LAMB1_DROME
ID LAMB1_DROME Reviewed; 1788 AA.
AC P11046; A4V0D8; Q26328; Q6AWM6; Q8SWY0; Q9VLW6; Q9XZT4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 4.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Laminin subunit beta-1;
DE AltName: Full=Laminin B1 chain;
DE Flags: Precursor;
GN Name=LanB1; Synonyms=lamB1; ORFNames=CG7123;
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 [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=8397815; DOI=10.1089/dna.1993.12.573;
RA Gow C.-H., Chang H.-Y., Lih C.-J., Chang T.-W., Hui C.-F.;
RT "Analysis of the Drosophila gene for the laminin B1 chain.";
RL DNA Cell Biol. 12:573-587(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3365769; DOI=10.1016/0092-8674(88)90166-3;
RA Montell D.J., Goodman C.S.;
RT "Drosophila substrate adhesion molecule: sequence of laminin B1 chain
RT reveals domains of homology with mouse.";
RL Cell 53:463-473(1988).
RN [3]
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 [4]
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 [5]
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 (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-1788.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30260959; DOI=10.1371/journal.pgen.1007483;
RA Dai J., Estrada B., Jacobs S., Sanchez-Sanchez B.J., Tang J., Ma M.,
RA Magadan-Corpas P., Pastor-Pareja J.C., Martin-Bermudo M.D.;
RT "Dissection of Nidogen function in Drosophila reveals tissue-specific
RT mechanisms of basement membrane assembly.";
RL PLoS Genet. 14:E1007483-E1007483(2018).
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 (By similarity). Required for Ndg
CC localization to the basement membrane (PubMed:30260959).
CC {ECO:0000250|UniProtKB:Q13753, ECO:0000269|PubMed:30260959}.
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 {ECO:0000269|PubMed:30260959}.
CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major component).
CC -!- DEVELOPMENTAL STAGE: In the larva, expressed mainly by fat body
CC adipocytes and blood cells and secreted in the basal membranes that
CC surround the fat body, imaginal disks, tracheae, salivary glands,
CC midgut, mature muscles and heart (at protein level).
CC {ECO:0000269|PubMed:30260959}.
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.
CC -!- DISRUPTION PHENOTYPE: Results in strong reduction of Ndg accumulation
CC at the basement membrane in the gut, muscles and ventral nerve cord
CC (PubMed:30260959). RNAi-mediated knockdown in the larvae reduces Ndg
CC accumulation and created holes in the basal membrane of fat bodies
CC (PubMed:30260959). {ECO:0000269|PubMed:30260959}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT94451.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M95811; AAD19752.1; -; Genomic_DNA.
DR EMBL; M19525; AAA28663.1; -; mRNA.
DR EMBL; AE014134; AAF52563.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10647.1; -; Genomic_DNA.
DR EMBL; BT015222; AAT94451.1; ALT_FRAME; mRNA.
DR EMBL; AY095001; AAM11329.1; ALT_INIT; mRNA.
DR PIR; A28783; MMFFB1.
DR RefSeq; NP_476618.1; NM_057270.5.
DR RefSeq; NP_723319.1; NM_164773.3.
DR AlphaFoldDB; P11046; -.
DR SMR; P11046; -.
DR BioGRID; 60207; 27.
DR IntAct; P11046; 9.
DR STRING; 7227.FBpp0079113; -.
DR GlyGen; P11046; 16 sites.
DR iPTMnet; P11046; -.
DR PaxDb; P11046; -.
DR PRIDE; P11046; -.
DR EnsemblMetazoa; FBtr0079490; FBpp0079113; FBgn0261800.
DR EnsemblMetazoa; FBtr0079491; FBpp0079114; FBgn0261800.
DR GeneID; 34068; -.
DR KEGG; dme:Dmel_CG7123; -.
DR CTD; 34068; -.
DR FlyBase; FBgn0261800; LanB1.
DR VEuPathDB; VectorBase:FBgn0261800; -.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000167171; -.
DR HOGENOM; CLU_001560_1_0_1; -.
