LAMA2_MOUSE
ID LAMA2_MOUSE Reviewed; 3118 AA.
AC Q60675; F8VQ43; Q05003; Q64061;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Laminin subunit alpha-2;
DE AltName: Full=Laminin M chain;
DE AltName: Full=Laminin-12 subunit alpha;
DE AltName: Full=Laminin-2 subunit alpha;
DE AltName: Full=Laminin-4 subunit alpha;
DE AltName: Full=Merosin heavy chain;
DE Flags: Precursor;
GN Name=Lama2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N; TISSUE=Embryo, and Heart;
RX PubMed=7795883; DOI=10.1016/0945-053x(95)90002-0;
RA Bernier S.M., Utani A., Sugiyama S., Doi T., Polistina C., Yamada Y.;
RT "Cloning and expression of laminin alpha 2 chain (M-chain) in the mouse.";
RL Matrix Biol. 14:447-455(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2162-2279.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=8345183;
RA Chang A.C., Wadsworth S., Coligan J.E.;
RT "Expression of merosin in the thymus and its interaction with thymocytes.";
RL J. Immunol. 151:1789-1801(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-281.
RX PubMed=7874173; DOI=10.1038/ng1194-297;
RA Xu H., Wu X.R., Wewer U.M., Engvall E.;
RT "Murine muscular dystrophy caused by a mutation in the laminin alpha 2
RT (Lama2) gene.";
RL Nat. Genet. 8:297-302(1994).
RN [5]
RP PROTEIN SEQUENCE OF 20-25.
RX PubMed=11829758; DOI=10.1042/0264-6021:3620213;
RA Garbe J.H., Gohring W., Mann K., Timpl R., Sasaki T.;
RT "Complete sequence, recombinant analysis and binding to laminins and
RT sulphated ligands of the N-terminal domains of laminin alpha3B and alpha5
RT chains.";
RL Biochem. J. 362:213-221(2002).
RN [6]
RP INTERACTION WITH FBLN1; FBLN2 AND NID2.
RX PubMed=10022829; DOI=10.1093/emboj/18.4.863;
RA Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.;
RT "Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan
RT to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix
RT proteins.";
RL EMBO J. 18:863-870(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2932-3106.
RX PubMed=10619025; DOI=10.1016/s1097-2765(00)80388-3;
RA Hohenester E., Tisi D., Talts J.F., Timpl R.;
RT "The crystal structure of a laminin G-like module reveals the molecular
RT basis of alpha-dystroglycan binding to laminins, perlecan, and agrin.";
RL Mol. Cell 4:783-792(1999).
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. Alpha-2 is a
CC subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221
CC or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2
CC and NID2. {ECO:0000269|PubMed:10022829}.
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, IV and G are globular.
CC -!- DISEASE: Note=Defects in Lama2 are a cause of murine muscular dystrophy
CC (dy2J).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52165.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U12147; AAC52165.1; ALT_FRAME; mRNA.
DR EMBL; AC101709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X69869; CAA49502.1; -; mRNA.
DR EMBL; S75315; AAB33573.1; -; mRNA.
DR CCDS; CCDS48526.1; -.
DR PIR; I49077; S53868.
DR RefSeq; NP_032507.2; NM_008481.2.
DR PDB; 1DYK; X-ray; 2.00 A; A=2730-3118.
DR PDB; 1OKQ; X-ray; 2.80 A; A=2730-3118.
DR PDB; 1QU0; X-ray; 2.35 A; A/B/C/D=2932-3118.
DR PDB; 2WJS; X-ray; 2.80 A; A=2136-2749.
DR PDB; 5IK4; X-ray; 1.27 A; A=2730-3118.
DR PDB; 5IK5; X-ray; 1.39 A; A=2730-3118.
DR PDB; 5IK7; X-ray; 2.00 A; A/B=2742-3118.
DR PDB; 5IK8; X-ray; 2.00 A; A/B=2742-3118.
DR PDBsum; 1DYK; -.
DR PDBsum; 1OKQ; -.
DR PDBsum; 1QU0; -.
DR PDBsum; 2WJS; -.
DR PDBsum; 5IK4; -.
DR PDBsum; 5IK5; -.
DR PDBsum; 5IK7; -.
DR PDBsum; 5IK8; -.
DR SMR; Q60675; -.
DR BioGRID; 201097; 3.
