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Laminin subunit gamma-1 (Laminin B2 chain) (Laminin-1 subunit gamma) (Laminin-10 subunit gamma) (Laminin-11 subunit gamma) (Laminin-2 subunit gamma) (Laminin-3 subunit gamma) (Laminin-4 subunit gamma) (Laminin-6 subunit gamma) (Laminin-7 subunit gamma) (Laminin-8 subunit gamma) (Laminin-9 subunit gamma) (S-laminin subunit gamma) (S-LAM gamma)

 LAMC1_MOUSE             Reviewed;        1607 AA.
P02468;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
07-NOV-2018, entry version 186.
RecName: Full=Laminin subunit gamma-1;
AltName: Full=Laminin B2 chain;
AltName: Full=Laminin-1 subunit gamma;
AltName: Full=Laminin-10 subunit gamma;
AltName: Full=Laminin-11 subunit gamma;
AltName: Full=Laminin-2 subunit gamma;
AltName: Full=Laminin-3 subunit gamma;
AltName: Full=Laminin-4 subunit gamma;
AltName: Full=Laminin-6 subunit gamma;
AltName: Full=Laminin-7 subunit gamma;
AltName: Full=Laminin-8 subunit gamma;
AltName: Full=Laminin-9 subunit gamma;
AltName: Full=S-laminin subunit gamma;
Short=S-LAM gamma;
Flags: Precursor;
Name=Lamc1; Synonyms=Lamb-2, Lamc-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3680290;
Sasaki M., Yamada Y.;
"The laminin B2 chain has a multidomain structure homologous to the B1
chain.";
J. Biol. Chem. 262:17111-17117(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3167041; DOI=10.1021/bi00414a038;
Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.;
"Primary structure of the mouse laminin B2 chain and comparison with
laminin B1.";
Biochemistry 27:5198-5204(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
PubMed=2836421;
Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.;
"The laminin B2 chain promoter contains unique repeat sequences and is
active in transient transfection.";
J. Biol. Chem. 263:8384-8389(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1607.
PubMed=6209134;
Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.;
"Sequencing of laminin B chain cDNAs reveals C-terminal regions of
coiled-coil alpha-helix.";
EMBO J. 3:2355-2362(1984).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-648; ASN-1105; ASN-1203;
ASN-1221 AND ASN-1393.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932.
PubMed=8648630; DOI=10.1006/jmbi.1996.0191;
Stetefeld J., Mayer U., Timpl R., Huber R.;
"Crystal structure of three consecutive laminin-type epidermal growth
factor-like (LE) modules of laminin gamma1 chain harboring the nidogen
binding site.";
J. Mol. Biol. 257:644-657(1996).
[8]
STRUCTURE BY NMR OF 824-881.
PubMed=8648631; DOI=10.1006/jmbi.1996.0192;
Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R.,
Holak T.A.;
"Structure of the nidogen binding LE module of the laminin gamma1
chain in solution.";
J. Mol. Biol. 257:658-668(1996).
-!- FUNCTION: Binding to cells via a high affinity receptor, laminin
is thought to mediate the attachment, migration and organization
of cells into tissues during embryonic development by interacting
with other extracellular matrix components.
-!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
different polypeptide chains (alpha, beta, gamma), which are bound
to each other by disulfide bonds into a cross-shaped molecule
comprising one long and three short arms with globules at each
end. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS
laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-
121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6
(laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin),
laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10
(laminin-511) and laminin-11 (laminin-521).
-!- INTERACTION:
P02469:Lamb1; NbExp=4; IntAct=EBI-7059830, EBI-6662997;
P10493:Nid1; NbExp=5; IntAct=EBI-7059830, EBI-1032117;
Q9JI33:Ntn4; NbExp=2; IntAct=EBI-7059830, EBI-15755373;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- TISSUE SPECIFICITY: Found in the basement membranes (major
component).
-!- DOMAIN: The alpha-helical domains I and II are thought to interact
with other laminin chains to form a coiled coil structure.
-!- DOMAIN: Domains VI and IV are globular.
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EMBL; X05211; CAA28838.1; -; mRNA.
EMBL; J03484; AAA39405.1; -; mRNA.
EMBL; J02930; AAA39408.1; -; mRNA.
EMBL; J03749; AAA39409.1; -; Genomic_DNA.
