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Laminin-like protein epi-1

 EPI1_CAEEL              Reviewed;        3672 AA.
Q21313;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 124.
RecName: Full=Laminin-like protein epi-1;
Flags: Precursor;
Name=epi-1; ORFNames=K08C7.3;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Bristol N2;
PubMed=12754521; DOI=10.1038/nbt829;
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
Kasai K., Takahashi N., Isobe T.;
"Lectin affinity capture, isotope-coded tagging and mass spectrometry
to identify N-linked glycoproteins.";
Nat. Biotechnol. 21:667-672(2003).
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249; ASN-351; ASN-761;
ASN-1014; ASN-1341; ASN-1756; ASN-2231; ASN-2235; ASN-2401 AND
ASN-2487, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15888633; DOI=10.1093/glycob/cwi075;
Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H.,
Mahuran D.J.;
"Identification of the hydrophobic glycoproteins of Caenorhabditis
elegans.";
Glycobiology 15:952-964(2005).
[4]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-2802.
PubMed=16495308; DOI=10.1242/dev.02300;
Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
"FGF negatively regulates muscle membrane extension in Caenorhabditis
elegans.";
Development 133:1263-1275(2006).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-249; ASN-351;
ASN-477; ASN-634; ASN-761; ASN-1014; ASN-1341; ASN-1705; ASN-1756;
ASN-1944; ASN-2207; ASN-2231; ASN-2235; ASN-2401 AND ASN-2487, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Bristol N2;
PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
Taoka M., Takahashi N., Isobe T.;
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
elegans and suggests an atypical translocation mechanism for integral
membrane proteins.";
Mol. Cell. Proteomics 6:2100-2109(2007).
-!- FUNCTION: During the formation of neuromuscular junctions at the
larval stage, negatively regulates membrane protrusion from body
wall muscles, probably downstream of the integrin complex formed
by pat-2 and pat-3. {ECO:0000269|PubMed:16495308}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in L4 larval stage,
causes ectopic membrane extensions from body wall muscles.
{ECO:0000269|PubMed:16495308}.
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EMBL; Z70286; CAA94293.1; -; Genomic_DNA.
PIR; T23433; T23433.
RefSeq; NP_001023282.1; NM_001028111.3.
UniGene; Cel.18380; -.
ProteinModelPortal; Q21313; -.
SMR; Q21313; -.
BioGrid; 43057; 8.
STRING; 6239.K08C7.3a.1; -.
PaxDb; Q21313; -.
PRIDE; Q21313; -.
EnsemblMetazoa; K08C7.3b.1; K08C7.3b.1; WBGene00001328.
EnsemblMetazoa; K08C7.3b.2; K08C7.3b.2; WBGene00001328.
GeneID; 177956; -.
UCSC; K08C7.3a; c. elegans.
CTD; 177956; -.
WormBase; K08C7.3b; CE06136; WBGene00001328; epi-1.
eggNOG; ENOG410IP6A; Eukaryota.
eggNOG; ENOG410ZVNS; LUCA.
GeneTree; ENSGT00780000121851; -.
HOGENOM; HOG000017472; -.
InParanoid; Q21313; -.
PRO; PR:Q21313; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00001328; -.
ExpressionAtlas; Q21313; baseline.
GO; GO:0005604; C:basement membrane; IDA:WormBase.
GO; GO:0005201; F:extracellular matrix structural constituent; ISS:WormBase.
GO; GO:0007414; P:axonal defasciculation; IMP:WormBase.
GO; GO:0071711; P:basement membrane organization; IMP:WormBase.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0016477; P:cell migration; IMP:WormBase.
GO; GO:0001764; P:neuron migration; IMP:WormBase.
GO; GO:0010950; P:positive regulation of endopeptidase activity; IMP:WormBase.
GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
GO; GO:0042127; P:regulation of cell proliferation; IMP:WormBase.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0009408; P:response to heat; IMP:WormBase.
GO; GO:0051788; P:response to misfolded protein; IMP:WormBase.
