GenomeNet

Database: UniProt
Entry: DENR_HUMAN
LinkDB: DENR_HUMAN
Original site: DENR_HUMAN 
ID   DENR_HUMAN              Reviewed;         198 AA.
AC   O43583; Q9H3U6; Q9UKZ0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   25-OCT-2017, entry version 135.
DE   RecName: Full=Density-regulated protein;
DE            Short=DRP;
DE   AltName: Full=Protein DRP1;
DE   AltName: Full=Smooth muscle cell-associated protein 3;
DE            Short=SMAP-3;
GN   Name=DENR; Synonyms=DRP1; ORFNames=H14;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9628587; DOI=10.1089/dna.1998.17.437;
RA   Deyo J.E., Chiao P.J., Tainsky M.A.;
RT   "Drp, a novel protein expressed at high cell density but not during
RT   growth arrest.";
RL   DNA Cell Biol. 17:437-447(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.;
RT   "Molecular cloning and characterization of human smooth muscle cell
RT   associated protein-3 (SMAP-3).";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-198, AND INDUCTION BY ERBB2.
RX   PubMed=10497265; DOI=10.1093/nar/27.20.4008;
RA   Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
RT   "Identification of differentially expressed genes associated with HER-
RT   2/neu overexpression in human breast cancer cells.";
RL   Nucleic Acids Res. 27:4008-4017(1999).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH MCTS1.
RX   PubMed=16982740; DOI=10.1158/0008-5472.CAN-06-1999;
RA   Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M.,
RA   Bachman K.E., He H., Gartenhaus R.B.;
RT   "MCT-1 protein interacts with the cap complex and modulates messenger
RT   RNA translational profiles.";
RL   Cancer Res. 66:8994-9001(2006).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   FUNCTION, AND INDUCTION BY HNRNPD.
RX   PubMed=17878526;
RA   Mazan-Mamczarz K., Gartenhaus R.B.;
RT   "Post-transcriptional control of the MCT-1-associated protein DENR/DRP
RT   by RNA-binding protein AUF1.";
RL   Cancer Genomics Proteomics 4:233-239(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   FUNCTION.
RX   PubMed=20713520; DOI=10.1101/gad.1957510;
RA   Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U.,
RA   Pestova T.V.;
RT   "Activities of ligatin and MCT-1/DENR in eukaryotic translation
RT   initiation and ribosomal recycling.";
RL   Genes Dev. 24:1787-1801(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-73 AND THR-86,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: May be involved in the translation of target mRNAs by
CC       scanning and recognition of the initiation codon. Involved in
CC       translation initiation; promotes recruitmnet of aminoacetyled
CC       initiator tRNA to P site of 40S ribosomes. Can promote release of
CC       deacylated tRNA and mRNA from recycled 40S subunits following
CC       ABCE1-mediated dissociation of post-termination ribosomal
CC       complexes into subunits. Plays a role in the modulation of the
CC       translational profile of a subset of cancer-related mRNAs when
CC       recruited to the translational initiation complex by the oncogene
CC       MCTS1. {ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:17878526,
CC       ECO:0000269|PubMed:20713520}.
CC   -!- SUBUNIT: Interacts with MCTS1. {ECO:0000269|PubMed:16982740}.
CC   -!- INTERACTION:
CC       Q9NX47:MARCH5; NbExp=2; IntAct=EBI-716083, EBI-2341610;
CC       Q9ULC4:MCTS1; NbExp=4; IntAct=EBI-716083, EBI-716076;
CC       Q8WX92:NELFB; NbExp=2; IntAct=EBI-716083, EBI-347721;
CC       P0CG48:UBC; NbExp=3; IntAct=EBI-716083, EBI-3390054;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle
CC       and moderately expressed in the brain, placenta, liver and
CC       pancreas. Weakly expressed in the lung and kidney.
CC       {ECO:0000269|PubMed:9628587}.
CC   -!- INDUCTION: Up-regulated with increasing cell-density by HNRNPD.
CC       Up-regulated in ovarian and breast cancer cells by ERBB2
CC       overexpression. Not induced by TGFB1.
CC       {ECO:0000269|PubMed:10497265, ECO:0000269|PubMed:17878526,
CC       ECO:0000269|PubMed:9628587}.
