HNRPQ_ARATH
ID HNRPQ_ARATH Reviewed; 495 AA.
AC Q9ASP6; F4JHN3; F4JHN6; O23093;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein Q {ECO:0000305};
DE Short=hnRNP Q {ECO:0000305};
DE AltName: Full=Protein LHP1-INTERACTING FACTOR 2 {ECO:0000303|PubMed:21304947};
GN Name=LIF2 {ECO:0000303|PubMed:21304947};
GN OrderedLocusNames=At4g00830 {ECO:0000312|Araport:AT4G00830};
GN ORFNames=A_TM018A10.14 {ECO:0000312|EMBL:AAB62861.1},
GN T18A10.13 {ECO:0000312|EMBL:AAB62861.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENE FAMILY.
RX PubMed=21120628; DOI=10.1007/s10059-011-0001-2;
RA Peal L., Jambunathan N., Mahalingam R.;
RT "Phylogenetic and expression analysis of RNA-binding proteins with triple
RT RNA recognition motifs in plants.";
RL Mol. Cells 31:55-64(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LHP1.
RC STRAIN=cv. Columbia;
RX PubMed=21304947; DOI=10.1371/journal.pone.0016592;
RA Latrasse D., Germann S., Houba-Herin N., Dubois E., Bui-Prodhomme D.,
RA Hourcade D., Juul-Jensen T., Le Roux C., Majira A., Simoncello N.,
RA Granier F., Taconnat L., Renou J.P., Gaudin V.;
RT "Control of flowering and cell fate by LIF2, an RNA binding partner of the
RT polycomb complex component LHP1.";
RL PLoS ONE 6:E16592-E16592(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY PATHOGEN INFECTION.
RC STRAIN=cv. Columbia;
RX PubMed=24914891; DOI=10.1371/journal.pone.0099343;
RA Le Roux C., Del Prete S., Boutet-Mercey S., Perreau F., Balague C.,
RA Roby D., Fagard M., Gaudin V.;
RT "The hnRNP-Q protein LIF2 participates in the plant immune response.";
RL PLoS ONE 9:E99343-E99343(2014).
RN [8]
RP FUNCTION, INDUCTION BY JASMONIC ACID, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=27495811; DOI=10.1105/tpc.16.00244;
RA Molitor A., Latrasse D., Zytnicki M., Andrey P., Houba-Herin N., Hachet M.,
RA Battail C., Del Prete S., Alberti A., Quesneville H., Gaudin V.;
RT "The Arabidopsis hnRNP-Q Protein LIF2 and the PRC1 subunit LHP1 function in
RT concert to regulate the transcription of stress-responsive genes.";
RL Plant Cell 28:2197-2211(2016).
CC -!- FUNCTION: Transcriptional activator that binds DNA on GAGA-like motif
CC and 5'-(C/G)ACGTG(G/T)C(A/G)-3' consensus motif in the promoters of
CC target genes (PubMed:27495811). Component of ribonucleosomes, which are
CC complexes of at least 20 other different heterogeneous nuclear
CC ribonucleoproteins (hnRNP). hnRNP play an important role in processing
CC of precursor mRNA in the nucleus (By similarity). Required during
CC flower development and for cell fate determination (PubMed:21304947).
CC Acts both as an antagonist and as a promoter of polycomb LHP1 gene
CC regulation activity, depending of target genes, to regulate the
CC transcription of stress-responsive and flowering genes
CC (PubMed:21304947, PubMed:27495811). May regulate histone H3
CC trimethylation on lysine 27 (H3K27me3) (PubMed:21304947). Recognizes
CC and binds histone H3 tails methylated at 'Lys-4' (H3K4me) and
CC acetylated at 'Lys-9' (H3K9ac), leading to epigenetic activation. When
CC in complex with LHP1, recognizes and binds histone H3 tails methylated
CC at 'Lys-4' (H3K4me) and 'Lys-27' (H3K27me), mostly corresponding to
CC stress-responsive genes (PubMed:27495811). May function as a suppressor
CC of cell-autonomous immune responses involving glucosinolates, salicylic
CC acid (SA) and jasmonic acid (JA) pathways toward pathogenic bacteria
CC and fungi (PubMed:24914891). {ECO:0000250|UniProtKB:O60506,
CC ECO:0000269|PubMed:21304947, ECO:0000269|PubMed:24914891,
CC ECO:0000269|PubMed:27495811}.