Gene3D; 2.60.120.260; -; 4.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR010307; Laminin_domII.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR001791; Laminin_G.
InterPro; IPR000034; Laminin_IV.
InterPro; IPR008211; Laminin_N.
Pfam; PF00052; Laminin_B; 1.
Pfam; PF00053; Laminin_EGF; 21.
Pfam; PF00054; Laminin_G_1; 1.
Pfam; PF02210; Laminin_G_2; 3.
Pfam; PF06009; Laminin_II; 1.
Pfam; PF00055; Laminin_N; 1.
SMART; SM00181; EGF; 14.
SMART; SM00180; EGF_Lam; 21.
SMART; SM00281; LamB; 1.
SMART; SM00282; LamG; 5.
SMART; SM00136; LamNT; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF49899; SSF49899; 6.
PROSITE; PS00022; EGF_1; 19.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS01248; EGF_LAM_1; 21.
PROSITE; PS50027; EGF_LAM_2; 21.
PROSITE; PS50025; LAM_G_DOMAIN; 5.
PROSITE; PS51115; LAMININ_IVA; 1.
PROSITE; PS51117; LAMININ_NTER; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein;
Laminin EGF-like domain; Reference proteome; Repeat; Signal.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 3672 Laminin-like protein epi-1.
/FTId=PRO_0000017100.
DOMAIN 28 297 Laminin N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00466}.
DOMAIN 298 356 Laminin EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 357 426 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 427 471 Laminin EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 472 518 Laminin EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 519 563 Laminin EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 564 609 Laminin EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 610 655 Laminin EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 656 700 Laminin EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 701 755 Laminin EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 756 808 Laminin EGF-like 10.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 809 839 Laminin EGF-like 11; truncated.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1415 1460 Laminin EGF-like 12.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1461 1505 Laminin EGF-like 13.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1506 1553 Laminin EGF-like 14.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1554 1604 Laminin EGF-like 15.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1605 1614 Laminin EGF-like 16; first part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1615 1796 Laminin IV type A. {ECO:0000255|PROSITE-
ProRule:PRU00458}.
DOMAIN 1797 1829 Laminin EGF-like 16; second part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1830 1879 Laminin EGF-like 17.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1880 1936 Laminin EGF-like 18.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1937 1989 Laminin EGF-like 19.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1990 2036 Laminin EGF-like 20.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 2037 2083 Laminin EGF-like 21.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 2084 2131 Laminin EGF-like 22.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 2693 2884 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 2896 3066 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 3072 3235 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 3310 3482 Laminin G-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 3488 3669 Laminin G-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754521,
ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 511 511 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 530 530 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 634 634 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 761 761 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 1014 1014 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 1341 1341 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 1705 1705 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 1756 1756 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 1868 1868 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1944 1944 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 1986 1986 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2002 2002 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2159 2159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2207 2207 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 2231 2231 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 2235 2235 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 2401 2401 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 2421 2421 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2487 2487 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15888633,
ECO:0000269|PubMed:17761667}.
CARBOHYD 2821 2821 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3087 3087 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3242 3242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3541 3541 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 298 307 {ECO:0000250}.
DISULFID 300 320 {ECO:0000250}.
DISULFID 322 331 {ECO:0000250}.
DISULFID 334 354 {ECO:0000250}.
DISULFID 357 366 {ECO:0000250}.
DISULFID 359 391 {ECO:0000250}.
DISULFID 394 403 {ECO:0000250}.
DISULFID 406 424 {ECO:0000250}.
DISULFID 427 438 {ECO:0000250}.
DISULFID 429 445 {ECO:0000250}.
DISULFID 447 456 {ECO:0000250}.
DISULFID 459 469 {ECO:0000250}.
DISULFID 472 484 {ECO:0000250}.
DISULFID 474 491 {ECO:0000250}.
DISULFID 493 502 {ECO:0000250}.
DISULFID 505 516 {ECO:0000250}.
DISULFID 519 531 {ECO:0000250}.
DISULFID 521 538 {ECO:0000250}.
