ID ZMYM2_MOUSE Reviewed; 1376 AA.
AC Q9CU65; B2RUS2; Q3UUZ8; Q3UXK7; Q80XP0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 160.
DE RecName: Full=Zinc finger MYM-type protein 2;
DE AltName: Full=Zinc finger protein 198;
GN Name=Zmym2; Synonyms=Zfp198, Znf198;
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=C57BL/6J; TISSUE=Muellerian duct, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1375, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1063 AND THR-1375, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, 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 [5]
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF 257-GLY--ASP-1376.
RX PubMed=32891193; DOI=10.1016/j.ajhg.2020.08.013;
RA Connaughton D.M., Dai R., Owen D.J., Marquez J., Mann N.,
RA Graham-Paquin A.L., Nakayama M., Coyaud E., Laurent E.M.N.,
RA St-Germain J.R., Blok L.S., Vino A., Klaembt V., Deutsch K., Wu C.W.,
RA Kolvenbach C.M., Kause F., Ottlewski I., Schneider R., Kitzler T.M.,
RA Majmundar A.J., Buerger F., Onuchic-Whitford A.C., Youying M., Kolb A.,
RA Salmanullah D., Chen E., van der Ven A.T., Rao J., Ityel H., Seltzsam S.,
RA Rieke J.M., Chen J., Vivante A., Hwang D.Y., Kohl S., Dworschak G.C.,
RA Hermle T., Alders M., Bartolomaeus T., Bauer S.B., Baum M.A.,
RA Brilstra E.H., Challman T.D., Zyskind J., Costin C.E., Dipple K.M.,
RA Duijkers F.A., Ferguson M., Fitzpatrick D.R., Fick R., Glass I.A.,
RA Hulick P.J., Kline A.D., Krey I., Kumar S., Lu W., Marco E.J.,
RA Wentzensen I.M., Mefford H.C., Platzer K., Povolotskaya I.S., Savatt J.M.,
RA Shcherbakova N.V., Senguttuvan P., Squire A.E., Stein D.R., Thiffault I.,
RA Voinova V.Y., Somers M.J.G., Ferguson M.A., Traum A.Z., Daouk G.H.,
RA Daga A., Rodig N.M., Terhal P.A., van Binsbergen E., Eid L.A., Tasic V.,
RA Rasouly H.M., Lim T.Y., Ahram D.F., Gharavi A.G., Reutter H.M., Rehm H.L.,
RA MacArthur D.G., Lek M., Laricchia K.M., Lifton R.P., Xu H., Mane S.M.,
RA Sanna-Cherchi S., Sharrocks A.D., Raught B., Fisher S.E., Bouchard M.,
RA Khokha M.K., Shril S., Hildebrandt F.;
RT "Mutations of the transcriptional corepressor ZMYM2 cause syndromic urinary
RT tract malformations.";
RL Am. J. Hum. Genet. 107:727-742(2020).
CC -!- FUNCTION: Involved in the negative regulation of transcription.
CC {ECO:0000250|UniProtKB:Q9UBW7}.
CC -!- SUBUNIT: Can form homodimers (By similarity). May be a component of a
CC BHC histone deacetylase complex that contains HDAC1, HDAC2,
CC HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3,
CC GSE1 and GTF2I. Interacts with FOXP1 and FOXP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBW7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UBW7}.
CC -!- TISSUE SPECIFICITY: Low but widespread expression is detected in the
CC developing kidney. {ECO:0000269|PubMed:32891193}.
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DR EMBL; AK017929; BAB31008.1; -; mRNA.
DR EMBL; AK135499; BAE22556.1; -; mRNA.
DR EMBL; AK137708; BAE23471.1; -; mRNA.
DR EMBL; AK137720; BAE23475.1; -; mRNA.
DR EMBL; BC043450; AAH43450.1; -; mRNA.
DR EMBL; BC141403; AAI41404.1; -; mRNA.
DR CCDS; CCDS49506.1; -.
DR RefSeq; NP_083774.2; NM_029498.3.
DR RefSeq; XP_006519728.1; XM_006519665.3.
DR RefSeq; XP_017171710.1; XM_017316221.1.
DR AlphaFoldDB; Q9CU65; -.
DR SMR; Q9CU65; -.
DR BioGRID; 217903; 18.
DR DIP; DIP-29928N; -.
DR IntAct; Q9CU65; 4.
DR MINT; Q9CU65; -.
DR STRING; 10090.ENSMUSP00000022511; -.
DR iPTMnet; Q9CU65; -.
DR PhosphoSitePlus; Q9CU65; -.
DR SwissPalm; Q9CU65; -.
DR EPD; Q9CU65; -.
DR jPOST; Q9CU65; -.
DR MaxQB; Q9CU65; -.
DR PaxDb; 10090-ENSMUSP00000022511; -.
DR PeptideAtlas; Q9CU65; -.
DR ProteomicsDB; 299567; -.
DR Pumba; Q9CU65; -.
DR Antibodypedia; 22277; 176 antibodies from 23 providers.
DR DNASU; 76007; -.
DR Ensembl; ENSMUST00000022511.10; ENSMUSP00000022511.9; ENSMUSG00000021945.10.
DR GeneID; 76007; -.
DR KEGG; mmu:76007; -.
DR UCSC; uc007ucs.1; mouse.
DR AGR; MGI:1923257; -.
DR CTD; 7750; -.
DR MGI; MGI:1923257; Zmym2.
DR VEuPathDB; HostDB:ENSMUSG00000021945; -.
DR eggNOG; ENOG502QQQ9; Eukaryota.
DR GeneTree; ENSGT00940000157028; -.
DR HOGENOM; CLU_004099_0_0_1; -.
DR InParanoid; Q9CU65; -.
DR OMA; KEPTCHF; -.
