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 03-AUG-2022, entry version 150.
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 Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND IDENTIFICATION BY MASS
RP 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 to
RT 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 ASN-2487,
RP 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., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-2802.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-249; ASN-351; ASN-477;
RP ASN-634; ASN-761; ASN-1014; ASN-1341; ASN-1705; ASN-1756; ASN-1944;
RP ASN-2207; ASN-2231; ASN-2235; ASN-2401 AND ASN-2487, AND IDENTIFICATION BY
RP 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 -!- FUNCTION: During the formation of neuromuscular junctions at the larval
CC stage, negatively regulates membrane protrusion from body wall muscles,
CC probably downstream of the integrin complex formed by pat-2 and pat-3.
CC {ECO:0000269|PubMed:16495308}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in L4 larval stage,
CC causes ectopic membrane extensions from body wall muscles.
CC {ECO:0000269|PubMed:16495308}.
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DR EMBL; Z70286; CAA94293.1; -; Genomic_DNA.
DR PIR; T23433; T23433.
DR RefSeq; NP_001023282.1; NM_001028111.3.
DR SMR; Q21313; -.
DR BioGRID; 43057; 9.
DR STRING; 6239.K08C7.3a.1; -.
DR iPTMnet; Q21313; -.
DR PaxDb; Q21313; -.
DR EnsemblMetazoa; K08C7.3b.1; K08C7.3b.1; WBGene00001328.
DR GeneID; 177956; -.
DR UCSC; K08C7.3a; c. elegans.
DR CTD; 177956; -.
DR WormBase; K08C7.3b; CE06136; WBGene00001328; epi-1.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000167067; -.
DR InParanoid; Q21313; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-3000157; Laminin interactions.
DR Reactome; R-CEL-446107; Type I hemidesmosome assembly.
DR PRO; PR:Q21313; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001328; Expressed in embryo and 12 other tissues.
DR ExpressionAtlas; Q21313; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:WormBase.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
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 population 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 GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 20.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 21.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 14.
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; 5.
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 Disulfide bond; Glycoprotein; Laminin EGF-like domain; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..3672
FT /note="Laminin-like protein epi-1"
FT /id="PRO_0000017100"
FT DOMAIN 28..297
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 298..356
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 357..426
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 427..471
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 472..518
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 519..563
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 564..609
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 610..655
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 656..700
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 701..755
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 756..808
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 809..839
FT /note="Laminin EGF-like 11; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1415..1460
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1461..1505
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1506..1553
FT /note="Laminin EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1554..1604
FT /note="Laminin EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1605..1614
FT /note="Laminin EGF-like 16; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1615..1796
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 1797..1829
FT /note="Laminin EGF-like 16; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1830..1879
FT /note="Laminin EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1880..1936
FT /note="Laminin EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1937..1989
FT /note="Laminin EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1990..2036
FT /note="Laminin EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2037..2083
FT /note="Laminin EGF-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2084..2131
FT /note="Laminin EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2693..2884
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2896..3066
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3072..3235
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3310..3482
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3488..3669
