RBM39_MOUSE
ID RBM39_MOUSE Reviewed; 530 AA.
AC Q8VH51; Q5RJI0; Q99KV0;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=RNA-binding protein 39;
DE AltName: Full=Coactivator of activating protein 1 and estrogen receptors {ECO:0000303|PubMed:11704680};
DE Short=Coactivator of AP-1 and ERs {ECO:0000303|PubMed:11704680};
DE AltName: Full=RNA-binding motif protein 39;
DE AltName: Full=RNA-binding region-containing protein 2;
GN Name=Rbm39; Synonyms=Caper {ECO:0000303|PubMed:11704680}, Rnpc2;
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), FUNCTION, AND INTERACTION
RP WITH NCOA6; ESR1; ESR2 AND JUN.
RC TISSUE=Liver;
RX PubMed=11704680; DOI=10.1074/jbc.m110417200;
RA Jung D.-J., Na S.-Y., Na D.S., Lee J.W.;
RT "Molecular cloning and characterization of CAPER, a novel coactivator of
RT activating protein-1 and estrogen receptors.";
RL J. Biol. Chem. 277:1229-1234(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, Mammary fibroblast, and Retina;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-136; SER-334 AND
RP SER-337, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP INTERACTION WITH ZNF106.
RX PubMed=27418600; DOI=10.1073/pnas.1608423113;
RA Anderson D.M., Cannavino J., Li H., Anderson K.M., Nelson B.R.,
RA McAnally J., Bezprozvannaya S., Liu Y., Lin W., Liu N., Bassel-Duby R.,
RA Olson E.N.;
RT "Severe muscle wasting and denervation in mice lacking the RNA-binding
RT protein ZFP106.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4494-E4503(2016).
CC -!- FUNCTION: RNA-binding protein that acts as a pre-mRNA splicing factor.
CC Acts by promoting exon inclusion via regulation of exon cassette
CC splicing (By similarity). Also acts as a transcriptional coactivator
CC for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and
CC JUN/AP-1, independently of the pre-mRNA splicing factor activity
CC (PubMed:11704680). {ECO:0000250|UniProtKB:Q14498,
CC ECO:0000269|PubMed:11704680}.
CC -!- SUBUNIT: Interacts with NCOA6 and JUN (PubMed:11704680). Interacts with
CC ESR1 and ESR2, in the presence of estradiol (E2) (PubMed:11704680).
CC Interacts with RSRC1 (via Arg/Ser-rich domain) (By similarity).
CC Interacts with SF3B1 (By similarity). Interacts with ZNF106 (via N-
CC terminus) (PubMed:27418600). {ECO:0000250|UniProtKB:Q14498,
CC ECO:0000269|PubMed:11704680, ECO:0000269|PubMed:27418600}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=HCC1.4;
CC IsoId=Q8VH51-1; Sequence=Displayed;
CC Name=2; Synonyms=HCC1.3;
CC IsoId=Q8VH51-2; Sequence=VSP_005822;
CC Name=3;
CC IsoId=Q8VH51-3; Sequence=VSP_005821, VSP_005822;
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AY061882; AAL32373.1; -; mRNA.
DR EMBL; AK147076; BAE27657.1; -; mRNA.
DR EMBL; AL929404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06184.1; -; Genomic_DNA.
DR EMBL; BC004000; AAH04000.1; -; mRNA.
DR EMBL; BC030493; AAH30493.1; -; mRNA.
DR EMBL; BC086645; AAH86645.1; -; mRNA.
DR CCDS; CCDS16964.1; -. [Q8VH51-1]
DR CCDS; CCDS71168.1; -. [Q8VH51-2]
DR RefSeq; NP_001278043.1; NM_001291114.1. [Q8VH51-2]
DR RefSeq; NP_001278044.1; NM_001291115.1. [Q8VH51-2]
DR RefSeq; NP_573505.2; NM_133242.3. [Q8VH51-1]
DR RefSeq; XP_011237628.1; XM_011239326.2.
DR RefSeq; XP_011237629.1; XM_011239327.2. [Q8VH51-3]
DR RefSeq; XP_017171483.1; XM_017315994.1. [Q8VH51-3]
DR RefSeq; XP_017171487.1; XM_017315998.1.
DR RefSeq; XP_017171494.1; XM_017316005.1. [Q8VH51-3]
DR RefSeq; XP_017171497.1; XM_017316008.1. [Q8VH51-3]
DR PDB; 2LQ5; NMR; -; A=418-530.
DR PDB; 3S6E; X-ray; 0.95 A; A/B=418-530.
DR PDB; 4J5O; X-ray; 1.11 A; A/B=418-530.
DR PDB; 4RU2; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q=418-530.
DR PDB; 5CXT; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q=418-530.
DR PDBsum; 2LQ5; -.
DR PDBsum; 3S6E; -.
DR PDBsum; 4J5O; -.
DR PDBsum; 4RU2; -.
DR PDBsum; 5CXT; -.
DR AlphaFoldDB; Q8VH51; -.
DR BMRB; Q8VH51; -.
DR SMR; Q8VH51; -.
DR BioGRID; 228442; 36.
DR IntAct; Q8VH51; 10.
