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Database: UniProt
Entry: EPI1_CAEEL
LinkDB: EPI1_CAEEL
Original site: EPI1_CAEEL 
ID   EPI1_CAEEL              Reviewed;        3672 AA.
AC   Q21313;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   01-OCT-2014, entry version 102.
DE   RecName: Full=Laminin-like protein epi-1;
DE   Flags: Precursor;
GN   Name=epi-1; ORFNames=K08C7.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND IDENTIFICATION BY
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry
RT   to identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249; ASN-351; ASN-761;
RP   ASN-1014; ASN-1341; ASN-1756; ASN-2231; ASN-2235; ASN-2401 AND
RP   ASN-2487, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA   Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H.,
RA   Mahuran D.J.;
RT   "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT   elegans.";
RL   Glycobiology 15:952-964(2005).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-249; ASN-351;
RP   ASN-477; ASN-634; ASN-761; ASN-1014; ASN-1341; ASN-1705; ASN-1756;
RP   ASN-1944; ASN-2207; ASN-2231; ASN-2235; ASN-2401 AND ASN-2487, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- SIMILARITY: Contains 22 laminin EGF-like domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00460}.
CC   -!- SIMILARITY: Contains 5 laminin G-like domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00122}.
CC   -!- SIMILARITY: Contains 1 laminin IV type A domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00458}.
CC   -!- SIMILARITY: Contains 1 laminin N-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00466}.
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DR   EMBL; Z70286; CAA94293.1; -; Genomic_DNA.
DR   PIR; T23433; T23433.
DR   RefSeq; NP_001023282.1; NM_001028111.3.
DR   UniGene; Cel.18380; -.
DR   ProteinModelPortal; Q21313; -.
DR   SMR; Q21313; 112-841, 1431-1585, 1796-2116, 2718-3671.
DR   BioGrid; 43057; 8.
DR   PaxDb; Q21313; -.
DR   PRIDE; Q21313; -.
DR   EnsemblMetazoa; K08C7.3b.1; K08C7.3b.1; WBGene00001328.
DR   EnsemblMetazoa; K08C7.3b.2; K08C7.3b.2; WBGene00001328.
DR   GeneID; 177956; -.
DR   KEGG; cel:CELE_K08C7.3; -.
DR   UCSC; K08C7.3a; c. elegans.
DR   CTD; 177956; -.
DR   WormBase; K08C7.3b; CE06136; WBGene00001328; epi-1.
DR   eggNOG; NOG292643; -.
DR   GeneTree; ENSGT00750000117374; -.
DR   HOGENOM; HOG000017472; -.
DR   NextBio; 899114; -.
DR   PRO; PR:Q21313; -.
DR   GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR   GO; GO:0007414; P:axonal defasciculation; IMP:WormBase.
DR   GO; GO:0071711; P:basement membrane organization; IMP:WormBase.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0016477; P:cell migration; IMP:WormBase.
DR   GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR   GO; GO:0010950; P:positive regulation of endopeptidase activity; IMP:WormBase.
DR   GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR   GO; GO:0042127; P:regulation of cell proliferation; IMP:WormBase.
DR   GO; GO:0000003; P:reproduction; IMP:WormBase.
DR   GO; GO:0009408; P:response to heat; IMP:WormBase.
DR   GO; GO:0051788; P:response to misfolded protein; IMP:WormBase.
DR   Gene3D; 2.60.120.200; -; 5.
DR   InterPro; IPR008985; ConA-like_lec_gl_sf.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR018031; Laminin_B_subgr.
DR   InterPro; IPR000034; Laminin_B_type_IV.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR010307; Laminin_II.
DR   InterPro; IPR008211; Laminin_N.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 21.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00180; EGF_Lam; 21.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 6.
DR   PROSITE; PS00022; EGF_1; 19.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 21.
DR   PROSITE; PS50027; EGF_LAM_2; 21.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Signal.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   3672       Laminin-like protein epi-1.
FT                                /FTId=PRO_0000017100.