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 3236..3294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3236..3253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3267..3282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 2231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 2235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 2401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 2421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 2821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3087
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 298..307
FT /evidence="ECO:0000250"
FT DISULFID 300..320
FT /evidence="ECO:0000250"
FT DISULFID 322..331
FT /evidence="ECO:0000250"
FT DISULFID 334..354
FT /evidence="ECO:0000250"
FT DISULFID 357..366
FT /evidence="ECO:0000250"
FT DISULFID 359..391
FT /evidence="ECO:0000250"
FT DISULFID 394..403
FT /evidence="ECO:0000250"
FT DISULFID 406..424
FT /evidence="ECO:0000250"
FT DISULFID 427..438
FT /evidence="ECO:0000250"
FT DISULFID 429..445
FT /evidence="ECO:0000250"
FT DISULFID 447..456
FT /evidence="ECO:0000250"
FT DISULFID 459..469
FT /evidence="ECO:0000250"
FT DISULFID 472..484
FT /evidence="ECO:0000250"
FT DISULFID 474..491
FT /evidence="ECO:0000250"
FT DISULFID 493..502
FT /evidence="ECO:0000250"
FT DISULFID 505..516
FT /evidence="ECO:0000250"
FT DISULFID 519..531
FT /evidence="ECO:0000250"
FT DISULFID 521..538
FT /evidence="ECO:0000250"
FT DISULFID 540..549
FT /evidence="ECO:0000250"
FT DISULFID 552..561
FT /evidence="ECO:0000250"
FT DISULFID 564..576
FT /evidence="ECO:0000250"
FT DISULFID 566..583
FT /evidence="ECO:0000250"
FT DISULFID 585..594
FT /evidence="ECO:0000250"
FT DISULFID 597..607
FT /evidence="ECO:0000250"
FT DISULFID 610..622
FT /evidence="ECO:0000250"
FT DISULFID 612..629
FT /evidence="ECO:0000250"
FT DISULFID 631..640
FT /evidence="ECO:0000250"
FT DISULFID 643..653
FT /evidence="ECO:0000250"
FT DISULFID 656..668
FT /evidence="ECO:0000250"
FT DISULFID 658..674
FT /evidence="ECO:0000250"
FT DISULFID 676..685
FT /evidence="ECO:0000250"
FT DISULFID 688..698
FT /evidence="ECO:0000250"
FT DISULFID 701..715
FT /evidence="ECO:0000250"
FT DISULFID 703..724
FT /evidence="ECO:0000250"
FT DISULFID 726..735
FT /evidence="ECO:0000250"
FT DISULFID 738..753
FT /evidence="ECO:0000250"
FT DISULFID 756..770
FT /evidence="ECO:0000250"
FT DISULFID 758..777
FT /evidence="ECO:0000250"
FT DISULFID 779..788
FT /evidence="ECO:0000250"
FT DISULFID 791..806
FT /evidence="ECO:0000250"
FT DISULFID 809..821
FT /evidence="ECO:0000250"
FT DISULFID 811..828
FT /evidence="ECO:0000250"
FT DISULFID 830..839
FT /evidence="ECO:0000250"
FT DISULFID 1415..1427
FT /evidence="ECO:0000250"
FT DISULFID 1417..1434
FT /evidence="ECO:0000250"
FT DISULFID 1436..1445
FT /evidence="ECO:0000250"
FT DISULFID 1448..1458
FT /evidence="ECO:0000250"
FT DISULFID 1461..1469
FT /evidence="ECO:0000250"
FT DISULFID 1463..1476
FT /evidence="ECO:0000250"
FT DISULFID 1478..1487
FT /evidence="ECO:0000250"
FT DISULFID 1490..1503
FT /evidence="ECO:0000250"
FT DISULFID 1506..1520
FT /evidence="ECO:0000250"
FT DISULFID 1508..1527
FT /evidence="ECO:0000250"
FT DISULFID 1529..1538
FT /evidence="ECO:0000250"
FT DISULFID 1541..1551
FT /evidence="ECO:0000250"
FT DISULFID 1554..1566
FT /evidence="ECO:0000250"
FT DISULFID 1556..1573
FT /evidence="ECO:0000250"
FT DISULFID 1575..1584
FT /evidence="ECO:0000250"
FT DISULFID 1587..1602
FT /evidence="ECO:0000250"
FT DISULFID 1830..1839
FT /evidence="ECO:0000250"
FT DISULFID 1832..1846
FT /evidence="ECO:0000250"
FT DISULFID 1849..1858
FT /evidence="ECO:0000250"
FT DISULFID 1861..1877
FT /evidence="ECO:0000250"
FT DISULFID 1880..1894
FT /evidence="ECO:0000250"
FT DISULFID 1882..1905
FT /evidence="ECO:0000250"
FT DISULFID 1907..1916
FT /evidence="ECO:0000250"
FT DISULFID 1919..1934
FT /evidence="ECO:0000250"
FT DISULFID 1937..1951
FT /evidence="ECO:0000250"
FT DISULFID 1939..1958
FT /evidence="ECO:0000250"
FT DISULFID 1961..1970
FT /evidence="ECO:0000250"
FT DISULFID 1973..1987
FT /evidence="ECO:0000250"
FT DISULFID 1990..2000
FT /evidence="ECO:0000250"
FT DISULFID 1992..2007
FT /evidence="ECO:0000250"
FT DISULFID 2009..2018
FT /evidence="ECO:0000250"
FT DISULFID 2021..2034
FT /evidence="ECO:0000250"
FT DISULFID 2037..2048
FT /evidence="ECO:0000250"
FT DISULFID 2039..2055
FT /evidence="ECO:0000250"
FT DISULFID 2057..2066
FT /evidence="ECO:0000250"
FT DISULFID 2069..2081
FT /evidence="ECO:0000250"
FT DISULFID 2084..2096
FT /evidence="ECO:0000250"
FT DISULFID 2086..2103
FT /evidence="ECO:0000250"
FT DISULFID 2105..2114
FT /evidence="ECO:0000250"
FT DISULFID 2117..2129
FT /evidence="ECO:0000250"
FT DISULFID 3040..3066
FT /evidence="ECO:0000250"
FT DISULFID 3209..3235
FT /evidence="ECO:0000250"
FT DISULFID 3460..3482
FT /evidence="ECO:0000250"
FT DISULFID 3633..3669
FT /evidence="ECO:0000250"
FT MUTAGEN 2802
FT /note="L->F: In rh152; causes ectopic muscle membrane
FT extensions."
FT /evidence="ECO:0000269|PubMed:16495308"
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