DR ComplexPortal; CPX-3009; Laminin-211 complex.
DR ComplexPortal; CPX-3011; Laminin-221 complex.
DR ComplexPortal; CPX-3018; Laminin-213 complex.
DR CORUM; Q60675; -.
DR IntAct; Q60675; 1.
DR STRING; 10090.ENSMUSP00000090304; -.
DR UniLectin; Q60675; -.
DR GlyConnect; 2456; 11 N-Linked glycans (7 sites).
DR GlyGen; Q60675; 29 sites, 11 N-linked glycans (7 sites).
DR iPTMnet; Q60675; -.
DR PhosphoSitePlus; Q60675; -.
DR CPTAC; non-CPTAC-3655; -.
DR CPTAC; non-CPTAC-3835; -.
DR MaxQB; Q60675; -.
DR PaxDb; Q60675; -.
DR PeptideAtlas; Q60675; -.
DR PRIDE; Q60675; -.
DR ProteomicsDB; 265034; -.
DR ABCD; Q60675; 1 sequenced antibody.
DR Antibodypedia; 763; 214 antibodies from 33 providers.
DR DNASU; 16773; -.
DR Ensembl; ENSMUST00000092639; ENSMUSP00000090304; ENSMUSG00000019899.
DR GeneID; 16773; -.
DR KEGG; mmu:16773; -.
DR UCSC; uc007esf.2; mouse.
DR CTD; 3908; -.
DR MGI; MGI:99912; Lama2.
DR VEuPathDB; HostDB:ENSMUSG00000019899; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000155362; -.
DR HOGENOM; CLU_000301_0_0_1; -.
DR InParanoid; Q60675; -.
DR OMA; KDYRDDA; -.
DR OrthoDB; 128982at2759; -.
DR PhylomeDB; Q60675; -.
DR TreeFam; TF335359; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 16773; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Lama2; mouse.
DR EvolutionaryTrace; Q60675; -.
DR PRO; PR:Q60675; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q60675; protein.
DR Bgee; ENSMUSG00000019899; Expressed in sciatic nerve and 186 other tissues.
DR ExpressionAtlas; Q60675; baseline and differential.
DR Genevisible; Q60675; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IC:ComplexPortal.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:MGI.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC:ComplexPortal.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 16.
DR CDD; cd00110; LamG; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR009254; Laminin_aI.
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; 2.
DR Pfam; PF00053; Laminin_EGF; 16.
DR Pfam; PF00054; Laminin_G_1; 4.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00180; EGF_Lam; 16.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; SSF49899; 5.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00022; EGF_1; 11.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS01248; EGF_LAM_1; 14.
DR PROSITE; PS50027; EGF_LAM_2; 16.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:11829758"
FT CHAIN 20..3118
FT /note="Laminin subunit alpha-2"
FT /id="PRO_0000017057"
FT DOMAIN 31..282
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 283..339
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 340..409
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 410..464
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 465..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 527..719
FT /note="Laminin IV type A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 720..752
FT /note="Laminin EGF-like 5; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 753..802
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 803..860
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 861..913
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 914..962
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 963..1009
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1010..1055
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1056..1101
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1102..1161
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1162..1171
FT /note="Laminin EGF-like 14; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1172..1375
FT /note="Laminin IV type A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 1376..1415
FT /note="Laminin EGF-like 14; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1416..1464
FT /note="Laminin EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1465..1522
FT /note="Laminin EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1523..1569
FT /note="Laminin EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2141..2324
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2336..2517
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2522..2706
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2759..2930
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2929..3115
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1570..2140
FT /note="Domain II and I"