FT   DOMAIN       28    297       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      298    356       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      357    426       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      427    471       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      472    518       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      519    563       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      564    609       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      610    655       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      656    700       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      701    755       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      756    808       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      809    839       Laminin EGF-like 11; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1415   1460       Laminin EGF-like 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1461   1505       Laminin EGF-like 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1506   1553       Laminin EGF-like 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1554   1604       Laminin EGF-like 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1605   1614       Laminin EGF-like 16; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1615   1796       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN     1797   1829       Laminin EGF-like 16; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1830   1879       Laminin EGF-like 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1880   1936       Laminin EGF-like 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1937   1989       Laminin EGF-like 19.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1990   2036       Laminin EGF-like 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     2037   2083       Laminin EGF-like 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     2084   2131       Laminin EGF-like 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     2693   2884       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2896   3066       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3072   3235       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3310   3482       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3488   3669       Laminin G-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    140    140       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    249    249       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:12754521,
FT                                ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    351    351       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    477    477       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    511    511       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    530    530       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    634    634       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    761    761       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   1014   1014       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   1341   1341       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   1705   1705       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   1756   1756       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   1868   1868       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1944   1944       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   1986   1986       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   2002   2002       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   2159   2159       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   2207   2207       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   2231   2231       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   2235   2235       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   2401   2401       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   2421   2421       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   2487   2487       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   2821   2821       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   3087   3087       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   3242   3242       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   3541   3541       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    298    307       {ECO:0000250}.
FT   DISULFID    300    320       {ECO:0000250}.
FT   DISULFID    322    331       {ECO:0000250}.
FT   DISULFID    334    354       {ECO:0000250}.
FT   DISULFID    357    366       {ECO:0000250}.
FT   DISULFID    359    391       {ECO:0000250}.
FT   DISULFID    394    403       {ECO:0000250}.
FT   DISULFID    406    424       {ECO:0000250}.
FT   DISULFID    427    438       {ECO:0000250}.
FT   DISULFID    429    445       {ECO:0000250}.
FT   DISULFID    447    456       {ECO:0000250}.
FT   DISULFID    459    469       {ECO:0000250}.
FT   DISULFID    472    484       {ECO:0000250}.
FT   DISULFID    474    491       {ECO:0000250}.
FT   DISULFID    493    502       {ECO:0000250}.
FT   DISULFID    505    516       {ECO:0000250}.
FT   DISULFID    519    531       {ECO:0000250}.
FT   DISULFID    521    538       {ECO:0000250}.
FT   DISULFID    540    549       {ECO:0000250}.
FT   DISULFID    552    561       {ECO:0000250}.
FT   DISULFID    564    576       {ECO:0000250}.
FT   DISULFID    566    583       {ECO:0000250}.
FT   DISULFID    585    594       {ECO:0000250}.
FT   DISULFID    597    607       {ECO:0000250}.
FT   DISULFID    610    622       {ECO:0000250}.
FT   DISULFID    612    629       {ECO:0000250}.
FT   DISULFID    631    640       {ECO:0000250}.
FT   DISULFID    643    653       {ECO:0000250}.
FT   DISULFID    656    668       {ECO:0000250}.
FT   DISULFID    658    674       {ECO:0000250}.
FT   DISULFID    676    685       {ECO:0000250}.
FT   DISULFID    688    698       {ECO:0000250}.
FT   DISULFID    701    715       {ECO:0000250}.
FT   DISULFID    703    724       {ECO:0000250}.
FT   DISULFID    726    735       {ECO:0000250}.
FT   DISULFID    738    753       {ECO:0000250}.
FT   DISULFID    756    770       {ECO:0000250}.
FT   DISULFID    758    777       {ECO:0000250}.
FT   DISULFID    779    788       {ECO:0000250}.
FT   DISULFID    791    806       {ECO:0000250}.
FT   DISULFID    809    821       {ECO:0000250}.
FT   DISULFID    811    828       {ECO:0000250}.
FT   DISULFID    830    839       {ECO:0000250}.
FT   DISULFID   1415   1427       {ECO:0000250}.