DR InParanoid; P11046; -.
DR OMA; LMHQITG; -.
DR OrthoDB; 65841at2759; -.
DR PhylomeDB; P11046; -.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-DME-2022928; HS-GAG biosynthesis.
DR Reactome; R-DME-2024096; HS-GAG degradation.
DR Reactome; R-DME-3000157; Laminin interactions.
DR Reactome; R-DME-3000178; ECM proteoglycans.
DR Reactome; R-DME-373752; Netrin-1 signaling.
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; P11046; -.
DR BioGRID-ORCS; 34068; 0 hits in 3 CRISPR screens.
DR ChiTaRS; LanB1; fly.
DR GenomeRNAi; 34068; -.
DR PRO; PR:P11046; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261800; Expressed in embryonic/larval hemocyte (Drosophila) and 27 other tissues.
DR Genevisible; P11046; DM.
DR GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0048513; P:animal organ development; IMP:FlyBase.
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:UniProtKB.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
DR GO; GO:0016477; P:cell migration; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:FlyBase.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP: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; 13.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 12.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1788
FT /note="Laminin subunit beta-1"
FT /id="PRO_0000017073"
FT DOMAIN 50..287
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 288..354
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 355..417
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 418..477
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 478..528
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 529..559
FT /note="Laminin EGF-like 5; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 567..783
FT /note="Laminin IV type B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT DOMAIN 789..836
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 837..882
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 883..932
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 933..990
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 991..1042
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1043..1093
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1094..1141
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1142..1188
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 23..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1405
FT /note="Domain II"
FT REGION 1406..1432
FT /note="Domain alpha"
FT REGION 1433..1788
FT /note="Domain I"
FT REGION 1690..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1255..1405
FT /evidence="ECO:0000255"
FT COILED 1453..1505
FT /evidence="ECO:0000255"
FT COILED 1540..1561
FT /evidence="ECO:0000255"
FT COILED 1608..1762
FT /evidence="ECO:0000255"
FT MOTIF 641..643
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 26..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1051
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 1515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 288..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 290..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 320..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 332..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 355..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 357..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 385..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 397..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 418..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 420..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 448..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 460..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 478..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 480..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 500..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 512..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 529..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 531..548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 550..559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 789..801
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 791..808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 810..819
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 822..834
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 837..849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 839..856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 858..867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 870..880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 883..892
