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Database: UniProt
Entry: Q8C0P7
LinkDB: Q8C0P7
Original site: Q8C0P7 
ID   ZN451_MOUSE             Reviewed;        1056 AA.
AC   Q8C0P7;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   13-FEB-2019, entry version 123.
DE   RecName: Full=E3 SUMO-protein ligase ZNF451 {ECO:0000305|PubMed:26524493};
DE            EC=2.3.2.- {ECO:0000269|PubMed:26524493};
DE   AltName: Full=E3 SUMO-protein transferase ZNF451 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 451;
GN   Name=Znf451; Synonyms=Zfp451;
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 [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   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=26524493; DOI=10.1038/nsmb.3114;
RA   Eisenhardt N., Chaugule V.K., Koidl S., Droescher M., Dogan E.,
RA   Rettich J., Sutinen P., Imanishi S.Y., Hofmann K., Palvimo J.J.,
RA   Pichler A.;
RT   "A new vertebrate SUMO enzyme family reveals insights into SUMO-chain
RT   assembly.";
RL   Nat. Struct. Mol. Biol. 22:959-967(2015).
CC   -!- FUNCTION: E3 SUMO-protein ligase; has a preference for SUMO2 and
CC       SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target
CC       proteins. Plays a role in protein SUMO2 modification in response
CC       to stress caused by DNA damage and by proteasome inhibitors (in
CC       vitro). Required for MCM4 sumoylation. Has no activity with SUMO1
CC       (PubMed:26524493). Preferentially transfers an additional SUMO2
CC       chain onto the SUMO2 consensus site 'Lys-11'. Negatively regulates
CC       transcriptional activation mediated by the SMAD4 complex in
CC       response to TGF-beta signaling. Inhibits EP300-mediated
CC       acetylation of histone H3 at 'Lys-9'. Plays a role in regulating
CC       the transcription of AR targets (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y4E5, ECO:0000269|PubMed:26524493}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000269|PubMed:26524493}.
CC   -!- SUBUNIT: Homooligomer. Interacts (via N-terminal region) with
CC       SUMO1. Interacts (via N-terminal region) with SUMO2. Interacts
CC       simultaneously with two SUMO2 chains. Identified in a complex with
CC       SUMO2 and UBE2I/UBC9, where one ZNF451 interacts with one
CC       UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9
CC       active site and the other to another region of the same UBE2I/UBC9
CC       molecule. Interacts (via C-terminus) with ubiquitin. Interacts
CC       (via N-terminal zinc-finger domains) with SMAD4 (via MH2 domain).
CC       Interacts with SMAD2 and SMAD3. Identified in a complex that
CC       contains at least ZNF451, SMAD2, SMAD3 and SMAD4. Interacts with
CC       EP300. Inhibits interaction between EP300 and the SMAD4 complex.
CC       {ECO:0000250|UniProtKB:Q9Y4E5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y4E5}.
CC       Nucleus, PML body {ECO:0000250|UniProtKB:Q9Y4E5}. Nucleus,
CC       nucleoplasm {ECO:0000250|UniProtKB:Q9Y4E5}. Note=Colocalizes with
CC       UBE2I/UBC9, SUMO1 and SUMO2 in nuclear granules; this probably
CC       requires sumoylation. Desumoylation leads to diffuse nucleoplasmic
CC       location. {ECO:0000250|UniProtKB:Q9Y4E5}.
CC   -!- DOMAIN: Binds UBE2I/UBC9 and two SUMO2 molecules via its N-
CC       terminus. The most N-terminal region interacts with the SUMO2
CC       chain that is covalently bound to the UBE2I/UBC9 active site,
CC       while the second region interacts with another SUMO2 that is non-
CC       covalently associated with the same UBE2I/UBC9 chain.
CC       {ECO:0000250|UniProtKB:Q9Y4E5}.
CC   -!- PTM: Sumoylated. Predominantly sumoylated on the N-terminal region
CC       that is important for interaction with SUMO1 and SUMO2.
CC       Sumoylation is important for localization in nuclear granules;
CC       desumoylation leads to diffuse nucleoplasmic location.
CC       Autosumoylated (in vitro). Sumoylation enhances E3 SUMO-protein
CC       ligase activity. {ECO:0000250|UniProtKB:Q9Y4E5}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
DR   EMBL; AK030088; BAC26778.1; -; mRNA.
DR   CCDS; CCDS14865.1; -.
DR   RefSeq; NP_001277628.1; NM_001290699.1.
DR   RefSeq; NP_598578.1; NM_133817.3.
DR   UniGene; Mm.289103; -.
DR   UniGene; Mm.440137; -.
DR   ProteinModelPortal; Q8C0P7; -.
DR   SMR; Q8C0P7; -.
DR   BioGrid; 221052; 1.
DR   STRING; 10090.ENSMUSP00000019861; -.
DR   iPTMnet; Q8C0P7; -.
DR   PhosphoSitePlus; Q8C0P7; -.
DR   EPD; Q8C0P7; -.
DR   MaxQB; Q8C0P7; -.
DR   PaxDb; Q8C0P7; -.
DR   PRIDE; Q8C0P7; -.
DR   Ensembl; ENSMUST00000019861; ENSMUSP00000019861; ENSMUSG00000042197.