FT   DISULFID   1417   1434       {ECO:0000250}.
FT   DISULFID   1436   1445       {ECO:0000250}.
FT   DISULFID   1448   1458       {ECO:0000250}.
FT   DISULFID   1461   1469       {ECO:0000250}.
FT   DISULFID   1463   1476       {ECO:0000250}.
FT   DISULFID   1478   1487       {ECO:0000250}.
FT   DISULFID   1490   1503       {ECO:0000250}.
FT   DISULFID   1506   1520       {ECO:0000250}.
FT   DISULFID   1508   1527       {ECO:0000250}.
FT   DISULFID   1529   1538       {ECO:0000250}.
FT   DISULFID   1541   1551       {ECO:0000250}.
FT   DISULFID   1554   1566       {ECO:0000250}.
FT   DISULFID   1556   1573       {ECO:0000250}.
FT   DISULFID   1575   1584       {ECO:0000250}.
FT   DISULFID   1587   1602       {ECO:0000250}.
FT   DISULFID   1830   1839       {ECO:0000250}.
FT   DISULFID   1832   1846       {ECO:0000250}.
FT   DISULFID   1849   1858       {ECO:0000250}.
FT   DISULFID   1861   1877       {ECO:0000250}.
FT   DISULFID   1880   1894       {ECO:0000250}.
FT   DISULFID   1882   1905       {ECO:0000250}.
FT   DISULFID   1907   1916       {ECO:0000250}.
FT   DISULFID   1919   1934       {ECO:0000250}.
FT   DISULFID   1937   1951       {ECO:0000250}.
FT   DISULFID   1939   1958       {ECO:0000250}.
FT   DISULFID   1961   1970       {ECO:0000250}.
FT   DISULFID   1973   1987       {ECO:0000250}.
FT   DISULFID   1990   2000       {ECO:0000250}.
FT   DISULFID   1992   2007       {ECO:0000250}.
FT   DISULFID   2009   2018       {ECO:0000250}.
FT   DISULFID   2021   2034       {ECO:0000250}.
FT   DISULFID   2037   2048       {ECO:0000250}.
FT   DISULFID   2039   2055       {ECO:0000250}.
FT   DISULFID   2057   2066       {ECO:0000250}.
FT   DISULFID   2069   2081       {ECO:0000250}.
FT   DISULFID   2084   2096       {ECO:0000250}.
FT   DISULFID   2086   2103       {ECO:0000250}.
FT   DISULFID   2105   2114       {ECO:0000250}.
FT   DISULFID   2117   2129       {ECO:0000250}.
FT   DISULFID   3040   3066       {ECO:0000250}.
FT   DISULFID   3209   3235       {ECO:0000250}.
FT   DISULFID   3460   3482       {ECO:0000250}.
FT   DISULFID   3633   3669       {ECO:0000250}.
