RBMX_MOUSE
ID RBMX_MOUSE Reviewed; 391 AA.
AC Q9WV02; Q8C2U6; Q9R0Y0;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=RNA-binding motif protein, X chromosome;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G;
DE Short=hnRNP G;
DE Contains:
DE RecName: Full=RNA-binding motif protein, X chromosome, N-terminally processed;
GN Name=Rbmx; Synonyms=Hnrnpg, Hnrpg, Rbmxp1, Rbmxrt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=10391207; DOI=10.1038/10282;
RA Mazeyrat S., Saut N., Mattei M.G., Mitchell M.J.;
RT "RBMY evolved on the Y chromosome from a ubiquitously transcribed X-Y
RT identical gene.";
RL Nat. Genet. 22:224-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Eye, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INDUCTION, ASSOCIATION WITH CHROMATIN, SREBF1 TRANSACTIVATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17188681; DOI=10.1016/j.febslet.2006.12.014;
RA Takemoto T., Nishio Y., Sekine O., Ikeuchi C., Nagai Y., Maeno Y.,
RA Maegawa H., Kimura H., Kashiwagi A.;
RT "RBMX is a novel hepatic transcriptional regulator of SREBP-1c gene
RT response to high-fructose diet.";
RL FEBS Lett. 581:218-222(2007).
RN [7]
RP FUNCTION, INTERACTION WITH SAFB, AND ASSOCIATION WITH CHROMATIN.
RX PubMed=19403048; DOI=10.5483/bmbrep.2009.42.4.232;
RA Omura Y., Nishio Y., Takemoto T., Ikeuchi C., Sekine O., Morino K.,
RA Maeno Y., Obata T., Ugi S., Maegawa H., Kimura H., Kashiwagi A.;
RT "SAFB1, an RBMX-binding protein, is a newly identified regulator of hepatic
RT SREBP-1c gene.";
RL BMB Rep. 42:232-237(2009).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-125; ARG-144; ARG-164 AND
RP ARG-172, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: RNA-binding protein that plays several role in the regulation
CC of pre- and post-transcriptional processes. Implicated in tissue-
CC specific regulation of gene transcription and alternative splicing of
CC several pre-mRNAs. Binds to and stimulates transcription from the tumor
CC suppressor TXNIP gene promoter; may thus be involved in tumor
CC suppression. When associated with SAFB, binds to and stimulates
CC transcription from the SREBF1 promoter. Associates with nascent mRNAs
CC transcribed by RNA polymerase II. Component of the supraspliceosome
CC complex that regulates pre-mRNA alternative splice site selection. Can
CC either activate or suppress exon inclusion; acts additively with TRA2B
CC to promote exon 7 inclusion of the survival motor neuron SMN2.
CC Represses the splicing of MAPT/Tau exon 10. Binds preferentially to
CC single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a
CC single-stranded conformation; probably binds RNA as a homodimer. Binds
CC non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic
CC TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated
CC inducible proteolytic cleavage of TNFR1 ectodomains and the release of
CC TNFR1 exosome-like vesicles to the extracellular compartment.
CC {ECO:0000269|PubMed:17188681, ECO:0000269|PubMed:19403048}.
CC -!- SUBUNIT: Homomultimer. Found in the supraspliceosome complex.
CC Identified in the spliceosome C complex. Interacts with KHDRBS3. Forms
CC a complex with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA Interacts
CC with CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the
CC interaction is RNA-independent (By similarity). Interacts with
CC SAFB/SAFB1 (PubMed:19403048). Interacts with PPIA/CYPA (By similarity).
CC {ECO:0000250|UniProtKB:P38159, ECO:0000269|PubMed:19403048}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Localizes in numerous small
CC granules in the nucleus (By similarity). Component of ribonucleosomes.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WV02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WV02-2; Sequence=VSP_042129;
CC -!- TISSUE SPECIFICITY: Both isoforms are widely expressed.
CC {ECO:0000269|PubMed:10391207}.
CC -!- INDUCTION: By high-fructose diet. {ECO:0000269|PubMed:17188681}.
CC -!- DOMAIN: The RRM domain is necessary for RNA-binding, but not for splice
CC site selection, indicating that its splicing activity does not require
CC direct binding to RNA. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: Arg-182 is dimethylated, probably to asymmetric dimethylarginine.
