269|PubMed:15282545"
FT VARIANT 385
FT /note="L -> V (in strain: cv. Landsberg erecta)"
FT /evidence="ECO:0000269|PubMed:15282545"
FT VARIANT 655
FT /note="D -> G (in strain: cv. Landsberg erecta)"
FT /evidence="ECO:0000269|PubMed:15282545"
FT MUTAGEN 80
FT /note="D->N: Impaired cytokinin-mediated and ethylene-
FT mediated phosphorylation, severe pleiotropic aberrations in
FT growth and development."
FT /evidence="ECO:0000269|PubMed:15282545,
FT ECO:0000269|PubMed:16407152"
FT CONFLICT 35
FT /note="D -> G (in Ref. 7; BAD43141)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="H -> R (in Ref. 7; BAD43141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 72578 MW; F930558EB55549F4 CRC64;
MVNPGHGRGP DSGTAAGGSN SDPFPANLRV LVVDDDPTCL MILERMLMTC LYRVTKCNRA
ESALSLLRKN KNGFDIVISD VHMPDMDGFK LLEHVGLEMD LPVIMMSADD SKSVVLKGVT
HGAVDYLIKP VRIEALKNIW QHVVRKKRNE WNVSEHSGGS IEDTGGDRDR QQQHREDADN
NSSSVNEGNG RSSRKRKEEE VDDQGDDKED SSSLKKPRVV WSVELHQQFV AAVNQLGVDK
AVPKKILEMM NVPGLTRENV ASHLQKYRIY LRRLGGVSQH QGNMNHSFMT GQDQSFGPLS
SLNGFDLQSL AVTGQLPPQS LAQLQAAGLG RPTLAKPGMS VSPLVDQRSI FNFENPKIRF
GDGHGQTMNN GNLLHGVPTG SHMRLRPGQN VQSSGMMLPV ADQLPRGGPS MLPSLGQQPI
LSSSVSRRSD LTGALAVRNS IPETNSRVLP TTHSVFNNFP ADLPRSSFPL ASAPGISVPV
SVSYQEEVNS SDAKGGSSAA TAGFGNPSYD IFNDFPQHQQ HNKNISNKLN DWDLRNMGLV
FSSNQDAATA TATAAFSTSE AYSSSSTQRK RRETDATVVG EHGQNLQSPS RNLYHLNHVF
MDGGSVRVKS ERVAETVTCP PANTLFHEQY NQEDLMSAFL KQEGIPSVDN EFEFDGYSID
NIQV