FT COILED 1662..1863
FT /evidence="ECO:0000255"
FT COILED 1923..2146
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
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 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2013
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2041
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 283..292
FT /evidence="ECO:0000250"
FT DISULFID 285..303
FT /evidence="ECO:0000250"
FT DISULFID 305..314
FT /evidence="ECO:0000250"
FT DISULFID 317..337
FT /evidence="ECO:0000250"
FT DISULFID 340..349
FT /evidence="ECO:0000250"
FT DISULFID 342..374
FT /evidence="ECO:0000250"
FT DISULFID 377..386
FT /evidence="ECO:0000250"
FT DISULFID 389..407
FT /evidence="ECO:0000250"
FT DISULFID 410..422
FT /evidence="ECO:0000250"
FT DISULFID 412..438
FT /evidence="ECO:0000250"
FT DISULFID 440..449
FT /evidence="ECO:0000250"
FT DISULFID 452..462
FT /evidence="ECO:0000250"
FT DISULFID 465..478
FT /evidence="ECO:0000250"
FT DISULFID 467..482
FT /evidence="ECO:0000250"
FT DISULFID 484..493
FT /evidence="ECO:0000250"
FT DISULFID 496..511
FT /evidence="ECO:0000250"
FT DISULFID 753..762
FT /evidence="ECO:0000250"
FT DISULFID 755..769
FT /evidence="ECO:0000250"
FT DISULFID 772..781
FT /evidence="ECO:0000250"
FT DISULFID 784..800
FT /evidence="ECO:0000250"
FT DISULFID 803..818
FT /evidence="ECO:0000250"
FT DISULFID 805..828
FT /evidence="ECO:0000250"
FT DISULFID 831..840
FT /evidence="ECO:0000250"
FT DISULFID 843..858
FT /evidence="ECO:0000250"
FT DISULFID 861..875
FT /evidence="ECO:0000250"
FT DISULFID 863..882
FT /evidence="ECO:0000250"
FT DISULFID 885..894
FT /evidence="ECO:0000250"
FT DISULFID 897..911
FT /evidence="ECO:0000250"
FT DISULFID 914..926
FT /evidence="ECO:0000250"
FT DISULFID 916..933
FT /evidence="ECO:0000250"
FT DISULFID 935..944
FT /evidence="ECO:0000250"
FT DISULFID 947..960
FT /evidence="ECO:0000250"
FT DISULFID 963..975
FT /evidence="ECO:0000250"
FT DISULFID 965..981
FT /evidence="ECO:0000250"
FT DISULFID 983..992
FT /evidence="ECO:0000250"
FT DISULFID 995..1007
FT /evidence="ECO:0000250"
FT DISULFID 1010..1019
FT /evidence="ECO:0000250"
FT DISULFID 1012..1026
FT /evidence="ECO:0000250"
FT DISULFID 1028..1037
FT /evidence="ECO:0000250"
FT DISULFID 1040..1053
FT /evidence="ECO:0000250"
FT DISULFID 1056..1068
FT /evidence="ECO:0000250"
FT DISULFID 1058..1075
FT /evidence="ECO:0000250"
FT DISULFID 1077..1086
FT /evidence="ECO:0000250"
FT DISULFID 1089..1099
FT /evidence="ECO:0000250"
FT DISULFID 1102..1114
FT /evidence="ECO:0000250"
FT DISULFID 1104..1130
FT /evidence="ECO:0000250"
FT DISULFID 1132..1141
FT /evidence="ECO:0000250"
FT DISULFID 1144..1159
FT /evidence="ECO:0000250"
FT DISULFID 1378..1387
FT /evidence="ECO:0000250"
FT DISULFID 1416..1425
FT /evidence="ECO:0000250"
FT DISULFID 1418..1432
FT /evidence="ECO:0000250"
FT DISULFID 1435..1444
FT /evidence="ECO:0000250"
FT DISULFID 1447..1462
FT /evidence="ECO:0000250"
FT DISULFID 1465..1480
FT /evidence="ECO:0000250"
FT DISULFID 1467..1490
FT /evidence="ECO:0000250"
FT DISULFID 1493..1502
FT /evidence="ECO:0000250"
FT DISULFID 1505..1520
FT /evidence="ECO:0000250"
FT DISULFID 1523..1535
FT /evidence="ECO:0000250"
FT DISULFID 1525..1542
FT /evidence="ECO:0000250"
FT DISULFID 1544..1553
FT /evidence="ECO:0000250"
FT DISULFID 1556..1567
FT /evidence="ECO:0000250"
FT DISULFID 1570
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1574
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2298..2324
FT /evidence="ECO:0000250"
FT DISULFID 2491..2517
FT /evidence="ECO:0000250"
FT DISULFID 2679..2706
FT /evidence="ECO:0000250"
FT DISULFID 2905..2930
FT /evidence="ECO:0000250"
FT DISULFID 3083..3115
FT /evidence="ECO:0000250"
FT CONFLICT 616
FT /note="I -> L (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="I -> V (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 678..682
FT /note="ERVLM -> GEILI (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="A -> P (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="I -> V (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="A -> T (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="N -> D (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 925
FT /note="I -> D (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1694
FT /note="Q -> K (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1840
FT /note="R -> Q (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2205