SQ   SEQUENCE   3672 AA;  404230 MW;  28E262DB5FF14BFA CRC64;
     MSPYDSSPWA TKALFLIVTL LAQFTYSQVL TPSQITISHR KPITATSTCG EIQGQPVTEI
     YCSLTGSTQY TPLNSYSYQD DEQQKSWSQY ENPMVRGGHG CGHCNAGNEN SHPAANMVDG
     NNSWWMSPPL SRGLQHNEVN ITIDLEQEFH VAYVWIQMAN SPRPGSWVLE RSTDHGKTYQ
     PWFNFAENAA ECMRRFGMES LSPISEDDSV TCRTDMASLQ PLENAEMVIR ILEHRPSSRQ
     FATSEALQNF TRATNVRLRL LGTRTLQGHL MDMNEWRDPT VTRRYFYAIK EIMIGGRCVC
     NGHAVTCDIL EPQRPKSLLC RCEHNTCGDM CERCCPGFVQ KQWQAATAHN NFTCEACNCF
     GRSNECEYDA EVDLNKQSID SQGNYEGGGV CKNCRENTEG VNCNKCSFGY FRPEGVTWNE
     PQPCKVCDCD PDKHTGACAE ETGKCECLPR FVGEDCDQCA SGYYDAPKCK PCECNVNGTI
     GDVCLPEDGQ CPCKAGFGGT FCETCADGYT NVTAGCVECV CDATGSEHGN CSASTGQCEC
     KPAYAGLSCD KCQVGYFGDD CKFCNCDPMG TEGGVCDQTT GQCLCKEGFA GDKCDRCDIA
     FYGYPNCKAC ACDGAGITSP ECDATSGQCP CNGNFTGRTC DKCAAGFYNY PDCRGCECLL
     SGAKGQTCDS NGQCYCKGNF EGERCDRCKP NFYNFPICEE CNCNPSGVTR DFQGCDKVSP
     GELCSCRKHV TGRICDQCKP TFWDLQYHHE DGCRSCDCNV NGTISGLNTC DLKTGQCMCK
     KNADGRRCDQ CADGFYRLNS YNQMGCESCH CDIGGALRAE CDITSGQCKC RPRVTGLRCD
     QPIENHYFPT LWHNQYEAED AHTEDQKPVR FAVDPEQFAD FSWRGYAVFS PIQDKILIDV
     DITKATVYRL LFRYRNPTSV PVTATVTINP RFTHTHDVEQ TGKATFAPGD LPAMKEITVD
     GKPFVLNPGK WSLAISTKQR LFLDYVVVLP AEYYEGTVLR QRAPQPCLSH STKNTTCVDL
     IYPPIPSVSR QFVDMDKVPF NYINEDGTTT ALEHVPVEIL LSEITGPAAF VRADENPRVV
     EAKLDVPETG EYVIVLEYHN REETDGNIGV GISQNDKEVL NGNAVIHHCP YATFCRELVS
     SEGTIPYIPL EKGEATVRLN IKPNHEFGLA GVQLIKKSDF SSEYLQQVPV CIKKDARCVQ
     QSYPPAADSV TTEAESGSNM DKSILGDKLP FPVSNSKEMR VVPLDDAQAT VEISGVVPTR
     GHYMFMVHYF NPDNTPINID VLIQNEHYFQ GDSCNSFACS SVPLAFCPSI SGCRALIRDK
     ERPEVIQFYM DDKYTATFYH NSSQKGPIYI DSITAVPYNS YKDKLMEPLA LDLSNEFLKE
     CSEDNLKNHP ESVSDFCKQK IFSLTTDFNA AALSCDCVAQ GSESFQCEQY GGQCKCKPGV
     IGRRCERCAP GYYNFPECIK CQCNAGQQCD ERTGQCFCPP HVEGQTCDRC VSNAFGYDPL
     IGCQKCGCHP QGSEGGNLVC DPESGQCLCR ESMGGRQCDR CLAGFYGFPH CYGCSCNRAG
     TTEEICDATN AQCKCKENVY GGRCEACKAG TFDLSAENPL GCVNCFCFGV TDSCRSSMYP
     VTIMSVDMSS FLTTDDNGMV DNKDDTVIYT SEETSPNSVY FNVPIEKKDY TTSYGLKLTF
     KLSTVPRGGR KSMNADADVR LTGANMTIEY WASEQPTNPE EQFTVKCKLV PENFLTAEGK
     TVTREELMKV LHSLQNITLK ASYFDHPKTS TLYEFGLEIS EPNGVDSVIK ASSVEQCQCP
     APYTGPSCQL CASGYHRVQS GSFLGACVPC ECNGHSATCD PDTGICTDCE HNTNGDHCEF
