PR40A_MOUSE
ID PR40A_MOUSE Reviewed; 953 AA.
AC Q9R1C7; Q61049; Q8BQ76; Q8BRW4; Q8C2U1;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Pre-mRNA-processing factor 40 homolog A;
DE AltName: Full=Formin-binding protein 11;
DE Short=FBP-11;
DE AltName: Full=Formin-binding protein 3;
GN Name=Prpf40a; Synonyms=Fbp11, Fnbp3;
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] (ISOFORM 1).
RA Bedford M.T., Das R., Reed R., Leder P.;
RT "FBP11, a mammalian ortholog of the essential yeast splicing factor
RT PRP40.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-380 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 647-953.
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Aorta, Embryonic spinal ganglion, Thymus, and Vein;
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 [MRNA] OF 146-212, AND INTERACTION WITH FORMIN.
RC STRAIN=FVB/NJ;
RX PubMed=8605874; DOI=10.1002/j.1460-2075.1996.tb00442.x;
RA Chan D.C., Bedford M.T., Leder P.;
RT "Formin binding proteins bear WWP/WW domains that bind proline-rich
RT peptides and functionally resemble SH3 domains.";
RL EMBO J. 15:1045-1054(1996).
RN [4]
RP INTERACTION WITH SF1; SRPK1; ENAH; ATBF1 AND MECP2.
RX PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA Bedford M.T., Chan D.C., Leder P.;
RT "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-
RT rich ligands.";
RL EMBO J. 16:2376-2383(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASL.
RX PubMed=14697212; DOI=10.1016/j.bbrc.2003.11.139;
RA Mizutani K., Suetsugu S., Takenawa T.;
RT "FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-
RT dependent microspike formation.";
RL Biochem. Biophys. Res. Commun. 313:468-474(2004).
RN [6]
RP INTERACTION WITH AKAP8L, AND SUBCELLULAR LOCATION.
RX PubMed=16391387; DOI=10.1385/nmm:7:4:297;
RA Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.;
RT "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin:
RT implications for nuclear toxicity in Huntington's disease pathogenesis.";
RL NeuroMolecular Med. 7:297-310(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-928; SER-929; SER-931 AND
RP SER-934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; THR-928; SER-929; SER-931
RP AND SER-934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196, 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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-9, AND IDENTIFICATION BY MASS
RP 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 WASL/N-WASP and suppresses its translocation from
CC the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic
CC function. Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the control of cell shape and
CC migration. May play a role in cytokinesis. May be involved in pre-mRNA
CC splicing. {ECO:0000269|PubMed:14697212}.
CC -!- SUBUNIT: Interacts with the N-terminus of HTT and with the
CC phosphorylated C-terminal domain of POLR2A (By similarity). Interacts
CC with AKAP8L, SF1, SRPK1, ENAH, ATBF1 and MECP2. Interacts through the
CC WW domains with formin proline-rich regions and with WASL/N-WASP.
CC {ECO:0000250, ECO:0000269|PubMed:14697212, ECO:0000269|PubMed:16391387,
CC ECO:0000269|PubMed:8605874, ECO:0000269|PubMed:9171351}.
CC -!- INTERACTION:
CC Q9R1C7; Q9ULX6: AKAP8L; Xeno; NbExp=3; IntAct=EBI-645554, EBI-357530;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Nucleus matrix. Note=Colocalizes
CC with AKAP8L in the nuclear matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9R1C7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R1C7-2; Sequence=VSP_008049;
CC -!- DOMAIN: The WW domains are essential for localization to nuclear
CC speckles.
CC -!- SIMILARITY: Belongs to the PRPF40 family. {ECO:0000305}.
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DR EMBL; AF135439; AAD39463.1; -; mRNA.
DR EMBL; AK041205; BAC30863.1; -; mRNA.
DR EMBL; AK051375; BAC34617.1; -; mRNA.
DR EMBL; AK087963; BAC40061.2; -; mRNA.
DR EMBL; U40747; AAC52475.1; -; mRNA.
DR PIR; S64713; S64713.
DR RefSeq; NP_061255.1; NM_018785.2.
DR AlphaFoldDB; Q9R1C7; -.
DR BMRB; Q9R1C7; -.
DR SMR; Q9R1C7; -.
DR BioGRID; 207833; 28.
DR ELM; Q9R1C7; -.
DR IntAct; Q9R1C7; 5.
DR MINT; Q9R1C7; -.
DR STRING; 10090.ENSMUSP00000075655; -.
DR iPTMnet; Q9R1C7; -.
DR PhosphoSitePlus; Q9R1C7; -.
DR EPD; Q9R1C7; -.
DR jPOST; Q9R1C7; -.
DR MaxQB; Q9R1C7; -.
DR PaxDb; Q9R1C7; -.
