ID   FUBP2_MOUSE             Reviewed;         748 AA.
AC   Q3U0V1; E9QKH3; Q2VPQ6; Q6P2L2;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Far upstream element-binding protein 2;
DE            Short=FUSE-binding protein 2;
DE   AltName: Full=KH type-splicing regulatory protein;
DE            Short=KSRP;
GN   Name=Khsrp; Synonyms=Fubp2;
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 [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-748.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40; ARG-412; ARG-414; ARG-416 AND
RP   ARG-443, 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: Binds to the dendritic targeting element and may play a role
CC       in mRNA trafficking. Part of a ternary complex that binds to the
CC       downstream control sequence (DCS) of the pre-mRNA. Mediates exon
CC       inclusion in transcripts that are subject to tissue-specific
CC       alternative splicing. May interact with single-stranded DNA from the
CC       far-upstream element (FUSE). May activate gene expression. Also
CC       involved in degradation of inherently unstable mRNAs that contain AU-
CC       rich elements (AREs) in their 3'-UTR, possibly by recruiting
CC       degradation machinery to ARE-containing mRNAs (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and
CC       HNRPH1. Interacts with PARN. Interacts with PQBP1.
CC       {ECO:0000250|UniProtKB:Q92945}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=A small proportion is also found in the cytoplasm of neuronal cell
CC       bodies and dendrites. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
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DR   EMBL; AK156541; BAE33750.1; -; mRNA.
DR   EMBL; CT571247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC064454; AAH64454.1; -; mRNA.
DR   EMBL; BC108414; AAI08415.1; -; mRNA.
DR   CCDS; CCDS50157.1; -.
DR   RefSeq; NP_034743.3; NM_010613.3.
DR   AlphaFoldDB; Q3U0V1; -.
DR   SMR; Q3U0V1; -.
DR   BioGRID; 200927; 29.
DR   IntAct; Q3U0V1; 9.
DR   MINT; Q3U0V1; -.
DR   STRING; 10090.ENSMUSP00000007814; -.
DR   GlyGen; Q3U0V1; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q3U0V1; -.
DR   PhosphoSitePlus; Q3U0V1; -.
DR   SwissPalm; Q3U0V1; -.
DR   EPD; Q3U0V1; -.
DR   jPOST; Q3U0V1; -.
DR   MaxQB; Q3U0V1; -.
DR   PaxDb; 10090-ENSMUSP00000007814; -.
DR   PeptideAtlas; Q3U0V1; -.
DR   ProteomicsDB; 266885; -.
DR   Pumba; Q3U0V1; -.
DR   Antibodypedia; 6316; 367 antibodies from 34 providers.
DR   DNASU; 16549; -.
DR   Ensembl; ENSMUST00000007814.10; ENSMUSP00000007814.9; ENSMUSG00000007670.11.
DR   GeneID; 16549; -.
DR   KEGG; mmu:16549; -.
DR   UCSC; uc008ddr.2; mouse.
DR   AGR; MGI:1336214; -.
DR   CTD; 8570; -.
DR   MGI; MGI:1336214; Khsrp.
DR   VEuPathDB; HostDB:ENSMUSG00000007670; -.
DR   eggNOG; KOG1676; Eukaryota.
DR   GeneTree; ENSGT00940000156051; -.
DR   HOGENOM; CLU_014285_1_0_1; -.
DR   InParanoid; Q3U0V1; -.
DR   OMA; QPVHQWA; -.
DR   OrthoDB; 1662at2759; -.
DR   PhylomeDB; Q3U0V1; -.
DR   TreeFam; TF313654; -.
DR   Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR   BioGRID-ORCS; 16549; 5 hits in 80 CRISPR screens.
DR   ChiTaRS; Khsrp; mouse.
DR   PRO; PR:Q3U0V1; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q3U0V1; Protein.
DR   Bgee; ENSMUSG00000007670; Expressed in ventricular zone and 227 other cell types or tissues.