CC   -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC02985.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/DENRID40295ch12q24.html";
DR   EMBL; AF038554; AAC02985.2; ALT_INIT; mRNA.
DR   EMBL; AB014731; BAB20268.1; -; mRNA.
DR   EMBL; AC026331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007860; AAH07860.1; -; mRNA.
DR   EMBL; AF103800; AAF02420.1; -; mRNA.
DR   CCDS; CCDS45003.1; -.
DR   RefSeq; NP_003668.2; NM_003677.4.
DR   UniGene; Hs.22393; -.
DR   PDB; 5VYC; X-ray; 6.00 A; l1/l2/l3/l4/l5/l6=1-198.
DR   PDBsum; 5VYC; -.
DR   ProteinModelPortal; O43583; -.
DR   SMR; O43583; -.
DR   BioGrid; 114131; 47.
DR   IntAct; O43583; 6.
DR   MINT; MINT-1405155; -.
DR   STRING; 9606.ENSP00000280557; -.
DR   iPTMnet; O43583; -.
DR   PhosphoSitePlus; O43583; -.
DR   BioMuta; DENR; -.
DR   EPD; O43583; -.
DR   MaxQB; O43583; -.
DR   PaxDb; O43583; -.
DR   PeptideAtlas; O43583; -.
DR   PRIDE; O43583; -.
DR   TopDownProteomics; O43583; -.
DR   DNASU; 8562; -.
DR   Ensembl; ENST00000280557; ENSP00000280557; ENSG00000139726.
DR   GeneID; 8562; -.
DR   KEGG; hsa:8562; -.
DR   UCSC; uc001uda.4; human.
DR   CTD; 8562; -.
DR   DisGeNET; 8562; -.
DR   EuPathDB; HostDB:ENSG00000139726.10; -.
DR   GeneCards; DENR; -.
DR   HGNC; HGNC:2769; DENR.
DR   HPA; HPA021783; -.
DR   MIM; 604550; gene.
DR   neXtProt; NX_O43583; -.
DR   OpenTargets; ENSG00000139726; -.
DR   PharmGKB; PA27252; -.
DR   eggNOG; KOG3239; Eukaryota.
DR   eggNOG; COG0023; LUCA.
DR   GeneTree; ENSGT00390000014349; -.
DR   HOGENOM; HOG000237611; -.
DR   HOVERGEN; HBG005471; -.
DR   InParanoid; O43583; -.
DR   OMA; SGGHDCK; -.
DR   OrthoDB; EOG091G0R9X; -.
DR   PhylomeDB; O43583; -.
DR   TreeFam; TF105912; -.
DR   ChiTaRS; DENR; human.
DR   GenomeRNAi; 8562; -.
DR   PRO; PR:O43583; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000139726; -.
DR   CleanEx; HS_DENR; -.
DR   ExpressionAtlas; O43583; baseline and differential.
DR   Genevisible; O43583; HS.
DR   GO; GO:0070992; C:translation initiation complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IDA:UniProtKB.
DR   GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR   GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB.
DR   GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR   Gene3D; 3.30.780.10; -; 1.
DR   InterPro; IPR005873; Drp1.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR005872; SUI1_arc_bac.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   PANTHER; PTHR12789; PTHR12789; 1.
DR   Pfam; PF01253; SUI1; 1.
DR   SUPFAM; SSF55159; SSF55159; 2.
DR   TIGRFAMs; TIGR01159; DRP1; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Initiation factor;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:22223895,
FT                                ECO:0000244|PubMed:22814378}.
FT   CHAIN         2    198       Density-regulated protein.
FT                                /FTId=PRO_0000130600.
FT   DOMAIN      115    182       SUI1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00200}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:22223895,
FT                                ECO:0000244|PubMed:22814378}.
FT   MOD_RES      20     20       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      73     73       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES      86     86       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     189    189       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9CQJ6}.
FT   CONFLICT     49     50       DV -> HE (in Ref. 5; AAF02420).
FT                                {ECO:0000305}.
SQ   SEQUENCE   198 AA;  22092 MW;  023F70E0C6C0B25D CRC64;
     MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
     FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
     PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
     KWPEVDDDSI EDLGEVKK
//
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