LAMC1_DROME
ID LAMC1_DROME Reviewed; 1639 AA.
AC P15215; Q24373; Q5BI30; Q9VT18;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Laminin subunit gamma-1;
DE AltName: Full=Laminin B2 chain;
DE Flags: Precursor;
GN Name=LanB2; Synonyms=LAMC1, LAMG1; ORFNames=CG3322;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=2912972; DOI=10.1016/s0021-9258(18)94221-3;
RA Chi H.-C., Hui C.-F.;
RT "Primary structure of the Drosophila laminin B2 chain and comparison with
RT human, mouse, and Drosophila laminin B1 and B2 chains.";
RL J. Biol. Chem. 264:1543-1550(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=2808533; DOI=10.1083/jcb.109.5.2441;
RA Montell D.J., Goodman C.S.;
RT "Drosophila laminin: sequence of B2 subunit and expression of all three
RT subunits during embryogenesis.";
RL J. Cell Biol. 109:2441-2453(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=1840513; DOI=10.1089/dna.1991.10.451;
RA Chi H.-C., Juminaga D., Wang S.Y., Hui C.-F.;
RT "Structure of the Drosophila gene for the laminin B2 chain.";
RL DNA Cell Biol. 10:451-466(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 344-1639.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=3405777; DOI=10.1093/nar/16.14.7205;
RA Chi H.-C., Hui C.-F.;
RT "cDNA and amino acid sequences of Drosophila laminin B2 chain.";
RL Nucleic Acids Res. 16:7205-7206(1988).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domains VI and IV are globular.
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DR EMBL; M58417; AAA28665.1; -; Genomic_DNA.
DR EMBL; M25063; AAA28664.1; -; mRNA.
DR EMBL; AE014296; AAF50238.1; -; Genomic_DNA.
DR EMBL; BT021394; AAX33542.1; -; mRNA.
DR PIR; A31483; MMFFB2.
DR RefSeq; NP_001287009.1; NM_001300080.1.
DR RefSeq; NP_524006.1; NM_079282.2.
DR AlphaFoldDB; P15215; -.
DR SMR; P15215; -.
DR BioGRID; 64509; 15.
DR DIP; DIP-21994N; -.
DR IntAct; P15215; 12.
DR STRING; 7227.FBpp0076111; -.
DR GlyGen; P15215; 10 sites.
DR PaxDb; P15215; -.
DR PRIDE; P15215; -.
DR EnsemblMetazoa; FBtr0076382; FBpp0076111; FBgn0267348.
DR EnsemblMetazoa; FBtr0345031; FBpp0311281; FBgn0267348.
DR GeneID; 39118; -.
DR KEGG; dme:Dmel_CG3322; -.
DR CTD; 39118; -.
DR FlyBase; FBgn0267348; LanB2.
DR VEuPathDB; VectorBase:FBgn0267348; -.
DR eggNOG; KOG1836; Eukaryota.
DR HOGENOM; CLU_002471_1_0_1; -.
DR InParanoid; P15215; -.
DR OMA; TCVQLAD; -.
DR OrthoDB; 156553at2759; -.
DR PhylomeDB; P15215; -.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-3000157; Laminin interactions.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-446107; Type I hemidesmosome assembly.
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR SignaLink; P15215; -.
DR BioGRID-ORCS; 39118; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39118; -.
DR PRO; PR:P15215; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0267348; Expressed in embryonic/larval hemocyte (Drosophila) and 33 other tissues.
DR ExpressionAtlas; P15215; baseline and differential.
DR Genevisible; P15215; DM.
DR GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IMP:FlyBase.
DR GO; GO:0071711; P:basement membrane organization; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP:FlyBase.
DR GO; GO:0085029; P:extracellular matrix assembly; IMP:FlyBase.
DR GO; GO:0007494; P:midgut development; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 9.
DR InterPro; IPR000742; EGF-like_dom.