CC -!- SUBUNIT: Interacts with LHP1 in the nucleus on a common set of
CC chromatin regions. {ECO:0000269|PubMed:21304947,
CC ECO:0000269|PubMed:27495811}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21304947}. Cytoplasm
CC {ECO:0000269|PubMed:21304947}. Microsome
CC {ECO:0000250|UniProtKB:Q7TMK9}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:Q7TMK9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ASP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ASP6-2; Sequence=VSP_059005;
CC Name=3;
CC IsoId=Q9ASP6-3; Sequence=VSP_059006;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in vascular and
CC meristematic tissues. Expressed throughout development in seedlings,
CC roots, leaves, floral buds and siliques. {ECO:0000269|PubMed:21304947}.
CC -!- DEVELOPMENTAL STAGE: In young plants, expressed in the distal regions
CC of cotyledons, throughout leaves and root apical meristem, lateral root
CC meristems and young floral buds. Strongly detected in the vascular
CC tissues of various organs (e.g. roots, leaves, hypocotyls, sepals,
CC petals, anther filaments) as well as in the gynophore. In the
CC gynoecium, mainly detected in apical and basal regions as well as in
CC the developing ovules in these regions. {ECO:0000269|PubMed:21304947}.
CC -!- INDUCTION: Slighty induced upon pathogen infection (e.g. P.syringae)
CC (PubMed:24914891). Rapidly recruited to chromatin upon methyl jasmonate
CC treatment (MeJA) to mediate transcriptional gene activation
CC (PubMed:27495811). {ECO:0000269|PubMed:24914891,
CC ECO:0000269|PubMed:27495811}.
CC -!- DISRUPTION PHENOTYPE: Mild early flowering phenotype, reduced rosette
CC diameter, abnormal floral developmental homeostasis and altered
CC gynoecium growth determination associated with indeterminate ovaries
CC growth. Production of ectopic inflorescences with severely affected
CC flowers showing proliferation of ectopic stigmatic papillae and ovules
CC in short-day conditions. Repression of FLC accompanied by an increase
CC in histone H3 trimethylation on lysine 27 (H3K27me3). Altered
CC expression of several genes, including LHP1-regulated genes
CC (PubMed:21304947). Basal primed defense state due to changes in the
CC basal expression of the salicylic acid (SA)- and jasmonic acid
CC (JA)- dependent defense marker genes PR1 and PDF1.2, and altered
CC composition of glucosinolates, a class of defense-related secondary
CC metabolites. Reduced susceptibility to the hemi-biotrophic bacteria
CC pathogen P.syringae and the necrotrophic ascomycete B.cinerea
CC (PubMed:24914891). {ECO:0000269|PubMed:21304947,
CC ECO:0000269|PubMed:24914891}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62861.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF013294; AAB62861.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80892.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81940.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81941.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81942.2; -; Genomic_DNA.
DR EMBL; CP002687; AEE81943.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66433.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66434.1; -; Genomic_DNA.
DR EMBL; AF367357; AAK32943.1; -; mRNA.
DR EMBL; AY113171; AAM47474.1; -; mRNA.
DR EMBL; AK227578; BAE99571.1; -; mRNA.
DR PIR; T01563; T01563.
DR RefSeq; NP_001031566.1; NM_001036489.3. [Q9ASP6-1]
DR RefSeq; NP_001190647.2; NM_001203718.2. [Q9ASP6-3]
DR RefSeq; NP_001190648.1; NM_001203719.2. [Q9ASP6-2]
DR RefSeq; NP_001328329.1; NM_001340269.1. [Q9ASP6-3]
DR RefSeq; NP_001328330.1; NM_001340270.1. [Q9ASP6-1]
DR RefSeq; NP_567192.1; NM_116309.4. [Q9ASP6-1]
DR AlphaFoldDB; Q9ASP6; -.
DR SMR; Q9ASP6; -.
DR STRING; 3702.AT4G00830.4; -.