DR   ExpressionAtlas; Q3U0V1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR   GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR   GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR   GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR   GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR   GO; GO:0006402; P:mRNA catabolic process; IDA:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:MGI.
DR   GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:2000628; P:regulation of miRNA metabolic process; IDA:MGI.
DR   GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd22479; KH-I_FUBP2_rpt1; 1.
DR   CDD; cd22482; KH-I_FUBP2_rpt2; 1.
DR   CDD; cd22485; KH-I_FUBP2_rpt3; 1.
DR   CDD; cd22488; KH-I_FUBP2_rpt4; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 4.
DR   InterPro; IPR015096; FUBP_C.
DR   InterPro; IPR047372; KH-I_FUBP2_rpt1.
DR   InterPro; IPR047369; KH-I_FUBP2_rpt2.
DR   InterPro; IPR047370; KH-I_FUBP2_rpt3.
DR   InterPro; IPR047371; KH-I_FUBP2_rpt4.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   PANTHER; PTHR10288:SF101; FAR UPSTREAM ELEMENT-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
DR   Pfam; PF09005; DUF1897; 2.
DR   Pfam; PF00013; KH_1; 4.
DR   SMART; SM00322; KH; 4.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 4.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 4.
DR   Genevisible; Q3U0V1; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Methylation;
KW   mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Transcription;
KW   Transcription regulation; Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   CHAIN           2..748
FT                   /note="Far upstream element-binding protein 2"
FT                   /id="PRO_0000298678"
FT   DOMAIN          145..209
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          234..300
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          323..387
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          425..492
FT                   /note="KH 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REPEAT          572..583
FT                   /note="1"
FT   REPEAT          618..629
FT                   /note="2"
FT   REPEAT          644..655
FT                   /note="3"
FT   REPEAT          674..685
FT                   /note="4"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..685
FT                   /note="4 X 12 AA imperfect repeats"
FT   REGION          588..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..546
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..615
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   MOD_RES         40
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         88
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         101
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   MOD_RES         412
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         414
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         416
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         443
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   CROSSLNK        122
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   CROSSLNK        122
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q92945"
FT   CONFLICT        387
FT                   /note="I -> F (in Ref. 1; BAE33750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   748 AA;  76775 MW;  0699217B3E1E54A9 CRC64;
     MSDYNTGGPP PGPPPPAGGG GGAAGAGGGP PPGPPGAGDR GGGGPGGGGP GGGGASGGPS
     QPPGGGGPGI RKDAFADAVQ RARQIAAKIG GDAATTVNNN TPDFGFGGQK RQLEDGDQPD
     SKKLASQGDS IGSQLGPIHP PPRTSMTEEY RVPDGMVGLI IGRGGEQINK IQQDSGCKVQ
     ISPDSGGLPE RSVSLTGAPE SVQKAKMMLD DIVSRGRGGP PGQFHDNANG GQNGTVQEIM
     IPAGKAGLVI GKGGETIKQL QERAGVKMIL IQDGSQNTNV DKPLRIIGDP YKVQQACEMV
     MDILRERDQG GFGDRNEYGS RVGGGIDVPV PRHSVGVVIG RSGEMIKKIQ NDAGVRIQFK
     QDDGTGPEKI AHIMGPPDRC EHAARIINDL LQSLRSGPPG PPGAPGMPPG GRGRGRGQGN
     WGPPGGEMTF SIPTHKCGLV IGRGGENVKA INQQTGAFVE ISRQLPPNGD PNFKLFVIRG
     SPQQIDHAKQ LIEEKIEGPL CPVGPGPGGP GPAGPMGPFN PGPFNQGPPG APPHAGGPPP
     HQYPPQGWGN TYPQWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA
     APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE EYYKKQAQVA
     TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ PPPTQQGQQQ ASGNCHPPPP
     PFSFQPPATV HPALVGSAGN PFPCGVCP
//