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DR EMBL; AJ237846; CAB51361.1; -; mRNA.
DR EMBL; AJ237847; CAB51362.1; -; mRNA.
DR EMBL; AK087940; BAC40051.1; -; mRNA.
DR EMBL; AK135164; BAE22448.1; -; mRNA.
DR EMBL; AK165006; BAE37998.1; -; mRNA.
DR EMBL; AL672106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466583; EDL42174.1; -; Genomic_DNA.
DR EMBL; CH466583; EDL42172.1; -; Genomic_DNA.
DR EMBL; BC003710; AAH03710.1; -; mRNA.
DR CCDS; CCDS30153.1; -. [Q9WV02-1]
DR RefSeq; NP_001160095.1; NM_001166623.1. [Q9WV02-1]
DR RefSeq; NP_035382.1; NM_011252.4. [Q9WV02-1]
DR AlphaFoldDB; Q9WV02; -.
DR SMR; Q9WV02; -.
DR BioGRID; 202824; 18.
DR IntAct; Q9WV02; 7.
DR MINT; Q9WV02; -.
DR STRING; 10090.ENSMUSP00000110374; -.
DR iPTMnet; Q9WV02; -.
DR PhosphoSitePlus; Q9WV02; -.
DR EPD; Q9WV02; -.
DR jPOST; Q9WV02; -.
DR MaxQB; Q9WV02; -.
DR PaxDb; Q9WV02; -.
DR PeptideAtlas; Q9WV02; -.
DR PRIDE; Q9WV02; -.
DR ProteomicsDB; 300274; -. [Q9WV02-1]
DR ProteomicsDB; 300275; -. [Q9WV02-2]
DR TopDownProteomics; Q9WV02-1; -. [Q9WV02-1]
DR Antibodypedia; 30459; 156 antibodies from 27 providers.
DR DNASU; 19655; -.
DR Ensembl; ENSMUST00000114726; ENSMUSP00000110374; ENSMUSG00000031134. [Q9WV02-1]
DR Ensembl; ENSMUST00000114730; ENSMUSP00000110378; ENSMUSG00000031134. [Q9WV02-1]
DR Ensembl; ENSMUST00000140384; ENSMUSP00000125720; ENSMUSG00000031134. [Q9WV02-2]
DR GeneID; 19655; -.
DR KEGG; mmu:19655; -.
DR UCSC; uc009thi.2; mouse. [Q9WV02-1]
DR CTD; 27316; -.
DR MGI; MGI:1343044; Rbmx.
DR VEuPathDB; HostDB:ENSMUSG00000031134; -.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000153425; -.
DR HOGENOM; CLU_042286_0_0_1; -.
DR InParanoid; Q9WV02; -.
DR OMA; AKYHEGF; -.
DR OrthoDB; 1248417at2759; -.
DR PhylomeDB; Q9WV02; -.
DR TreeFam; TF331833; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 19655; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Rbmx; mouse.
DR PRO; PR:Q9WV02; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9WV02; protein.
DR Bgee; ENSMUSG00000031134; Expressed in saccule of membranous labyrinth and 261 other tissues.
DR ExpressionAtlas; Q9WV02; baseline and differential.
DR Genevisible; Q9WV02; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0044530; C:supraspliceosomal complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:0006376; P:mRNA splice site selection; ISO:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Glycoprotein;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Transcription; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..391
FT /note="RNA-binding motif protein, X chromosome"
FT /id="PRO_0000414748"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CHAIN 2..391
FT /note="RNA-binding motif protein, X chromosome, N-
FT terminally processed"
FT /id="PRO_0000414747"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 62..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 2
FT /note="N-acetylvaline; in RNA-binding motif protein, X
FT chromosome, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 125
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 164
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT VAR_SEQ 290..391
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10391207,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_042129"
SQ SEQUENCE 391 AA; 42301 MW; 301E02E250EDDCD3 CRC64;
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGLPPPP RSRGPPRGLR GGRGGSGGTR
GPPSRGGHMD DGGYSMNFTM SSSRGPLPVK RGPPPRSGGP PPKRSAPSGP VRSSSGLGGR
APVSRGRDGY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSREYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP PSMERGYPPP
RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y