FT /note="D -> I (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2214..2215
FT /note="EY -> GF (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2523
FT /note="Y -> N (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2642
FT /note="M -> I (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2729
FT /note="P -> S (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2739
FT /note="A -> V (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2773
FT /note="A -> V (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2802
FT /note="A -> G (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2810
FT /note="A -> G (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2820
FT /note="Y -> F (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2829..2831
FT /note="DTS -> STR (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2878
FT /note="V -> G (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2946
FT /note="A -> G (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2953
FT /note="K -> I (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 2976
FT /note="V -> I (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 3011
FT /note="G -> E (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT CONFLICT 3022
FT /note="H -> Y (in Ref. 1; AAC52165)"
FT /evidence="ECO:0000305"
FT STRAND 2151..2154
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2163..2173
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2177..2183
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2190..2196
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2199..2208
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2210..2214
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2226..2233
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2236..2246
FT /evidence="ECO:0007829|PDB:2WJS"
FT TURN 2247..2250
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2256..2259
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2274..2279
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2297..2299
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2303..2308
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2316..2319
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2337..2348
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2357..2367
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2369..2377
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2381..2390
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2393..2399
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2404..2408
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2415..2417
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2419..2426
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2429..2436
FT /evidence="ECO:0007829|PDB:2WJS"
FT TURN 2437..2439
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2442..2448
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2463..2467
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2489..2497
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2500..2502
FT /evidence="ECO:0007829|PDB:2WJS"
FT HELIX 2504..2506
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2511..2516
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2524..2526
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2528..2530
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2532..2535
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2544..2553
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2555..2562
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2581..2587
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2590..2596
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2603..2607
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2614..2618
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2620..2626
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2628..2638
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2641..2644
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2656..2659
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2678..2685
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2696..2700
FT /evidence="ECO:0007829|PDB:2WJS"
FT STRAND 2760..2762
FT /evidence="ECO:0007829|PDB:1OKQ"
FT STRAND 2769..2773
FT /evidence="ECO:0007829|PDB:5IK4"
FT HELIX 2776..2779
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2780..2791
