GenomeNet

Database: UniProt/SWISS-PROT
Entry: KMT5B_MOUSE
LinkDB: KMT5B_MOUSE
Original site: KMT5B_MOUSE 
ID   KMT5B_MOUSE             Reviewed;         883 AA.
AC   Q3U8K7; Q3UTP6; Q6DI74; Q6Q784; Q8BU67; Q8BUN0; Q8BUT7; Q8BW73;
AC   Q8BZ24; Q91X81;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   10-MAY-2017, entry version 101.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5B {ECO:0000305};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methyltransferase 5B {ECO:0000250|UniProtKB:Q4FZB7};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 1;
DE            Short=Su(var)4-20 homolog 1;
DE            Short=Suv4-20h1;
GN   Name=Kmt5b {ECO:0000250|UniProtKB:Q4FZB7}; Synonyms=Suv420h1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5.
RC   STRAIN=C57BL/6J;
RX   PubMed=15145825; DOI=10.1101/gad.300704;
RA   Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA   Reinberg D., Jenuwein T.;
RT   "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT   constitutive heterochromatin.";
RL   Genes Dev. 18:1251-1262(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cerebellum, Hippocampus, Lung, Oviduct, and
RC   Vagina;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH RB1; RBL1 AND RBL2.
RX   PubMed=15750587; DOI=10.1038/ncb1235;
RA   Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M.,
RA   Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T.,
RA   Blasco M.A.;
RT   "Role of the RB1 family in stabilizing histone methylation at
RT   constitutive heterochromatin.";
RL   Nat. Cell Biol. 7:420-428(2005).
RN   [5]
RP   INTERACTION WITH RB1; RBL1 AND RBL2.
RX   PubMed=16612004; DOI=10.1128/MCB.26.9.3659-3671.2006;
RA   Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A.,
RA   Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G.,
RA   Dyson N.J., Dick F.A.;
RT   "The retinoblastoma protein regulates pericentric heterochromatin.";
RL   Mol. Cell. Biol. 26:3659-3671(2006).
RN   [6]
RP   FUNCTION, INTERACTION WITH FRG1, AND DISRUPTION PHENOTYPE.
RX   PubMed=23720823; DOI=10.1093/jmcb/mjt018;
RA   Neguembor M.V., Xynos A., Onorati M.C., Caccia R., Bortolanza S.,
RA   Godio C., Pistoni M., Corona D.F., Schotta G., Gabellini D.;
RT   "FSHD muscular dystrophy region gene 1 binds Suv4-20h1 histone
RT   methyltransferase and impairs myogenesis.";
RL   J. Mol. Cell Biol. 5:294-307(2013).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression. Mainly functions in pericentric heterochromatin
CC       regions, thereby playing a central role in the establishment of
CC       constitutive heterochromatin in these regions. KMT5B is targeted
CC       to histone H3 via its interaction with RB1 family proteins (RB1,
CC       RBL1 and RBL2). Plays a role in myogenesis by regulating the
CC       expression of target genes, such as EID3.
CC       {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:23720823}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00903,
CC       ECO:0000269|PubMed:15145825}.
CC   -!- SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5.
CC       Interacts with RB1 family proteins RB1, RBL1 and RBL2. Interacts
CC       (via C-terminus) with FRG1. {ECO:0000269|PubMed:15145825,
CC       ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004,
CC       ECO:0000269|PubMed:23720823}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15145825}.
CC       Chromosome {ECO:0000269|PubMed:15145825}. Note=Associated with
CC       pericentric heterochromatin. CBX1 and CBX5 are required for the
CC       localization to pericentric heterochromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q3U8K7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U8K7-2; Sequence=VSP_024055, VSP_024056;
CC       Name=3;
CC         IsoId=Q3U8K7-3; Sequence=VSP_024053;
CC       Name=4;
CC         IsoId=Q3U8K7-4; Sequence=VSP_024054;
CC       Name=5;
CC         IsoId=Q3U8K7-5; Sequence=VSP_024053, VSP_024057;
CC         Note=No experimental confirmation available.;
CC   -!- DISRUPTION PHENOTYPE: Partial muscle-specific knockout mice
CC       display several signs of muscular dystrophy including necrosis and
CC       an increased number of centrally nucleated myofibers. RNAi-
CC       mediated knockdown in C2C12 muscle cells causes reduced myogenic
CC       differentiation of the cells. {ECO:0000269|PubMed:23720823}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar4-20 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00903}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11214.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAT00539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC39834.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE23934.1; Type=Erroneous termination; Positions=3; Note=Translated as Trp.; Evidence={ECO:0000305};
DR   EMBL; AY555192; AAT00539.1; ALT_INIT; mRNA.
