GenomeNet

Database: UniProt
Entry: O14944
LinkDB: O14944
Original site: O14944 
ID   EREG_HUMAN              Reviewed;         169 AA.
AC   O14944; B2RC66; Q6FH69;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   07-OCT-2020, entry version 184.
DE   RecName: Full=Proepiregulin;
DE   Contains:
DE     RecName: Full=Epiregulin;
DE              Short=EPR;
DE   Flags: Precursor;
GN   Name=EREG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Colon adenocarcinoma;
RX   PubMed=9337852; DOI=10.1042/bj3260069;
RA   Toyoda H., Komurasaki T., Uchida D., Morimoto S.;
RT   "Distribution of mRNA for human epiregulin, a differentially expressed
RT   member of the epidermal growth factor family.";
RL   Biochem. J. 326:69-75(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   FUNCTION AS EGFR LIGAND, AND INTERACTION WITH EGFR AND ERBB4.
RX   PubMed=9419975; DOI=10.1038/sj.onc.1201458;
RA   Komurasaki T., Toyoda H., Uchida D., Morimoto S.;
RT   "Epiregulin binds to epidermal growth factor receptor and ErbB-4 and
RT   induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-
RT   2, ErbB-3 and ErbB-4.";
RL   Oncogene 15:2841-2848(1997).
RN   [7]
RP   STRUCTURE BY NMR OF 63-108, AND DISULFIDE BONDS.
RX   PubMed=14572630; DOI=10.1016/s0014-5793(03)01005-6;
RA   Sato K., Nakamura T., Mizuguchi M., Miura K., Tada M., Aizawa T., Gomi T.,
RA   Miyamoto K., Kawano K.;
RT   "Solution structure of epiregulin and the effect of its C-terminal domain
RT   for receptor binding affinity.";
RL   FEBS Lett. 553:232-238(2003).
RN   [8]
RP   REVIEW.
RX   PubMed=24631357; DOI=10.1016/j.semcdb.2014.03.005;
RA   Riese D.J. II, Cullum R.L.;
RT   "Epiregulin: roles in normal physiology and cancer.";
RL   Semin. Cell Dev. Biol. 28:49-56(2014).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] ALA-42.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR
CC       and ERBB4 tyrosine phosphorylation (PubMed:9419975). Contributes to
CC       inflammation, wound healing, tissue repair, and oocyte maturation by
CC       regulating angiogenesis and vascular remodeling and by stimulating cell
CC       proliferation (PubMed:24631357). {ECO:0000269|PubMed:9419975,
CC       ECO:0000303|PubMed:24631357}.
CC   -!- SUBUNIT: Interacts with EGFR and ERBB4. {ECO:0000269|PubMed:9419975}.
CC   -!- INTERACTION:
CC       O14944; Q07325: CXCL9; NbExp=3; IntAct=EBI-17272224, EBI-3911467;
CC       O14944; P00533: EGFR; NbExp=3; IntAct=EBI-17272224, EBI-297353;
CC       O14944; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-17272224, EBI-12070086;
CC       O14944; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-17272224, EBI-10317425;
CC       O14944; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-17272224, EBI-2804156;
CC   -!- SUBCELLULAR LOCATION: [Epiregulin]: Secreted, extracellular space
CC       {ECO:0000269|PubMed:9337852}.
CC   -!- SUBCELLULAR LOCATION: [Proepiregulin]: Cell membrane
CC       {ECO:0000269|PubMed:9337852}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:9337852}.
CC   -!- TISSUE SPECIFICITY: In normal adults, expressed predominantly in the
CC       placenta and peripheral blood leukocytes. High levels were detected in
CC       carcinomas of the bladder, lung, kidney and colon.
CC       {ECO:0000269|PubMed:9337852}.
DR   EMBL; D30783; BAA22146.1; -; mRNA.
DR   EMBL; AK314959; BAG37463.1; -; mRNA.
DR   EMBL; CR541887; CAG46685.1; -; mRNA.
DR   EMBL; CH471057; EAX05709.1; -; Genomic_DNA.
DR   EMBL; BC136404; AAI36405.1; -; mRNA.
DR   EMBL; BC136405; AAI36406.1; -; mRNA.
DR   CCDS; CCDS3564.1; -.
DR   RefSeq; NP_001423.1; NM_001432.2.
DR   PDB; 1K36; NMR; -; A=63-108.
DR   PDB; 1K37; NMR; -; A=63-108.
DR   PDB; 5E8D; X-ray; 2.50 A; A=38-108.
DR   PDB; 5WB7; X-ray; 2.94 A; E/F/G/H=56-116.
DR   PDBsum; 1K36; -.
DR   PDBsum; 1K37; -.
DR   PDBsum; 5E8D; -.
DR   PDBsum; 5WB7; -.
DR   BMRB; O14944; -.
DR   SMR; O14944; -.
DR   BioGRID; 108381; 9.
DR   IntAct; O14944; 10.
DR   STRING; 9606.ENSP00000244869; -.
DR   GlyGen; O14944; 1 site.
DR   iPTMnet; O14944; -.
DR   PhosphoSitePlus; O14944; -.
DR   BioMuta; EREG; -.
DR   jPOST; O14944; -.
DR   MassIVE; O14944; -.
DR   MaxQB; O14944; -.
DR   PaxDb; O14944; -.
DR   PeptideAtlas; O14944; -.
DR   PRIDE; O14944; -.
DR   ProteomicsDB; 48327; -.
DR   ABCD; O14944; 8 sequenced antibodies.
DR   Antibodypedia; 24625; 280 antibodies.
DR   DNASU; 2069; -.
DR   Ensembl; ENST00000244869; ENSP00000244869; ENSG00000124882.