DISULFID 540 549 {ECO:0000250}.
DISULFID 552 561 {ECO:0000250}.
DISULFID 564 576 {ECO:0000250}.
DISULFID 566 583 {ECO:0000250}.
DISULFID 585 594 {ECO:0000250}.
DISULFID 597 607 {ECO:0000250}.
DISULFID 610 622 {ECO:0000250}.
DISULFID 612 629 {ECO:0000250}.
DISULFID 631 640 {ECO:0000250}.
DISULFID 643 653 {ECO:0000250}.
DISULFID 656 668 {ECO:0000250}.
DISULFID 658 674 {ECO:0000250}.
DISULFID 676 685 {ECO:0000250}.
DISULFID 688 698 {ECO:0000250}.
DISULFID 701 715 {ECO:0000250}.
DISULFID 703 724 {ECO:0000250}.
DISULFID 726 735 {ECO:0000250}.
DISULFID 738 753 {ECO:0000250}.
DISULFID 756 770 {ECO:0000250}.
DISULFID 758 777 {ECO:0000250}.
DISULFID 779 788 {ECO:0000250}.
DISULFID 791 806 {ECO:0000250}.
DISULFID 809 821 {ECO:0000250}.
DISULFID 811 828 {ECO:0000250}.
DISULFID 830 839 {ECO:0000250}.
DISULFID 1415 1427 {ECO:0000250}.
DISULFID 1417 1434 {ECO:0000250}.
DISULFID 1436 1445 {ECO:0000250}.
DISULFID 1448 1458 {ECO:0000250}.
DISULFID 1461 1469 {ECO:0000250}.
DISULFID 1463 1476 {ECO:0000250}.
DISULFID 1478 1487 {ECO:0000250}.
DISULFID 1490 1503 {ECO:0000250}.
DISULFID 1506 1520 {ECO:0000250}.
DISULFID 1508 1527 {ECO:0000250}.
DISULFID 1529 1538 {ECO:0000250}.
DISULFID 1541 1551 {ECO:0000250}.
DISULFID 1554 1566 {ECO:0000250}.
DISULFID 1556 1573 {ECO:0000250}.
DISULFID 1575 1584 {ECO:0000250}.
DISULFID 1587 1602 {ECO:0000250}.
DISULFID 1830 1839 {ECO:0000250}.
DISULFID 1832 1846 {ECO:0000250}.
DISULFID 1849 1858 {ECO:0000250}.
DISULFID 1861 1877 {ECO:0000250}.
DISULFID 1880 1894 {ECO:0000250}.
DISULFID 1882 1905 {ECO:0000250}.
DISULFID 1907 1916 {ECO:0000250}.
DISULFID 1919 1934 {ECO:0000250}.
DISULFID 1937 1951 {ECO:0000250}.
DISULFID 1939 1958 {ECO:0000250}.
DISULFID 1961 1970 {ECO:0000250}.
DISULFID 1973 1987 {ECO:0000250}.
DISULFID 1990 2000 {ECO:0000250}.
DISULFID 1992 2007 {ECO:0000250}.
DISULFID 2009 2018 {ECO:0000250}.
DISULFID 2021 2034 {ECO:0000250}.
DISULFID 2037 2048 {ECO:0000250}.
DISULFID 2039 2055 {ECO:0000250}.
DISULFID 2057 2066 {ECO:0000250}.
DISULFID 2069 2081 {ECO:0000250}.
DISULFID 2084 2096 {ECO:0000250}.
DISULFID 2086 2103 {ECO:0000250}.
DISULFID 2105 2114 {ECO:0000250}.
DISULFID 2117 2129 {ECO:0000250}.
DISULFID 3040 3066 {ECO:0000250}.
DISULFID 3209 3235 {ECO:0000250}.
DISULFID 3460 3482 {ECO:0000250}.
DISULFID 3633 3669 {ECO:0000250}.
MUTAGEN 2802 2802 L->F: In rh152; causes ectopic muscle
membrane extensions.
{ECO:0000269|PubMed:16495308}.
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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