DR   GeneID; 98403; -.
DR   KEGG; mmu:98403; -.
DR   UCSC; uc007anz.2; mouse.
DR   CTD; 98403; -.
DR   MGI; MGI:2137896; Zfp451.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00390000011354; -.
DR   HOGENOM; HOG000155796; -.
DR   HOVERGEN; HBG057364; -.
DR   InParanoid; Q8C0P7; -.
DR   OMA; FDSQECV; -.
DR   OrthoDB; 148216at2759; -.
DR   PhylomeDB; Q8C0P7; -.
DR   TreeFam; TF331947; -.
DR   UniPathway; UPA00886; -.
DR   ChiTaRS; Zfp451; mouse.
DR   PRO; PR:Q8C0P7; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000042197; Expressed in 266 organ(s), highest expression level in rostral migratory stream.
DR   ExpressionAtlas; Q8C0P7; baseline and differential.
DR   Genevisible; Q8C0P7; MM.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0061665; F:SUMO ligase activity; ISS:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; ISS:UniProtKB.
DR   GO; GO:0060633; P:negative regulation of transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1056       E3 SUMO-protein ligase ZNF451.
FT                                /FTId=PRO_0000047599.
FT   ZN_FING     169    195       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     212    234       C2H2-type 2; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     253    277       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     315    338       C2H2-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     362    385       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     494    517       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     527    550       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     604    629       C2H2-type 8; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     634    657       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     665    688       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     751    774       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     787    810       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION        1    344       Important for interaction with SUMO1 and
FT                                SUMO2. {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   REGION        1    246       Sufficient for E3 SUMO-protein ligase
FT                                activity. {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   REGION       30     37       Interaction with SUMO2 1.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   REGION       42     50       Interaction with SUMO2 2.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   REGION      168    521       Important for interaction with SMAD4.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   REGION     1045   1056       Important for ubiquitin binding.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   MOTIF        38     41       PLRP. {ECO:0000305}.
FT   MOD_RES     155    155       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   MOD_RES     158    158       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   MOD_RES     429    429       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK     75     75       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK     77     77       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    106    106       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    139    139       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    153    153       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    167    167       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    270    270       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    275    275       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    283    283       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    288    288       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    301    301       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    309    309       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    420    420       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    431    431       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    539    539       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    583    583       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    645    645       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    704    704       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    704    704       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    729    729       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    746    746       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    788    788       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    815    815       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    843    843       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    849    849       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    947    947       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    988    988       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
FT   CROSSLNK    989    989       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4E5}.
SQ   SEQUENCE   1056 AA;  120070 MW;  7D8FBC0B50ECA622 CRC64;
     MGDPGPEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS SDDEEPSTSH
     SDENFKCKDY IDHQKDKVAL TLARLARHVE VEKQQKEEKN RAFREKIDFQ HAHGLQELEF
     IQGHSETEAA RQCVDQWLKM PGLRTNAANS GTKRSFQRGG RMWRSEKPIL CPIMHCNKEF
     DNGHLLLGHL KRFDHSPCDP TITLHGPLAN SFACAVCYEH FVTQQQYKDH LLSRTAAADG
     HSNSLLPQII QCYACPQCFL LFSTKDECLK HMSTKNHFHQ SFKLSDNKGT ARPISFPSFA
     KKRLVSLCKD VPFQVKCVAC HQTLRSHMEL TAHFRVRCQN AGPVAIAEKS ITQVAKEFIV
     RGYCSDCNQV FMDVASTQSH KNSGHKITLA NSVEESVLLY CHISEGSRPP CDLHLFSQPK
     ISSLKRILSV KESSAEDCIV PTKKVNLGVE SLGGATRVQR QSPAVTAWFC ECRRQFPSEE
     AVEKHVFSAN TMCYKCVVCG KVCEDSGVMR LHMSRFHGGA HLNNFLFWCR TCKKELVKKD
     AIMAHITEFH SGHRYFYEMD EVEEEEEEAM PSSSVESHLN TDKPPSPIAV VDHCPANSPP
     RGRWQCRICE DMFESQECVK QHCMSLTSHR FHRYSCAHCR KTFHKVETLY RHCQDEHDSE
     IMMKYFCGLC DLIFNKEEEF LSHYKEHHSI DYVFVSEKTK TSIKTEGDFK IVETSSLLSC
     GCHESYMCKI NRKEDYDRCL PVLLEKGRLW FRCSSCSATA QNVTDINTHV CQVHRKEKSE
     EEQQYVIKCG ICTKAFQNTE SAQQHFHRKH AALQKPTATP GGANRSSTCQ LAASASHAEK
     NLKQPSSQKH SDVEKGAEHD VRCQNIEEEV ELPDVDYLRT MTHIVFVDFD NWSNFFGHLP
     GHLNQGTFIW GFQGGNTNWK PPLSCKVYNY LSRIGCFFLH PRCSKRKDAA DFAICMHAGR
     LDEQLPKQIP FTILSGDQGF LELENQFKKT QRPAHILNPH HLEGDMMCAL LNSISDTTKE
     CDSDDSSGMK GSPAEELRAT EDVELEEAIR RSLEEM
//
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