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 885..899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 902..911
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 914..930
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 933..949
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 935..960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 962..971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 974..988
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 991..1005
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 993..1012
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1015..1024
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1027..1040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1043..1057
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1045..1064
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1066..1075
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1078..1091
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1094..1106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1096..1113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1115..1124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1127..1139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1142..1154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1144..1161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1163..1172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1175..1186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1189
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1192
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1786
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="L -> LAL (in Ref. 1; AAD19752 and 2; AAA28663)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="L -> H (in Ref. 1; AAD19752)"
FT /evidence="ECO:0000305"
FT CONFLICT 724..725
FT /note="DS -> VT (in Ref. 2; AAA28663)"
FT /evidence="ECO:0000305"
FT CONFLICT 766..767
FT /note="KS -> NA (in Ref. 1; AAD19752 and 2; AAA28663)"
FT /evidence="ECO:0000305"
FT CONFLICT 939
FT /note="V -> I (in Ref. 5; AAT94451)"
FT /evidence="ECO:0000305"
FT CONFLICT 946..947
FT /note="Missing (in Ref. 1; AAD19752 and 2; AAA28663)"
FT /evidence="ECO:0000305"
FT CONFLICT 1356..1373
FT /note="TDRNCKRVENLSNKIQAE -> SDRIAREWKICLIRFRPN (in Ref. 1;
FT AAD19752 and 2; AAA28663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1788 AA; 198333 MW; 7CB99C9608452085 CRC64;
MLELRLIVVI VLALLSWQWD PVDSQRPPQH GRRDRPKYPP NKFIKTHPCE RSSCYPATGN
LLIGRENRLT ASSTCGLHSP ERFCILSHLQ DKKCFLCDTR EETKHDPYKN HRIGQIIYKT
KPGTNIPTWW QSENGKENAT IQLDLEAEFH FTHLIITFTT FRPAAMYIER SFDFGQTWHI
YRYFAYDCKE SFPGVPTVLE NITDVMCTSR YSNVEPSRNG EVIFRVLPPN INVTDPYAEH
VQNQLKMTNL RIQMTKLHKL GDNLLDSRLE NEEKYYYGIS NMVVRGSCSC YGHASQCLPL
DPAFSQADNE DGMVHGRCEC THNTKGMNCE ECEDFFNDLP WKPAFGKKTN ACKKCECNDH
AVSCHFDEAV FTASGFVSGG VCDNCLHNTR GQHCEECMPY FYRDPEQDIT SERVCQPCDC
DPQGSSDDGI CDSLNELEEG AVAGACHCKA FVTGRRCNQC KDGYWNLQSD NPEGCEPCTC
NPLGTLNNSG CVMRTGECKC KKYVTGKDCN QCMPETYGLS ESPEGCSLCN CDAGGSYDNY
CDVISGQCRC RPHMTGRSCS QPKQNYFIPL LPEVHEAEVV DECISYGANG NCSLVAETPD
GSFTGIGFTR VPENSELVFT VGDIPRSMPY DAVIRYQSTS RGDWENAFIT LVRPDQVDPE
GGCGELAAAT SSETRIPFSL PDRSRQVVAL NEVCLEAGKV YKFRIYFERK RHDVDSPTAT
ILVDSLTLIP RIDVTPIFQG SVLADIRKKD YEKYNCKSSL YDMNYKSDPK CQNLDNILSV
FVHDGASMCN CNPTGSLSKV CESNGGYCQC KPNVVGRQCD QCAPGTYGFG PEGCKACDCN
SIGSKDKYCD LITGQCQCVP NTYGRECNQC QPGYWNFPEC RVCQCNGHAA TCDPIQGTCI
DCQDSTTGYS CDSCLDGYYG NPLFGSEIGC RPCRCPETVA SGLAHADGCS LDTRNNNMLC
HCQEGYSGSR CEICADNFFG NPDNGGTCSK CECSNNVDLY DTGNCDRQTG ACLKCLYQTT
GDHCELCKDG FFGDALQQNC QQCECDFLGT NNTIAHCDRF TGQCPCLPNV QGVRCDQCAE
NHWKIASGEG CESCNCDPIG ALHEQCNSYT GQCQCKPGFG GRACNQCQAH YWGNPNEKCQ
PCECDQFGAA DFQCDRETGN CVCHEGIGGY KCNECARGYI GQFPHCSPCG ECFNNWDLIL
SALEDATTAT ILRAKEIKQV GATGAYTSEF SELDKKLQHI RNLLQNTSVS LVDIEKLDYE
TQSLRDQLQA SHGRLSETEQ NLDDIYNSLS LSGVELESLQ NHSRLVQQLS KELKENGIQL
QESNIEGALN LTRHAYERVS NLSTLKDEAN ELASNTDRNC KRVENLSNKI QAEADDLANN
NKLIEDYRAE LTSLTSQIPE LNNQVCGKPG DPCDSLCGGA GCGHCGGFLS CEHGAKTHSE
EALKVAKDAE TAITSKKDQA DQTIRALTQA KLNASEAYEK AKRGFEQSER YLNQTNANIK
LAENLFIALN NFQENKTASP SESKELAQKT LDLDLKLEPE EIETLGDQIN RAVSSLKNVE
AIIYRTKPDL DRVNNLQSIA NATKEKADKI LDSANSVVES LAAADESQGK AKDAIQQANS
NIELAGQDLE KIDEETYSAE APANNTAQQV EKLAKKVQKL QNNIMKNDRD AKEITKEAGS
VKLEAMRARG EANNLQSATS ATNQTLTDRA SRSENARERA KQLLQRASKL TVDTNAKLKD
LNDLQTVYLN KNQQLLRLQA EIGPLNKELN EHLIHIKERG SHYRQCYT