DR   EMBL; AK036880; BAC29617.1; -; mRNA.
DR   EMBL; AK054093; BAC35652.1; -; mRNA.
DR   EMBL; AK082660; BAC38565.1; -; mRNA.
DR   EMBL; AK083227; BAC38817.1; -; mRNA.
DR   EMBL; AK087267; BAC39834.1; ALT_INIT; mRNA.
DR   EMBL; AK139255; BAE23934.1; ALT_SEQ; mRNA.
DR   EMBL; AK152179; BAE31010.1; -; mRNA.
DR   EMBL; BC011214; AAH11214.1; ALT_INIT; mRNA.
DR   EMBL; BC075709; AAH75709.1; -; mRNA.
DR   CCDS; CCDS29399.1; -. [Q3U8K7-3]
DR   CCDS; CCDS50343.1; -. [Q3U8K7-1]
DR   CCDS; CCDS50344.1; -. [Q3U8K7-2]
DR   CCDS; CCDS50345.1; -. [Q3U8K7-4]
DR   RefSeq; NP_001161356.1; NM_001167884.1. [Q3U8K7-4]
DR   RefSeq; NP_001161357.1; NM_001167885.1. [Q3U8K7-1]
DR   RefSeq; NP_001161358.1; NM_001167886.1. [Q3U8K7-3]
DR   RefSeq; NP_001161359.1; NM_001167887.1. [Q3U8K7-1]
DR   RefSeq; NP_001161360.1; NM_001167888.1. [Q3U8K7-4]
DR   RefSeq; NP_001161361.1; NM_001167889.1. [Q3U8K7-2]
DR   RefSeq; NP_659120.3; NM_144871.4. [Q3U8K7-3]
DR   RefSeq; XP_006531790.1; XM_006531727.3. [Q3U8K7-1]
DR   RefSeq; XP_006531791.1; XM_006531728.3. [Q3U8K7-1]
DR   RefSeq; XP_006531794.1; XM_006531731.2. [Q3U8K7-5]
DR   RefSeq; XP_011246925.1; XM_011248623.2. [Q3U8K7-1]
DR   RefSeq; XP_011246926.1; XM_011248624.2. [Q3U8K7-3]
DR   RefSeq; XP_017173632.1; XM_017318143.1. [Q3U8K7-1]
DR   UniGene; Mm.278578; -.
DR   PDB; 4BUP; X-ray; 2.17 A; A/B=70-336.
DR   PDBsum; 4BUP; -.
DR   ProteinModelPortal; Q3U8K7; -.
DR   SMR; Q3U8K7; -.
DR   BioGrid; 230441; 3.
DR   STRING; 10090.ENSMUSP00000109605; -.
DR   iPTMnet; Q3U8K7; -.
DR   PhosphoSitePlus; Q3U8K7; -.
DR   MaxQB; Q3U8K7; -.
DR   PaxDb; Q3U8K7; -.
DR   PeptideAtlas; Q3U8K7; -.
DR   PRIDE; Q3U8K7; -.
DR   DNASU; 225888; -.