CCDS; CCDS15370.1; -.
PIR; A28469; MMMSB2.
PIR; S55783; S55783.
UniGene; Mm.1249; -.
PDB; 1KLO; X-ray; 2.10 A; A=771-932.
PDB; 1NPE; X-ray; 2.30 A; B=769-932.
PDB; 1TLE; NMR; -; A=824-881.
PDB; 4AQT; X-ray; 3.20 A; A=33-395.
PDB; 5MC9; X-ray; 2.13 A; C=1548-1607.
PDBsum; 1KLO; -.
PDBsum; 1NPE; -.
PDBsum; 1TLE; -.
PDBsum; 4AQT; -.
PDBsum; 5MC9; -.
ProteinModelPortal; P02468; -.
SMR; P02468; -.
ComplexPortal; CPX-3008; Laminin-111 complex.
ComplexPortal; CPX-3009; Laminin-211 complex.
ComplexPortal; CPX-3010; Laminin-121 complex.
ComplexPortal; CPX-3011; Laminin-221 complex.
ComplexPortal; CPX-3013; Laminin-311 complex variant A.
ComplexPortal; CPX-3014; Laminin-321 complex.
ComplexPortal; CPX-3015; Laminin-411 complex.
ComplexPortal; CPX-3016; Laminin-511 complex.
ComplexPortal; CPX-3017; Laminin-521 complex.
ComplexPortal; CPX-3031; Laminin-421 complex.
ComplexPortal; CPX-3167; Laminin-311 complex variant B.
DIP; DIP-41793N; -.
IntAct; P02468; 10.
MINT; P02468; -.
STRING; 10090.ENSMUSP00000027752; -.
iPTMnet; P02468; -.
PhosphoSitePlus; P02468; -.
EPD; P02468; -.
MaxQB; P02468; -.
PaxDb; P02468; -.
PeptideAtlas; P02468; -.
PRIDE; P02468; -.
MGI; MGI:99914; Lamc1.
eggNOG; KOG1836; Eukaryota.
eggNOG; ENOG410XRDC; LUCA.
HOGENOM; HOG000019301; -.
HOVERGEN; HBG100808; -.
InParanoid; P02468; -.
PhylomeDB; P02468; -.
ChiTaRS; Lamc1; mouse.
EvolutionaryTrace; P02468; -.
PRO; PR:P02468; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_LAMC1; -.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005606; C:laminin-1 complex; ISO:MGI.
GO; GO:0043259; C:laminin-10 complex; IPI:MGI.
GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI.
GO; GO:0007155; P:cell adhesion; ISS:HGNC.
GO; GO:0016477; P:cell migration; ISS:HGNC.
GO; GO:0022617; P:extracellular matrix disassembly; ISS:HGNC.
GO; GO:0031581; P:hemidesmosome assembly; ISS:HGNC.
GO; GO:0031175; P:neuron projection development; IDA:MGI.
GO; GO:0065003; P:protein-containing complex assembly; ISS:HGNC.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
Gene3D; 2.60.120.1490; -; 1.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR000034; Laminin_IV.
InterPro; IPR008211; Laminin_N.
InterPro; IPR038684; Laminin_N_sf.
Pfam; PF00052; Laminin_B; 1.
Pfam; PF00053; Laminin_EGF; 11.
Pfam; PF00055; Laminin_N; 1.
SMART; SM00181; EGF; 9.
SMART; SM00180; EGF_Lam; 10.
SMART; SM00281; LamB; 1.
SMART; SM00136; LamNT; 1.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS01248; EGF_LAM_1; 10.
PROSITE; PS50027; EGF_LAM_2; 10.
PROSITE; PS51115; LAMININ_IVA; 1.
PROSITE; PS51117; LAMININ_NTER; 1.
1: Evidence at protein level;
3D-structure; Basement membrane; Cell adhesion; Coiled coil;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Laminin EGF-like domain; Phosphoprotein; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 33
CHAIN 34 1607 Laminin subunit gamma-1.
/FTId=PRO_0000017075.
DOMAIN 44 283 Laminin N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00466}.
DOMAIN 284 339 Laminin EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 340 395 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 396 442 Laminin EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 443 492 Laminin EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 493 502 Laminin EGF-like 5; first part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 512 687 Laminin IV type A. {ECO:0000255|PROSITE-
ProRule:PRU00458}.