DR   GeneID; 2069; -.
DR   KEGG; hsa:2069; -.
DR   UCSC; uc003hie.2; human.
DR   CTD; 2069; -.
DR   DisGeNET; 2069; -.
DR   EuPathDB; HostDB:ENSG00000124882.3; -.
DR   GeneCards; EREG; -.
DR   HGNC; HGNC:3443; EREG.
DR   HPA; ENSG00000124882; Tissue enhanced (bone marrow, tongue).
DR   MIM; 602061; gene.
DR   neXtProt; NX_O14944; -.
DR   OpenTargets; ENSG00000124882; -.
DR   PharmGKB; PA27856; -.
DR   eggNOG; ENOG502S5DM; Eukaryota.
DR   GeneTree; ENSGT00510000048748; -.
DR   HOGENOM; CLU_138015_0_0_1; -.
DR   InParanoid; O14944; -.
DR   KO; K09784; -.
DR   OMA; CTALVQM; -.
DR   OrthoDB; 1420179at2759; -.
DR   PhylomeDB; O14944; -.
DR   TreeFam; TF336145; -.
DR   PathwayCommons; O14944; -.
DR   Reactome; R-HSA-1227986; Signaling by ERBB2.
DR   Reactome; R-HSA-1236394; Signaling by ERBB4.
DR   Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling.
DR   Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
DR   Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR   Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-HSA-177929; Signaling by EGFR.
DR   Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR   Reactome; R-HSA-180292; GAB1 signalosome.
DR   Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR   Reactome; R-HSA-182971; EGFR downregulation.
DR   Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
DR   Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
DR   Reactome; R-HSA-212718; EGFR interacts with phospholipase C-gamma.
DR   Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR   Reactome; R-HSA-5638303; Inhibition of Signaling by Overexpressed EGFR.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR   Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR   Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR   Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR   SIGNOR; O14944; -.
DR   BioGRID-ORCS; 2069; 1 hit in 878 CRISPR screens.
DR   ChiTaRS; EREG; human.
DR   EvolutionaryTrace; O14944; -.
DR   GeneWiki; Epiregulin; -.
DR   GenomeRNAi; 2069; -.
DR   Pharos; O14944; Tbio.
DR   PRO; PR:O14944; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; O14944; protein.
DR   Bgee; ENSG00000124882; Expressed in bone marrow and 137 other tissues.
DR   Genevisible; O14944; HS.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; IDA:UniProtKB.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
DR   GO; GO:0007143; P:female meiotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0030216; P:keratinocyte differentiation; TAS:UniProtKB.
DR   GO; GO:0043616; P:keratinocyte proliferation; IDA:UniProtKB.
DR   GO; GO:0042700; P:luteinizing hormone signaling pathway; ISS:UniProtKB.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0061024; P:membrane organization; TAS:Reactome.
DR   GO; GO:0009299; P:mRNA transcription; IDA:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; TAS:UniProtKB.
DR   GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0001556; P:oocyte maturation; ISS:UniProtKB.
DR   GO; GO:0001550; P:ovarian cumulus expansion; ISS:UniProtKB.
DR   GO; GO:0030728; P:ovulation; ISS:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0042108; P:positive regulation of cytokine biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
DR   GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR   GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:0048160; P:primary follicle stage; ISS:UniProtKB.
DR   GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
DR   GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:Reactome.
DR   GO; GO:0042060; P:wound healing; TAS:UniProtKB.
DR   InterPro; IPR000742; EGF-like_dom.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Angiogenesis; Cell membrane; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Growth factor; Membrane; Mitogen; Polymorphism; Reference proteome;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..169
FT                   /note="Proepiregulin"
FT                   /id="PRO_0000302800"
FT   PROPEP          30..62
FT                   /evidence="ECO:0000250|UniProtKB:Q61521,
FT                   ECO:0000250|UniProtKB:Q9Z0L5"
FT                   /id="PRO_0000007556"
FT   CHAIN           63..108
FT                   /note="Epiregulin"
FT                   /id="PRO_0000007557"
FT   PROPEP          109..169
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007558"
FT   TOPO_DOM        60..119
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          64..104
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   COMPBIAS        145..152
FT                   /note="Arg/Lys-rich (basic)"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:14572630"
FT   DISULFID        76..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:14572630"
FT   DISULFID        94..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:14572630"
FT   VARIANT         42
FT                   /note="G -> A (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035833"
FT   VARIANT         147
FT                   /note="R -> Q (in dbSNP:rs35275884)"
FT                   /id="VAR_033827"
FT   STRAND          65..67
FT                   /evidence="ECO:0000244|PDB:5WB7"
FT   HELIX           70..72
FT                   /evidence="ECO:0000244|PDB:5E8D"
FT   TURN            73..75
FT                   /evidence="ECO:0000244|PDB:5E8D"
FT   STRAND          79..84
FT                   /evidence="ECO:0000244|PDB:5E8D"
FT   TURN            85..88
FT                   /evidence="ECO:0000244|PDB:5E8D"
FT   STRAND          89..94
FT                   /evidence="ECO:0000244|PDB:5E8D"
FT   STRAND          98..100
FT                   /evidence="ECO:0000244|PDB:5E8D"
SQ   SEQUENCE   169 AA;  19044 MW;  17F3926ADFB2BDEE CRC64;
     MTAGRRMEML CAGRVPALLL CLGFHLLQAV LSTTVIPSCI PGESSDNCTA LVQTEDNPRV
     AQVSITKCSS DMNGYCLHGQ CIYLVDMSQN YCRCEVGYTG VRCEHFFLTV HQPLSKEYVA
     LTVILIILFL ITVVGSTYYF CRWYRNRKSK EPKKEYERVT SGDPELPQV
//
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