DR   Ensembl; ENSMUST00000005518; ENSMUSP00000005518; ENSMUSG00000045098. [Q3U8K7-4]
DR   Ensembl; ENSMUST00000052699; ENSMUSP00000060162; ENSMUSG00000045098. [Q3U8K7-2]
DR   Ensembl; ENSMUST00000113968; ENSMUSP00000109601; ENSMUSG00000045098. [Q3U8K7-4]
DR   Ensembl; ENSMUST00000113970; ENSMUSP00000109603; ENSMUSG00000045098. [Q3U8K7-2]
DR   Ensembl; ENSMUST00000113972; ENSMUSP00000109605; ENSMUSG00000045098. [Q3U8K7-1]
DR   Ensembl; ENSMUST00000113973; ENSMUSP00000109606; ENSMUSG00000045098. [Q3U8K7-1]
DR   Ensembl; ENSMUST00000113974; ENSMUSP00000109607; ENSMUSG00000045098. [Q3U8K7-3]
DR   Ensembl; ENSMUST00000113977; ENSMUSP00000109610; ENSMUSG00000045098. [Q3U8K7-3]
DR   Ensembl; ENSMUST00000176262; ENSMUSP00000135563; ENSMUSG00000045098. [Q3U8K7-3]
DR   GeneID; 225888; -.
DR   KEGG; mmu:225888; -.
DR   UCSC; uc008fww.2; mouse. [Q3U8K7-4]
DR   UCSC; uc008fwz.2; mouse. [Q3U8K7-2]
DR   UCSC; uc008fxa.2; mouse. [Q3U8K7-1]
DR   UCSC; uc008fxc.2; mouse. [Q3U8K7-3]
DR   CTD; 51111; -.
DR   MGI; MGI:2444557; Kmt5b.
DR   eggNOG; KOG2589; Eukaryota.
DR   eggNOG; ENOG410XPH8; LUCA.
DR   GeneTree; ENSGT00520000055640; -.
DR   HOVERGEN; HBG105761; -.
DR   InParanoid; Q3U8K7; -.
DR   KO; K11429; -.
DR   OMA; SGCLTRH; -.
DR   OrthoDB; EOG091G0IUY; -.
DR   PhylomeDB; Q3U8K7; -.
DR   TreeFam; TF106433; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Suv420h1; mouse.
DR   PRO; PR:Q3U8K7; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000045098; -.
DR   ExpressionAtlas; Q3U8K7; baseline and differential.
DR   Genevisible; Q3U8K7; MM.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:MGI.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:MGI.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:InterPro.
DR   GO; GO:0016571; P:histone methylation; IDA:MGI.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR025790; Hist-Lys_N-MTase_Suvar4-20.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Isopeptide bond; Methyltransferase; Myogenesis;
KW   Nucleus; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT   CHAIN         1    883       Histone-lysine N-methyltransferase KMT5B.
FT                                /FTId=PRO_0000281788.
FT   DOMAIN      194    309       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   CROSSLNK    556    556       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q4FZB7}.
FT   VAR_SEQ     104    126       Missing (in isoform 3 and isoform 5).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024053.
FT   VAR_SEQ     328    883       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024054.
FT   VAR_SEQ     393    394       TS -> SK (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024055.
FT   VAR_SEQ     395    883       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024056.
FT   VAR_SEQ     831    883       EGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISS
FT                                RRREDQSLRLNA -> SGKAAEANCW (in isoform
FT                                5). {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_024057.
FT   CONFLICT     53     53       S -> N (in Ref. 3; AAH75709).
FT                                {ECO:0000305}.
FT   CONFLICT    153    153       K -> E (in Ref. 2; AAH11214).
FT                                {ECO:0000305}.
FT   CONFLICT    292    292       V -> L (in Ref. 1; BAC39834).
FT                                {ECO:0000305}.
FT   CONFLICT    328    328       R -> Q (in Ref. 2; BAE31010).
FT                                {ECO:0000305}.
FT   CONFLICT    428    428       P -> A (in Ref. 3; AAH75709).
FT                                {ECO:0000305}.
FT   CONFLICT    472    472       E -> G (in Ref. 1; BAC38817).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       N -> S (in Ref. 3; AAH75709).
FT                                {ECO:0000305}.
FT   CONFLICT    590    590       P -> H (in Ref. 1; BAC38817).
FT                                {ECO:0000305}.
FT   CONFLICT    595    595       R -> G (in Ref. 2; BAE31010).
FT                                {ECO:0000305}.
FT   CONFLICT    664    664       H -> Y (in Ref. 3; AAH75709).
FT                                {ECO:0000305}.