DOMAIN 688 721 Laminin EGF-like 5; second part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 722 770 Laminin EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 771 825 Laminin EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 826 881 Laminin EGF-like 8; nidogen-binding.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 882 932 Laminin EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 933 980 Laminin EGF-like 10.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 981 1028 Laminin EGF-like 11.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
REGION 1029 1607 Domain II and I.
COILED 1034 1594 {ECO:0000255}.
MOD_RES 1147 1147 Phosphoserine.
{ECO:0000250|UniProtKB:P11047}.
MOD_RES 1491 1491 Phosphoserine.
{ECO:0000250|UniProtKB:P11047}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 132 132 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 648 648 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 1020 1020 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1105 1105 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 1159 1159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1173 1173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1203 1203 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 1221 1221 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 1239 1239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1378 1378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1393 1393 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 1437 1437 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 284 293 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 286 303 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 305 314 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 340 349 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 342 365 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 368 377 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 380 393 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 396 408 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 398 414 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 416 425 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 428 440 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 443 454 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 445 461 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 463 472 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 475 490 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 722 731 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 724 738 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 740 749 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 752 768 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 771 779
DISULFID 773 790
DISULFID 793 802
DISULFID 805 823
DISULFID 826 840
DISULFID 828 847
DISULFID 850 859
DISULFID 862 879
DISULFID 882 896
DISULFID 884 903
DISULFID 905 914
DISULFID 917 930
DISULFID 933 945 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 935 952 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 954 963 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 966 978 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 981 993 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 983 999 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 1001 1010 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 1013 1026 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 1029 1029 Interchain. {ECO:0000305}.
DISULFID 1032 1032 Interchain. {ECO:0000305}.
DISULFID 1598 1598 Interchain (with beta-1 chain).
CONFLICT 216 216 G -> A (in Ref. 3; AAA39409).
{ECO:0000305}.
CONFLICT 260 260 E -> D (in Ref. 2). {ECO:0000305}.
CONFLICT 337 337 S -> C (in Ref. 2; AAA39408).
{ECO:0000305}.
CONFLICT 447 448 LR -> PS (in Ref. 2; AAA39408).
{ECO:0000305}.
CONFLICT 544 544 D -> Y (in Ref. 2; AAA39408).
{ECO:0000305}.
CONFLICT 662 662 T -> S (in Ref. 2; AAA39408).
{ECO:0000305}.
CONFLICT 886 886 Missing (in Ref. 2; AAA39408).
{ECO:0000305}.
CONFLICT 1158 1158 Missing (in Ref. 2; AAA39408).
{ECO:0000305}.
CONFLICT 1434 1434 V -> A (in Ref. 2; AAA39408).
{ECO:0000305}.
CONFLICT 1475 1475 R -> K (in Ref. 4; CAA28838).
{ECO:0000305}.
CONFLICT 1576 1576 D -> N (in Ref. 4; CAA28838).
{ECO:0000305}.
TURN 55 58 {ECO:0000244|PDB:4AQT}.
STRAND 62 64 {ECO:0000244|PDB:4AQT}.
STRAND 72 75 {ECO:0000244|PDB:4AQT}.
STRAND 87 90 {ECO:0000244|PDB:4AQT}.
STRAND 92 94 {ECO:0000244|PDB:4AQT}.
TURN 95 97 {ECO:0000244|PDB:4AQT}.
HELIX 101 104 {ECO:0000244|PDB:4AQT}.
STRAND 110 112 {ECO:0000244|PDB:4AQT}.
HELIX 121 123 {ECO:0000244|PDB:4AQT}.
STRAND 126 128 {ECO:0000244|PDB:4AQT}.
STRAND 131 153 {ECO:0000244|PDB:4AQT}.
STRAND 156 168 {ECO:0000244|PDB:4AQT}.
STRAND 171 177 {ECO:0000244|PDB:4AQT}.
HELIX 180 184 {ECO:0000244|PDB:4AQT}.
STRAND 202 205 {ECO:0000244|PDB:4AQT}.
STRAND 212 214 {ECO:0000244|PDB:4AQT}.
STRAND 216 221 {ECO:0000244|PDB:4AQT}.
TURN 222 225 {ECO:0000244|PDB:4AQT}.