DR PeptideAtlas; Q9R1C7; -.
DR PRIDE; Q9R1C7; -.
DR ProteomicsDB; 289391; -. [Q9R1C7-1]
DR ProteomicsDB; 289392; -. [Q9R1C7-2]
DR Antibodypedia; 33687; 93 antibodies from 17 providers.
DR DNASU; 56194; -.
DR Ensembl; ENSMUST00000239398; ENSMUSP00000159339; ENSMUSG00000061136. [Q9R1C7-1]
DR GeneID; 56194; -.
DR KEGG; mmu:56194; -.
DR UCSC; uc008jrk.2; mouse. [Q9R1C7-1]
DR CTD; 55660; -.
DR MGI; MGI:1860512; Prpf40a.
DR VEuPathDB; HostDB:ENSMUSG00000061136; -.
DR eggNOG; KOG0152; Eukaryota.
DR GeneTree; ENSGT00930000150980; -.
DR HOGENOM; CLU_005825_0_0_1; -.
DR InParanoid; Q9R1C7; -.
DR OrthoDB; 1112854at2759; -.
DR PhylomeDB; Q9R1C7; -.
DR TreeFam; TF318732; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 56194; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Prpf40a; mouse.
DR PRO; PR:Q9R1C7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9R1C7; protein.
DR Bgee; ENSMUSG00000061136; Expressed in embryonic post-anal tail and 268 other tissues.
DR ExpressionAtlas; Q9R1C7; baseline and differential.
DR Genevisible; Q9R1C7; MM.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0070064; F:proline-rich region binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR CDD; cd00201; WW; 2.
DR Gene3D; 1.10.10.440; -; 5.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR039726; Prp40-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11864; PTHR11864; 1.
DR Pfam; PF01846; FF; 5.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00441; FF; 5.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF81698; SSF81698; 5.
DR PROSITE; PS51676; FF; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..953
FT /note="Pre-mRNA-processing factor 40 homolog A"
FT /id="PRO_0000076086"
FT DOMAIN 140..173
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 181..214
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 389..443
FT /note="FF 1"
FT DOMAIN 456..510
FT /note="FF 2"
FT DOMAIN 523..583
FT /note="FF 3"
FT DOMAIN 603..663
FT /note="FF 4"
FT DOMAIN 668..723
FT /note="FF 5"
FT DOMAIN 738..795
FT /note="FF 6"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..823
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..877
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT MOD_RES 928
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75400"
FT VAR_SEQ 14..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008049"
FT CONFLICT 334
FT /note="E -> A (in Ref. 2; BAC40061)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="T -> I (in Ref. 2; BAC40061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 108481 MW; 3C627AB7404D2285 CRC64;
MRPGTGAERG GLMVSEMESQ PPSRGPGDGE RRLSGSNLCS SSWVSADGFL RRRPSMGHPG
MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM PGMMSSVMSG MMMSHMSQAS
MQPALPPGVN SMDVAAGAAS GAKSMWTEHK SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ
LLSKCPWKEY KSDSGKPYYY NSQTKESRWA KPKELEDLEG YQNTIVAGGL ITKSNLHAMI
KAEESSKQEE CTTASTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA ANANTSTTPT
NTVGSVPVAP EPEVTSIVAT AVDNENTVTV STEEQAQLAN TTAIQDLSGD ISSNTGEEPA
KQETVSDFTP KKEEEESQPA KKTYTWNTKE EAKQAFKELL KEKRVPSNAS WEQAMKMIIN
DPRYSALAKL SEKKQAFNAY KVQTEKEEKE EARSKYKEAK ESFQRFLENH EKMTSTTRYK
KAEQMFGEME VWNAISERDR LEIYEDVLFF LSKKEKEQAK QLRKRNWEAL KNILDNMANV
TYSTTWSEAQ QYLMDNPTFA EDEELQNMDK EDALICFEEH IRALEKEEEE EKQKTLLRER
RRQRKNRESF QIFLDELHEH GQLHSMSSWM ELYPTISSDI RFTNMLGQPG STALDLFKFY
VEDLKARYHD EKKIIKDILK DKGFVVEVNT TFEDFVAIIS STKRSTTLDA GNIKLAFNSL
LEKAEARERE REKEEARKMK RKESAFKSML KQATPPIELD AVWEDIRERF VKEPAFEDIT
LESERKRIFK DFMHVLEHEC QHHHSKNKKH SKKSKKHHRK RSRSRSGSES DDDDSHSKKK
RQRSESHSAS ERSSSAESER SYKKSKKHKK KSKKRRHKSD SPESDTEREK DKKEKDRDSE
KDRSRQRSES KHKSPKKKTG KDSGNWDTSG SELSEGELEK RRRTLLEQLD DDQ