FT   CONFLICT    678    678       A -> T (in Ref. 3; AAH75709).
FT                                {ECO:0000305}.
FT   HELIX        75     89       {ECO:0000244|PDB:4BUP}.
FT   HELIX        91     94       {ECO:0000244|PDB:4BUP}.
FT   HELIX       138    148       {ECO:0000244|PDB:4BUP}.
FT   HELIX       151    158       {ECO:0000244|PDB:4BUP}.
FT   HELIX       162    167       {ECO:0000244|PDB:4BUP}.
FT   HELIX       173    187       {ECO:0000244|PDB:4BUP}.
FT   HELIX       188    190       {ECO:0000244|PDB:4BUP}.
FT   STRAND      196    201       {ECO:0000244|PDB:4BUP}.
FT   STRAND      208    217       {ECO:0000244|PDB:4BUP}.
FT   STRAND      224    235       {ECO:0000244|PDB:4BUP}.
FT   HELIX       237    243       {ECO:0000244|PDB:4BUP}.
FT   TURN        246    248       {ECO:0000244|PDB:4BUP}.
FT   STRAND      253    256       {ECO:0000244|PDB:4BUP}.
FT   TURN        257    260       {ECO:0000244|PDB:4BUP}.
FT   STRAND      261    267       {ECO:0000244|PDB:4BUP}.
FT   HELIX       268    271       {ECO:0000244|PDB:4BUP}.
FT   STRAND      279    296       {ECO:0000244|PDB:4BUP}.
FT   TURN        310    313       {ECO:0000244|PDB:4BUP}.
FT   HELIX       315    317       {ECO:0000244|PDB:4BUP}.
FT   HELIX       323    328       {ECO:0000244|PDB:4BUP}.
FT   HELIX       331    333       {ECO:0000244|PDB:4BUP}.
SQ   SEQUENCE   883 AA;  98580 MW;  2B24461F582CC5F1 CRC64;
     MKWLGDSKNM VVNGRRNGGK LSNDHQQNQS KLQQHSGKDT LKTGRNAVER RSSRCHGNSG
     FEGQSRYVPS SGMSAKELCE NDDLATSLVL DPYLGFQTHK MNTSAFPSRS SRHISKADSF
     SHNNPVRFRP IKGRQEELKE VIERFKKDEH LEKAFKCLTS GEWARHYFLN KNKMQEKLFK
     EHVFIYLRMF ATDSGFEILP CNRYSSEQNG AKIVATKEWK RNDKIELLVG CIAELSEIEE
     NMLLRHGEND FSVMYSTRKN CAQLWLGPAA FINHDCRPNC KFVSTGRDTA CVKALRDIEP
     GEEISCYYGD GFFGENNEFC ECYTCERRGT GAFKSRVGLP APAPVINSKY GLRETDKRLN
     RLKKLGDSSK NSDSQSVSSN TDADTTQEKD NATSNRKSSV GVKKSSKSRA LTRPSMPRVP
     AASNSTSPKL VHTNNPRVPK KLRKPAKPLL SKIRLRNHCK RLDQKSASRK LEMGSLVLKE
     PKVVLYKNLP IKKEREPEGP AHAAVGSGCL TRHAAREHRQ NHGRGAHSQG DSLPCTYTTR
     RSLRTRTGLK ETTDIKLEPS PLDGYKNGIL EPCPDSGQQP TPEVLEELAP ETAHREEASQ
     ECPKNDSCLS RKKFRQVKPV KHLAKTEDCS PEHSFPGKDG LPDLPGSHPD QGEPSGTVRV
     PVSHTDSAPS PVGCSVVAPD SFTKDSFRTA QSKKKRRVTR YDAQLILENS SGIPKLTLRR
     RHDSSSKTND HESDGVNSSK ISIKLSKDHD SDSNLYVAKL SNGVSAGPGS SSTKLKIQLK
     RDEESRGPCA EGLHENGVCC SDPLSLLESQ MEVDDYSQYE EDSTDESSSS EGEEEEEDCE
     DDFDDDFIPL PPAKRLRLIV GKDSIDIDIS SRRREDQSLR LNA
//
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