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; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01248; EGF_LAM_1; 11.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1639
FT /note="Laminin subunit gamma-1"
FT /id="PRO_0000017081"
FT DOMAIN 63..298
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 299..358
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 359..413
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 414..460
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 461..513
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 514..523
FT /note="Laminin EGF-like 5; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 533..709
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 710..743
FT /note="Laminin EGF-like 5; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 744..792
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 793..846
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 847..901
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 902..955
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 956..1003
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1004..1049
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1050..1609
FT /note="Domain II and I"
FT COILED 1087..1109
FT /evidence="ECO:0000255"
FT COILED 1144..1247
FT /evidence="ECO:0000255"
FT COILED 1306..1627
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 299..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 301..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 324..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 336..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 359..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 361..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 387..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 399..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 414..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 416..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 434..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 446..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 461..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 463..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 484..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 496..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 712..721
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 724..741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 744..753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 746..760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 762..771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 774..790
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 793..801
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 795..811
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 814..823
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 826..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 847..861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 849..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 871..880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 883..899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 902..919
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 904..926
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 928..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 940..953
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 956..968
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 958..975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 977..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 989..1001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1004..1016
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1006..1022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1024..1033
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1036..1047
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1050
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1053
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1631
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT VARIANT 831
FT /note="F -> Y"
FT VARIANT 892
FT /note="L -> P (in strain: Oregon-R)"
FT CONFLICT 1026..1027
FT /note="DN -> EY (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1639 AA; 182339 MW; 8F510AC6933A52BC CRC64;
MKRSRWSHSG SSTARLLLIG VLFASCSTAI LGAQRPPINS AGGHELRGTT FMPALECYDP
YGRPQKCLPE FINAAYQLQI ESTNTCGEQN DNHFCIQTMN QNHKNCEFCK YNDHNPSFLT
DLHDPQSPTW WQSETMFEGI QHPNYVNLTL HLGKSYDITY VRILFRSPRP ESFTIYKRTS
ESGPWIPYQF YSATCRDTYS LPDSRAIRKG EGEAHALCTS EYSDISPLRD GEIAFSTLEG
RPSGINFERS GELQEWVTAT DIRITLDRLN TFGDELFGDS QVLKSYFYAI SDIAVGARCK
CNGHASKCVP STGMHGERTL VCECRHNTDG PDCDRCLPLY NDLKWKRSTS TEVNECKACN
CNGLADKCFF DANLFNRTGH GGHCLDCREN RDGPNCERCK ENFYMRDDGY CVNCACDPVG
SRSLQCNSHG KCQCKPGVTG DKCDRCDNNY YQFGPHGCQQ CGCDSGGSHQ NTPACDTETG
ICFCKENVEG RRCNECKPGF FNLDKNNRFG CTPCFCYGHT SECMTAPGYS IVSVTSNFNK
FKERWTAADL NQREVDIKYN QYSRSIGTTA QGNEHVYFQA PDRFLGDQRA SYNRDLKFKL
QLVGQVANTG VSDVILEGAG SRISLPIFAQ GNGIPDQGVK EYTFRLHEHH DYQWQPSQSA
RGFLSILSNL TAIKIRATYS VQGEAILDDV ELQTAHRGAA GHPATWIEQC TCPEGYLGQF
CESCAPGYRH SPARGGPFMP CIPCDCHGHA DICDSETGRC ICQHNTHGDN CDQCAKGFYG
NALGGTPNDC KRCPCPNDGA CLQINEDTVI CTECPKGYFG SRCEQCSDGF FGDPTGLLGE
VQTCKSCDCN GNVDPNAVGN CNRTTGECLK CIHNTAGEHC DQCLSGHFGD PLALPHGRCD
RCSCYEAGTE QDEQSITRCD QVTGQCQCKP NVIGRDCGEC QPGYFNIRSG NGCENCLCDP
VGSYNSTCDR YSGQCHCRPG VMGQRCDQCE NYFYGFSSEG CKPCECDESG SKGFQCDQNG
QCPCNDNVEG RRCDRCKENK YDRHRGCIDC PDCYNLVQDA ADLHRAKLFN LSQTLDEIAR
TPVTNDDEFE AKLKAVQEKV AVLAQDARDN SGDGGQTYAE VIDDLHKHLD SVREHLVSAD
KFQADANGEI DRARQNYTIL DQITENAKKE LQQALDLLND EGAQALARAK EKSVEFGQQS
EQISDISREA RALADKLESE AQFDLKNAKD AKDAVEKAHQ LAKSAIDLQL KIGTELRSEV
GLELSHVKQS LGTVVQTSKE ALRKANEVYD TALTLLNDVN RQTQPEIDIS QLKKDAVAAN
ERADELLKQI TELSNSNGEL FADFETEQEL TEALLKRAEQ QQLEDIELLE RAKAAHDKAT
KAVEQGDNTL KEANNTYEKL AGFQSDVQRS SESAEKALQT VPNIEKEIQN AESLISQAEE
ALDGANKNAN EAKKNAQEAQ LKYAEQASKD AELIRRKANE TKVAARNLRE EADQLNHRVK
LTEMDIFKLE ESSTKDDNLV DDAKRKVGQA KADTQEAQKQ IEKANADLTA IKDELENLKD
INTGDLDRLE NRLATVEGEI NRVNLTGRIE KYREQRTIQK NLIDKYDAEL RELKDEVQNI
GLISKALPDS CFSRNRLEP
