GenomeNet

Database: UniProt
Entry: Q9EQQ0
LinkDB: Q9EQQ0
Original site: Q9EQQ0 
ID   SUV92_MOUSE             Reviewed;         477 AA.
AC   Q9EQQ0; Q8BNK2; Q9CUK3; Q9JLP7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   13-FEB-2019, entry version 155.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H2;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 2;
DE            Short=H3-K9-HMTase 2;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 2;
DE            Short=Su(var)3-9 homolog 2;
GN   Name=Suv39h2;
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 [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=11094092; DOI=10.1128/MCB.20.24.9423-9433.2000;
RA   O'Carroll D., Scherthan H., Peters A.H.F.M., Opravil S., Haynes A.R.,
RA   Laible G., Rea S., Schmid M., Lebersorger A., Jerratsch M.,
RA   Sattler L., Mattei M.-G., Denny P., Brown S.D.M., Schweizer D.,
RA   Jenuwein T.;
RT   "Isolation and characterization of Suv39h2, a second histone H3
RT   methyltransferase gene that displays testis-specific expression.";
RL   Mol. Cell. Biol. 20:9423-9433(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11701123; DOI=10.1016/S0092-8674(01)00542-6;
RA   Peters A.H.F.M., O'Carroll D., Scherthan H., Mechtler K., Sauer S.,
RA   Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A.,
RA   Opravil S., Doyle M., Sibilia M., Jenuwein T.;
RT   "Loss of the Suv39h histone methyltransferases impairs mammalian
RT   heterochromatin and genome stability.";
RL   Cell 107:323-337(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=14690609; DOI=10.1016/S1097-2765(03)00477-5;
RA   Peters A.H.F.M., Kubicek S., Mechtler K., O'Sullivan R.J.,
RA   Derijck A.A., Perez-Burgos L., Kohlmaier A., Opravil S., Tachibana M.,
RA   Shinkai Y., Martens J.H.A., Jenuwein T.;
RT   "Partitioning and plasticity of repressive histone methylation states
RT   in mammalian chromatin.";
RL   Mol. Cell 12:1577-1589(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=14690610; DOI=10.1016/S1097-2765(03)00479-9;
RA   Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J.,
RA   Hunt D.F., Shinkai Y., Allis C.D.;
RT   "Histone methyltransferases direct different degrees of methylation to
RT   define distinct chromatin domains.";
RL   Mol. Cell 12:1591-1598(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=14702045; DOI=10.1038/ng1278;
RA   Garcia-Cao M., O'Sullivan R., Peters A.H.F.M., Jenuwein T.,
RA   Blasco M.A.;
RT   "Epigenetic regulation of telomere length in mammalian cells by the
RT   Suv39h1 and Suv39h2 histone methyltransferases.";
RL   Nat. Genet. 36:94-99(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER
RP   COMPLEX.
RX   PubMed=24413057; DOI=10.1038/nsmb.2746;
RA   Duong H.A., Weitz C.J.;
RT   "Temporal orchestration of repressive chromatin modifiers by circadian
RT   clock Period complexes.";
RL   Nat. Struct. Mol. Biol. 21:126-132(2014).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
CC       9' as substrate. H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting HP1
CC       (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly
CC       functions in heterochromatin regions, thereby playing a central
CC       role in the establishment of constitutive heterochromatin at
CC       pericentric and telomere regions. H3 'Lys-9' trimethylation is
CC       also required to direct DNA methylation at pericentric repeats.
CC       SUV39H1 is targeted to histone H3 via its interaction with RB1 and
CC       is involved in many processes, such as cell cycle regulation,
CC       transcriptional repression and regulation of telomere length. May
CC       participate in regulation of higher-order chromatin organization
CC       during spermatogenesis. Recruited by the large PER complex to the
CC       E-box elements of the circadian target genes such as PER2 itself
CC       or PER1, contributes to the conversion of local chromatin to a
CC       heterochromatin-like repressive state through H3 'Lys-9'
CC       trimethylation. {ECO:0000269|PubMed:11701123,
CC       ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610,
CC       ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:24413057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00912};
CC   -!- SUBUNIT: Interacts with SMAD5. The large PER complex involved in
CC       the histone methylation is composed of at least PER2, CBX3,
CC       TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the
CC       complex.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC       Note=Associates with centromeric constitutive heterochromatin
CC       during most stages of spermato- and spermiogenesis. Predominantly
CC       accumulates at the sex chromosomes present at the XY body.
CC   -!- TISSUE SPECIFICITY: Testis specific; predominant expression in
CC       type B spermatogonia and preleptotene spermatocytes.
CC   -!- DEVELOPMENTAL STAGE: Strong expression in early embryos with a
CC       peak at 10.5 dpc. Expression is down-regulated at 17.5 dpc, and is
CC       nearly absent during postnatal development. In adult testes,
CC       prominent expression in late but not early spermatocytes.
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both pre-SET and post-SET domains are required
CC       for methyltransferase activity. The SET domain also participates
CC       in stable binding to heterochromatin (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Suv39h1 and Suv39h2 display
CC       severely impaired viability and chromosomal instabilities that are
CC       associated with an increased tumor risk and perturbed chromosome
CC       interactions during male meiosis. They also show a higher level of
CC       histone H3 with phosphorylated 'Ser-10' and a reduced number of
CC       cells in G1 phase and an increased portion of cells with aberrant
CC       nuclear morphologies. {ECO:0000269|PubMed:11701123}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00912}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF73152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF149204; AAF73152.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF149205; AAG09134.1; -; mRNA.