     CNEGHYGNAT NGSPYDCMAC ACPFAPTNNF AKSCDVSEEG QLLQCNCKPG YTGDRCDRCA
     SGFFGHPQIS GESCSPCQCN GNNNLTDSRS CHPNSGDCYL CEQNTDGRHC ESCAAWFYGD
     AVTAKNCSSC ECSQCGSQYC DNKSGGCECK INVEGDSCDR CKPDHWGFSK CQGCQGCHCG
     TAAFNTQCNV ENGQCTCRPG ATGMRCEHCE HGYWNYGEHG CDKCDCEADL SMGTVCDVRT
     GQCHCQEGAT GSRCDQCLPS YLRIPTYGCR RCDECVHHLI GDVDNLELEI DVLGTAIANI
     SSATIVGARL ARNKKEFNDI NEITKMLNDE ENSFGNVFGD AQDILTNSTQ IQNKLVRTKT
     HSQNSVSSAK NITLNGTEFL QEVMKRAQRA RQSVRSLAEI ALAIGSSSKA VNVDPRLLKE
     AEETLMTLEA ASADQYPEKA QTVPGKLEEI QKKIQEETEK LDKQKETFEA QKKRAEELAA
     YLNSAQQLLK ESKSKADKSN NIAKMLQLTK VENLVAAITD DLERVEAAKG EFQKLNVAIG
     NITENLKDKR EEMTHAVTTL NETRNDVAEA LEAAKKRVRR DEKSVDMQLV NAKAHELHLQ
     ATTLRQTFDN NKDNTDQAVE AANAFSNLTD TLKNAKAQID NAYEALSAEP AFAESVQNAR
     DKPFPDETKE KIDALSKTVS QDLKETEKLK KQLEQLTELS EKLRKRKEAV KAGIPKYSKN
     TLDSIDEKVQ EVEKLKAEID ANIEETRAKI SEIAGKAEEI TEKANSAMEG IRLARRNSVQ
     LNKLAPVIVS KFEELKKLSS ARSAKVDSVS DKVSQIKEMI AVARDAANRI KLGAHFEKGS
     SLDLNIPQRV TRSAAHADIS FYFRTEQEHG IPLFFGNEET AVGSRAVPTA DYVAAEIEYG
     RPKITVDLGD APAVVKLDTP VNDGLWRRLN IERIGKTVSV TLSKPNSVET AETKSSVAGG
     NKSVLNLNQQ ISRLFVGGVP TSARISKDLY NRDFVGDIES LKLHGEPIGL WNSREKGNTN
     VNGAQKKPKI TDNADELVVS LDGEGYTSYK PSHWNPRKAT KISLSFLTFS PHGLLFFVGK
     DKDFMALELS DGGVKLSVDL GSGVGQWITE SSNYNDGKWH TVSIVREEKH VKIMIDGETE
     VLEGDVPGKD SEMSVTEFLY IGGTPSGLSV RTTIVPLRGC IKSVKLGSDN VDLESSHASK
     GVRSGCPLHS VRTVSFLSDR TTASFNNATE FSEDVSVTFK FKTRSIRQPS SLFTVNDDED
     SVLSVSINED GILTVTSGED IATLELAASP DEKWHYVSIR KTKYIIRIDA DDSFSNEVAR
     KHADDSNPDA SFLSAFFGKS GETPSFVGCI GDVTLNGKLL DFANSEIKEI SLNGCSLSDD
     ENISTTTTAA PKPTDDSDVA VLPIDEEEES TTTTTTTTTE EPTEEPAEAR PDGHCSLPED
     PMVQFEDAEG FNFGSQQYSR IEYDILPEAI DKSGEFTFKI RPTSDNGIIF IATNKRTDHI
     AVMLEHGRVV FTYDTGSGQV IIKSDKSIID GRWHTIKVSR RGKSAHLIVD DNSYESEGAA
     NQNEDLIETQ PPFYVGGVPA DLAGFARNLV VGVRSQFSGC IKDFKLNGKS LDNGKEFGTE
     QCSQFSEPGM YFGKDGGYAI VQKDYEVGLT FGLEVEMRPR MKNGILFSVG VLEYITVEFV
     NGSIKTTVES GSGGEELWHH PDIENQYCDG QWQSFKISKK RNLLTVAVNG KAHLKILKKA
     KTDVLTKDPL YFGGLPEGVT NKGIKTNKPF VGCIRFVSFG LKKDRKIRRK KQVDTERFDV
     FGDVHRNACP AI
//
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