DR OrthoDB; 5399298at2759; -.
DR PhylomeDB; Q9CU65; -.
DR TreeFam; TF336988; -.
DR BioGRID-ORCS; 76007; 10 hits in 86 CRISPR screens.
DR ChiTaRS; Zmym2; mouse.
DR PRO; PR:Q9CU65; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CU65; Protein.
DR Bgee; ENSMUSG00000021945; Expressed in manus and 231 other cell types or tissues.
DR ExpressionAtlas; Q9CU65; baseline and differential.
DR Genevisible; Q9CU65; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR010507; Znf_MYM.
DR PANTHER; PTHR45736; ZINC FINGER MYM-TYPE PROTEIN; 1.
DR PANTHER; PTHR45736:SF6; ZINC FINGER MYM-TYPE PROTEIN 2; 1.
DR Pfam; PF12012; DUF3504; 1.
DR Pfam; PF06467; zf-FCS; 8.
DR SMART; SM00746; TRASH; 9.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1376
FT /note="Zinc finger MYM-type protein 2"
FT /id="PRO_0000191383"
FT ZN_FING 326..362
FT /note="MYM-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 368..408
FT /note="MYM-type 2"
FT /evidence="ECO:0000255"
FT ZN_FING 420..455
FT /note="MYM-type 3"
FT /evidence="ECO:0000255"
FT ZN_FING 462..501
FT /note="MYM-type 4"
FT /evidence="ECO:0000255"
FT ZN_FING 532..569
FT /note="MYM-type 5"
FT /evidence="ECO:0000255"
FT ZN_FING 635..670
FT /note="MYM-type 6"
FT /evidence="ECO:0000255"
FT ZN_FING 722..757
FT /note="MYM-type 7"
FT /evidence="ECO:0000255"
FT ZN_FING 763..798
FT /note="MYM-type 8"
FT /evidence="ECO:0000255"
FT REGION 30..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1375
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 347
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 502
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 531
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 575
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 602
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 657
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 687
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 708
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 763
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 787
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 811
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT CROSSLNK 828
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW7"
FT MUTAGEN 257..1376
FT /note="Missing: Heterozygous mutant mice show anomalies of
FT the kidney and urinary tract."
FT /evidence="ECO:0000269|PubMed:32891193"
SQ SEQUENCE 1376 AA; 154642 MW; 1D4955422F0646B4 CRC64;
MDTSSVGTLE LTDQTPVLLG STAMATSLTN VGNSFSGPPN PLVSRSSKFQ NSSVEDDDDV
VFIEPVQPPP SSAPLVADQR PITFTSSKNE ELQGNDPKIL PSSKELAPQK GSVSETIVID
DEEDMETNQG QEKSSSNFIE RRPSETKNRT NDVDFSSSTF SRSKVNAGVS NSGITTEPDS
EIQIANVTTL ETGVSSVSDG QLESTDGRDM NLMITHVTSL HNTSLGDGSN GLQSSNFGVN
IQTYTPSLTS QTKAGVGPFN PGRMNVAGDV FQNGESAPHH NPDSWISQSA SFPRNQKQQG
VDSLSPVASL PKQIFQPSNQ QPTKPVKVTC ANCKKPLQKG QTAYQRKGSA HLFCSTTCLS
SFSHKPAPKK LCVMCKKDIT TMKGTIVAQV DSSESFQEFC STSCLSLYED KQSPAKGALN
KSRCTICGKL TEIRHEVSFK NMTHKLCSDH CFNRYRMANG LIMNCCEQCG EYLPSKGAGN
NVLVVDGQQK RFCCQSCVTE YKQVGSHPSF LKEVRDHMQD SFLMQPEKYG KLTTCTGCRT
QCRFFDMTQC IGPNGYMEPY CSTACMNSHK TKYAKSQSLG IICHFCKRNS LPQYQATMPD
GKLYNFCNSS CVAKFQALSM QSSPNGQFVA PSDIQLKCNY CKNSFCSKPE ILEWENKVHQ
FCSKTCSDDY KKLHCIVTYC EYCQEEKTLH ETVNFSGVKR PFCSEGCKLL YKQDFARRLG
LRCVTCNYCS QLCKKGATKE LDGVVRDFCS EDCCKKFQEW YYKAARCDCC KSQGTLKERV
QWRGEMKHFC DQHCLLRFYC QQNEPNMTTQ KGPENLHYDQ GCQTSRTKMT GSAPPPSPTP
NKEMKNKAIL CKPLTMTKAT YCKPHMQTKS CQTDENWKTE YVPVPIPVPV YVPVPMHMYS
QNIPVPTTVP VPVPVPVFLP APLDSSEKIP ATVEDLKSKV SSDPLDSELL TMTDMMTEEE
GKAEASNINS VIIETDIIGS DLTKNSDPDI QSNMPDVPYE PDLDIEIDFP RAAEELDMEN
EFLLPPVFGE EYEEQPRPRS KKKGTKRKAV SGYQSHDDSS DNSECSFPFK YTYGVNAWKH
WVKTRQLDED LLVLDELKSS KSVKLKEDLL SHTTAELNYG LAHFVNEIRR PNGENYAPDS
IYYLCLGIQE YLCGSNRKDN IFIDPGYQMF EQELNKILRS WQPSILPDGS IFSRVEEDYL
WRIKQLGSHS PVALLNTLFY FNTKYFGLKT VEQHLRLSFG TVFRHWKKNP LTMENKACLR
YQVSSLCGTD NEDKIATGKR KHEDDEPVFE QVENTANPSR CPVKMFECYL SKSPQNLNQR
MDVFYLQPEC SSSTDSPVWY TSTSLDRNTL ENMLVRVLLV KDIYDKDNYE LDEDTD
//