DR MINT; Q8VH51; -.
DR STRING; 10090.ENSMUSP00000105216; -.
DR iPTMnet; Q8VH51; -.
DR PhosphoSitePlus; Q8VH51; -.
DR EPD; Q8VH51; -.
DR jPOST; Q8VH51; -.
DR MaxQB; Q8VH51; -.
DR PaxDb; Q8VH51; -.
DR PeptideAtlas; Q8VH51; -.
DR PRIDE; Q8VH51; -.
DR ProteomicsDB; 255129; -. [Q8VH51-1]
DR ProteomicsDB; 255130; -. [Q8VH51-2]
DR ProteomicsDB; 255131; -. [Q8VH51-3]
DR Antibodypedia; 459; 238 antibodies from 28 providers.
DR DNASU; 170791; -.
DR Ensembl; ENSMUST00000029149; ENSMUSP00000029149; ENSMUSG00000027620. [Q8VH51-2]
DR Ensembl; ENSMUST00000109587; ENSMUSP00000105216; ENSMUSG00000027620. [Q8VH51-1]
DR Ensembl; ENSMUST00000146297; ENSMUSP00000119298; ENSMUSG00000027620. [Q8VH51-2]
DR GeneID; 170791; -.
DR KEGG; mmu:170791; -.
DR UCSC; uc008nmr.3; mouse. [Q8VH51-1]
DR CTD; 9584; -.
DR MGI; MGI:2157953; Rbm39.
DR VEuPathDB; HostDB:ENSMUSG00000027620; -.
DR eggNOG; KOG0147; Eukaryota.
DR GeneTree; ENSGT00940000154468; -.
DR InParanoid; Q8VH51; -.
DR OMA; GRDNDKG; -.
DR OrthoDB; 873705at2759; -.
DR PhylomeDB; Q8VH51; -.
DR TreeFam; TF320448; -.
DR BioGRID-ORCS; 170791; 21 hits in 74 CRISPR screens.
DR ChiTaRS; Rbm39; mouse.
DR EvolutionaryTrace; Q8VH51; -.
DR PRO; PR:Q8VH51; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VH51; protein.
DR Bgee; ENSMUSG00000027620; Expressed in metanephric cortical collecting duct and 268 other tissues.
DR ExpressionAtlas; Q8VH51; baseline and differential.
DR Genevisible; Q8VH51; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050733; F:RS domain binding; IPI:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR029123; RBM39_linker.
DR InterPro; IPR006509; RBM39_SF.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF15519; RBM39linker; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01622; SF-CC1; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CHAIN 2..530
FT /note="RNA-binding protein 39"
FT /id="PRO_0000081815"
FT DOMAIN 153..230
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 250..328
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 445..508
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..406
FT /note="Interaction with JUN"
FT /evidence="ECO:0000269|PubMed:11704680"
FT REGION 291..355
FT /note="Activating domain"
FT REGION 355..406
FT /note="Interaction with ESR1 and ESR2"
FT /evidence="ECO:0000269|PubMed:11704680"
FT REGION 406..530
FT /note="Interaction with NCOA6"
FT /evidence="ECO:0000269|PubMed:11704680"
FT COMPBIAS 9..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..92
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 95
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005821"
FT VAR_SEQ 392..397
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11704680,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005822"
FT CONFLICT 194
FT /note="K -> R (in Ref. 1; AAL32373)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="P -> R (in Ref. 1; AAL32373)"
FT /evidence="ECO:0000305"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:3S6E"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:3S6E"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:2LQ5"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:3S6E"
FT TURN 455..458
FT /evidence="ECO:0007829|PDB:3S6E"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:3S6E"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:3S6E"
FT HELIX 481..491
FT /evidence="ECO:0007829|PDB:3S6E"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:3S6E"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:3S6E"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:3S6E"
SQ SEQUENCE 530 AA; 59407 MW; 0CC6103096B7A040 CRC64;
MADDIDIEAM LEAPYKKDEN KLNSANGHEE RSKKRKKSKS RSRSHERKRS KSKERKRSRD
RERKKSKSRE RKRSRSKERR RSRSRSRDRR FRGRYRSPYS GPKFNSAIRG KIGLPHSIKL
SRRRSRSKSP FRKDKSPVRE PIDNLTPEER DARTVFCMQL AARIRPRDLE EFFSTVGKVR
DVRMISDRNS RRSKGIAYVE FVDVSSVPLA IGLTGQRVLG VPIIVQASQA EKNRAAAMAN
NLQKGSAGPM RLYVGSLHFN ITEDMLRGIF EPFGRIESIQ LMMDSETGRS KGYGFITFSD
SECAKKALEQ LNGFELAGRP MKVGHVTERT DASSASSFLD SDELERTGID LGTTGRLQLM
ARLAEGTGLQ IPPAAQQALQ MSGSLAFGAV AEFSFVIDLQ TRLSQQTEAS ALAAAASVQP
LATQCFQLSN MFNPQTEEEV GWDTEIKDDV IEECNKHGGV IHIYVDKNSA QGNVYVKCPS
IAAAIAAVNA LHGRWFAGKM ITAAYVPLPT YHNLFPDSMT ATQLLVPSRR