DR iPTMnet; Q9ASP6; -.
DR PaxDb; Q9ASP6; -.
DR PRIDE; Q9ASP6; -.
DR ProteomicsDB; 230138; -. [Q9ASP6-1]
DR EnsemblPlants; AT4G00830.1; AT4G00830.1; AT4G00830. [Q9ASP6-1]
DR EnsemblPlants; AT4G00830.2; AT4G00830.2; AT4G00830. [Q9ASP6-1]
DR EnsemblPlants; AT4G00830.3; AT4G00830.3; AT4G00830. [Q9ASP6-3]
DR EnsemblPlants; AT4G00830.4; AT4G00830.4; AT4G00830. [Q9ASP6-2]
DR EnsemblPlants; AT4G00830.5; AT4G00830.5; AT4G00830. [Q9ASP6-3]
DR EnsemblPlants; AT4G00830.6; AT4G00830.6; AT4G00830. [Q9ASP6-1]
DR GeneID; 827998; -.
DR Gramene; AT4G00830.1; AT4G00830.1; AT4G00830. [Q9ASP6-1]
DR Gramene; AT4G00830.2; AT4G00830.2; AT4G00830. [Q9ASP6-1]
DR Gramene; AT4G00830.3; AT4G00830.3; AT4G00830. [Q9ASP6-3]
DR Gramene; AT4G00830.4; AT4G00830.4; AT4G00830. [Q9ASP6-2]
DR Gramene; AT4G00830.5; AT4G00830.5; AT4G00830. [Q9ASP6-3]
DR Gramene; AT4G00830.6; AT4G00830.6; AT4G00830. [Q9ASP6-1]
DR KEGG; ath:AT4G00830; -.
DR Araport; AT4G00830; -.
DR TAIR; locus:2134638; AT4G00830.
DR eggNOG; KOG0117; Eukaryota.
DR OMA; PGVEHIE; -.
DR OrthoDB; 1384330at2759; -.
DR PhylomeDB; Q9ASP6; -.
DR PRO; PR:Q9ASP6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ASP6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1905933; P:regulation of cell fate determination; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010439; P:regulation of glucosinolate biosynthetic process; IMP:UniProtKB.
DR GO; GO:1902464; P:regulation of histone H3-K27 trimethylation; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW Endoplasmic reticulum; Microsome; Nucleus; Plant defense;
KW Reference proteome; Repeat; RNA-binding; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..495
FT /note="Heterogeneous nuclear ribonucleoprotein Q"
FT /id="PRO_0000440880"
FT DOMAIN 116..194
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 196..278
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 292..368
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 184..195
FT /note="GKTIRCSLSETK -> ASSTANCSLSLS (in isoform 2)"
FT /id="VSP_059005"
FT VAR_SEQ 223..230
FT /note="Missing (in isoform 3)"
FT /id="VSP_059006"
SQ SEQUENCE 495 AA; 55136 MW; EA011DFB75783CC7 CRC64;
MSDARDNDDR VDFEEGSYSE MEDEVEEEQV EEYEEEEEED DDDDDVGNQN AEEREVEDYG
DTKGGDMEDV QEEIAEDDDN HIDIETADDD EKPPSPIDDE DREKYSHLLS LPPHGSEVFI
GGLPRDVGEE DLRDLCEEIG EIFEVRLMKD RDSGDSKGYA FVAFKTKDVA QKAIEELHSK
EFKGKTIRCS LSETKNRLFI GNIPKNWTED EFRKVIEDVG PGVENIELIK DPTNTTRNRG
FAFVLYYNNA CADYSRQKMI DSNFKLEGNA PTVTWADPKS SPEHSAAAAQ VKALYVKNIP
ENTSTEQLKE LFQRHGEVTK IVTPPGKGGK RDFGFVHYAE RSSALKAVKD TERYEVNGQP
LEVVLAKPQA ERKHDPSSYS YGAAPTPAPF VHPTFGGFAA APYGAMGAGL GIAGSFSQPM
IYGRGAMPTG MQMVPMLLPD GRVGYVLQQP GMPMAAAPPQ RPRRNDRNNG SSGGSGRDNS
HEHDGNRGGR RYRPY