HELIX 229 234 {ECO:0000244|PDB:4AQT}.
HELIX 236 241 {ECO:0000244|PDB:4AQT}.
STRAND 243 253 {ECO:0000244|PDB:4AQT}.
HELIX 259 261 {ECO:0000244|PDB:4AQT}.
HELIX 265 268 {ECO:0000244|PDB:4AQT}.
STRAND 274 284 {ECO:0000244|PDB:4AQT}.
STRAND 293 295 {ECO:0000244|PDB:4AQT}.
STRAND 301 303 {ECO:0000244|PDB:4AQT}.
STRAND 309 311 {ECO:0000244|PDB:4AQT}.
HELIX 342 344 {ECO:0000244|PDB:4AQT}.
STRAND 349 351 {ECO:0000244|PDB:4AQT}.
HELIX 353 358 {ECO:0000244|PDB:4AQT}.
STRAND 363 365 {ECO:0000244|PDB:4AQT}.
TURN 369 371 {ECO:0000244|PDB:4AQT}.
STRAND 372 374 {ECO:0000244|PDB:4AQT}.
STRAND 382 385 {ECO:0000244|PDB:4AQT}.
STRAND 779 781 {ECO:0000244|PDB:1KLO}.
STRAND 783 785 {ECO:0000244|PDB:1KLO}.
STRAND 788 790 {ECO:0000244|PDB:1KLO}.
STRAND 797 799 {ECO:0000244|PDB:1KLO}.
STRAND 809 812 {ECO:0000244|PDB:1KLO}.
STRAND 816 819 {ECO:0000244|PDB:1NPE}.
STRAND 821 825 {ECO:0000244|PDB:1KLO}.
STRAND 834 837 {ECO:0000244|PDB:1TLE}.
TURN 842 844 {ECO:0000244|PDB:1KLO}.
STRAND 846 849 {ECO:0000244|PDB:1TLE}.
TURN 856 859 {ECO:0000244|PDB:1KLO}.
STRAND 866 868 {ECO:0000244|PDB:1KLO}.
HELIX 875 877 {ECO:0000244|PDB:1KLO}.
STRAND 878 881 {ECO:0000244|PDB:1KLO}.
TURN 886 888 {ECO:0000244|PDB:1KLO}.
HELIX 890 892 {ECO:0000244|PDB:1KLO}.
TURN 898 900 {ECO:0000244|PDB:1KLO}.
STRAND 909 911 {ECO:0000244|PDB:1KLO}.
HELIX 924 926 {ECO:0000244|PDB:1KLO}.
HELIX 1555 1593 {ECO:0000244|PDB:5MC9}.
SEQUENCE 1607 AA; 177298 MW; 81B7B08E4869F242 CRC64;
MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP EFVNAAFNVT
VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG AAFLTDYNNQ ADTTWWQSQT
MLAGVQYPNS INLTLHLGKA FDITYVRLKF HTSRPESFAI YKRTREDGPW IPYQYYSGSC
ENTYSKANRG FIRTGGDEQQ ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE
WVTATDIRVT LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK
LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY FDPELYRSTG
HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP VGSLSTQCDS YGRCSCKPGV
MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS TDECNVETGR CVCKDNVEGF NCERCKPGFF
NLESSNPKGC TPCFCFGHSS VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS
DRQDIAVISD SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL
RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT SIKIRGTYSE
RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE TCLPGYRRET PSLGPYSPCV
LCTCNGHSET CDPETGVCDC RDNTAGPHCE KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA
IVPKTKEVVC THCPTGTAGK RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC
NRLTGECLKC IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT
GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG QCECQPGITG
QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE CREGFVGNRC DQCEENYFYN
RSWPGCQECP ACYRLVKDKA AEHRVKLQEL ESLIANLGTG DDMVTDQAFE DRLKEAEREV
TDLLREAQEV KDVDQNLMDR LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE
QLIEIASREL EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK
TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR VHEEAKRAGD
KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ KLKDYEDLRE DMRGKEHEVK
NLLEKGKAEQ QTADQLLARA DAAKALAEEA AKKGRSTLQE ANDILNNLKD FDRRVNDNKT
AAEEALRRIP AINRTIAEAN EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS
TKADAERTFG EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN
ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS DLDRKVSDLE
SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN TPSIEKP


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