DR   EMBL; AK015728; BAB29948.1; -; mRNA.
DR   EMBL; AK083457; BAC38921.1; -; mRNA.
DR   EMBL; AL732620; CAM16043.1; -; Genomic_DNA.
DR   CCDS; CCDS15652.1; -.
DR   RefSeq; NP_073561.2; NM_022724.4.
DR   UniGene; Mm.128273; -.
DR   UniGene; Mm.23483; -.
DR   ProteinModelPortal; Q9EQQ0; -.
DR   SMR; Q9EQQ0; -.
DR   BioGrid; 211103; 2.
DR   DIP; DIP-32586N; -.
DR   IntAct; Q9EQQ0; 3.
DR   STRING; 10090.ENSMUSP00000027956; -.
DR   iPTMnet; Q9EQQ0; -.
DR   PhosphoSitePlus; Q9EQQ0; -.
DR   EPD; Q9EQQ0; -.
DR   MaxQB; Q9EQQ0; -.
DR   PaxDb; Q9EQQ0; -.
DR   PeptideAtlas; Q9EQQ0; -.
DR   PRIDE; Q9EQQ0; -.
DR   GeneID; 64707; -.
DR   KEGG; mmu:64707; -.
DR   UCSC; uc008ied.2; mouse.
DR   CTD; 79723; -.
DR   MGI; MGI:1890396; Suv39h2.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000231244; -.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; Q9EQQ0; -.
DR   KO; K11419; -.
DR   OrthoDB; 753093at2759; -.
DR   PhylomeDB; Q9EQQ0; -.
DR   TreeFam; TF106452; -.
DR   PRO; PR:Q9EQQ0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008276; F:protein methyltransferase activity; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0036123; P:histone H3-K9 dimethylation; IMP:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IGI:MGI.
DR   GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:UniProtKB.
DR   GO; GO:0034968; P:histone lysine methylation; IGI:MGI.
DR   GO; GO:0007140; P:male meiotic nuclear division; IEP:UniProtKB.
DR   GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   CDD; cd00024; CHROMO; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF009343; SUV39_SET; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Biological rhythms; Cell cycle; Centromere; Chromatin regulator;
KW   Chromosome; Complete proteome; Differentiation; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN         1    477       Histone-lysine N-methyltransferase
FT                                SUV39H2.
FT                                /FTId=PRO_0000186060.
FT   DOMAIN      118    176       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      256    314       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      317    440       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      461    477       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      328    330       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      397    398       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       258    258       Zinc 1. {ECO:0000250}.
FT   METAL       258    258       Zinc 2. {ECO:0000250}.
FT   METAL       260    260       Zinc 1. {ECO:0000250}.
FT   METAL       263    263       Zinc 1. {ECO:0000250}.
FT   METAL       263    263       Zinc 3. {ECO:0000250}.
FT   METAL       268    268       Zinc 1. {ECO:0000250}.
FT   METAL       269    269       Zinc 1. {ECO:0000250}.
FT   METAL       269    269       Zinc 2. {ECO:0000250}.
FT   METAL       296    296       Zinc 2. {ECO:0000250}.
FT   METAL       296    296       Zinc 3. {ECO:0000250}.
FT   METAL       300    300       Zinc 2. {ECO:0000250}.
FT   METAL       302    302       Zinc 3. {ECO:0000250}.
FT   METAL       306    306       Zinc 3. {ECO:0000250}.
FT   METAL       400    400       Zinc 4. {ECO:0000250}.
FT   METAL       465    465       Zinc 4. {ECO:0000250}.
FT   METAL       467    467       Zinc 4. {ECO:0000250}.
FT   METAL       472    472       Zinc 4. {ECO:0000250}.
FT   BINDING     371    371       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     448    448       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   MOD_RES     451    451       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   MOD_RES     455    455       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CONFLICT      3      3       T -> A (in Ref. 2; BAC38921).
FT                                {ECO:0000305}.
FT   CONFLICT    131    131       Missing (in Ref. 1; AAF73152).
FT                                {ECO:0000305}.
FT   CONFLICT    323    323       K -> R (in Ref. 2; BAB29948/BAC38921).
FT                                {ECO:0000305}.
FT   CONFLICT    325    325       S -> N (in Ref. 1; AAF73152).
FT                                {ECO:0000305}.
SQ   SEQUENCE   477 AA;  54098 MW;  4008D46CF0F07006 CRC64;
     MATARAKARG SEAGARCHRA PGPPPRPKAR RTARRRRAET LTARRSRPSA GERRAGSQRA
     WSGAPRAAVF GDECARGALF KAWCVPCLVS LDTLQELCRK EKLTCKSIGI TKRNLNNYEV
     EYLCDYKVAK GVEYYLVKWK GWPDSTNTWE PLRNLRCPQL LRQFSDDKKT YLAQERKCKA
     VNSKSLQPAI AEYIVQKAKQ RIALQRWQDY LNRRKNHKGM IFVENTVDLE GPPLDFYYIN
     EYRPAPGISI NSEATFGCSC TDCFFDKCCP AEAGVVLAYN KKQQIKIQPG TPIYECNSRC
     RCGPECPNRI VQKGTQYSLC IFKTSNGCGW GVKTLVKIKR MSFVMEYVGE VITSEEAERR
     GQFYDNKGIT YLFDLDYESD EFTVDAARYG NVSHFVNHSC DPNLQVFSVF IDNLDTRLPR
     IALFSTRTIN AGEELTFDYQ MKGSGEASSD SIDHSPAKKR VRTQCKCGAE TCRGYLN
//
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