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2796..2802
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2806..2815
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2818..2827
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2829..2833
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2840..2842
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2844..2851
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2854..2859
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2862..2867
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2869..2871
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2879..2885
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2903..2914
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2922..2926
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2931..2952
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2955..2969
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2971..2977
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2979..2981
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2983..2989
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 2992..3001
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 3003..3008
FT /evidence="ECO:0007829|PDB:5IK4"
FT HELIX 3015..3017
FT /evidence="ECO:0007829|PDB:1QU0"
FT STRAND 3018..3020
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 3022..3029
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 3032..3037
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 3040..3045
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 3058..3063
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 3081..3094
FT /evidence="ECO:0007829|PDB:5IK4"
FT HELIX 3101..3103
FT /evidence="ECO:0007829|PDB:5IK4"
FT STRAND 3105..3116
FT /evidence="ECO:0007829|PDB:5IK4"
SQ SEQUENCE 3118 AA; 343815 MW; CCD31C71B1E0DFD4 CRC64;
MPAATAGILL LLLLGTLEGS QTQRRQSQAH QQRGLFPAVL NLASNALITT NATCGEKGPE
MYCKLVEHVP GQPVRNPQCR ICNQNSSNPY QRHPITNAID GKNTWWQSPS IKNGVEYHYV
TITLDLQQVF QIAYVIVKAA NSPRPGNWIL ERSLDDVEYK PWQYHAVTDT ECLTLYNIYP
RTGPPSYAKD DEVICTSFYS KIHPLENGEI HISLINGRPS ADDPSPELLE FTSARYIRLR
FQRIRTLNAD LMMFAHKDPR EIDPIVTRRY YYSVKDISVG GMCICYGHAR ACPLDPATNK
SRCECEHNTC GESCDRCCPG FHQKPWRAGT FLTKSECEAC NCHGKAEECY YDETVASRNL
SLNIHGKYIG GGVCINCTHN TAGINCETCV DGFFRPKGVS PNYPRPCQPC HCDPTGSLSE
VCVKDEKYAQ RGLKPGSCHC KTGFGGVNCD RCVRGYHGYP DCQPCNCSGL GSTNEDPCVG
PCSCKENVEG EDCSRCKSGF FNLQEDNQKG CEECFCSGVS NRCQSSYWTY GNIQDMRGWY
LTDLSGRIRM APQLDNPDSP QQISISNSEA RKSLLDGYYW SAPPPYLGNR LPAVGGQLSF
TISYDLEEEE DDTEKILQLM IIFEGNDLRI STAYKEVYLE PSEEHIEEVS LKEEAFTIHG
TNLPVTRKDF MIVLTNLERV LMQITYNLGM DAIFRLSSVN LESAVPYPTD RRIATDVEVC
QCPPGYSGSS CETCWPRHRR VNGTIFGGIC EPCQCFAHAE ACDDITGECL NCKDHTGGPY
CNECLPGFYG DPTRGSPEDC QPCACPLNIP SNNFSPTCHL DRSLGLICDE CPIGYTGPRC
ERCAEGYFGQ PSIPGGSCQP CQCNDNLDYS IPGSCDSLSG SCLICKPGTT GRYCELCADG
YFGDAVNAKN CQPCRCNING SFSEICHTRT GQCECRPNVQ GRHCDECKPE TFGLQLGRGC
LPCNCNSFGS KSFDCEASGQ CWCQPGVAGK KCDRCAHGYF NFQEGGCIAC DCSHLGNNCD
PKTGQCICPP NTTGEKCSEC LPNTWGHSIV TGCKVCNCST VGSLASQCNV NTGQCSCHPK
FSGMKCSECS RGHWNYPLCT LCDCFLPGTD ATTCDLETRK CSCSDQTGQC SCKVNVEGVH
CDRCRPGKFG LDAKNPLGCS SCYCFGVTSQ CSEAKGLIRT WVTLSDEQTI LPLVDEALQH
TTTKGIAFQK PEIVAKMDEV RQELHLEPFY WKLPQQFEGK KLMAYGGKLK YAIYFEARDE
TGFATYKPQV IIRGGTPTHA RIITRHMAAP LIGQLTRHEI EMTEKEWKYY GDDPRISRTV
TREDFLDILY DIHYILIKAT YGNVVRQSRI SEISMEVAEP GHVLAGSPPA HLIERCDCPP
GYSGLSCETC APGFYRLRSE PGGRTPGPTL GTCVPCQCNG HSSQCDPETS VCQNCQHHTA
GDFCERCALG YYGIVRGLPN DCQPCACPLI SPSNNFSPSC VLEGLEDYRC TACPRGYEGQ
YCERCAPGYT GSPSSPGGSC QECECDPYGS LPVPCDRVTG LCTCRPGATG RKCDGCEHWH
AREGAECVFC GDECTGLLLG DLARLEQMTM NINLTGPLPA PYKILYGLEN TTQELKHLLS
PQRAPERLIQ LAEGNVNTLV METNELLTRA TKVTADGEQT GQDAERTNSR AESLEEFIKG
LVQDAEAINE KAVQLNETLG NQDKTAERNL EELQKEIDRM LKELRSKDLQ TQKEVAEDEL
VAAEGLLKRV NKLFGEPRAQ NEDMEKDLQQ KLAEYKNKLD DAWDLLREAT DKTRDANRLS
AANQKNMTIL ETKKEAIEGS KRQIENTLKE GNDILDEANR LLGEINSVID YVDDIKTKLP
PMSEELSDKI DDLAQEIKDR RLAEKVFQAE SHAAQLNDSS AVLDGILDEA KNISFNATAA
FRAYSNIKDY IDEAEKVARE AKELAQGATK LATSPQGLLK EDAKGSLQKS FRILNEAKKL
ANDVKGNHND LNDLKTRLET ADLRNSGLLG ALNDTMDKLS AITNDTAAKL QAVKEKAREA
NDTAKAVLAQ VKDLHQNLDG LKQNYNKLAD SVAKTNAVVK DPSKNKIIAD AGTSVRNLEQ
EADRLIDKLK PIKELEDNLK KNISEIKELI NQARKQANSI KVSVSSGGDC VRTYRPEIKK
GSYNNIVVHV KTAVADNLLF YLGSAKFIDF LAIEMRKGKV SFLWDVGSGV GRVEYPDLTI
DDSYWYRIEA SRTGRNGSIS VRALDGPKAS MVPSTYHSVS PPGYTILDVD ANAMLFVGGL
TGKIKKADAV RVITFTGCMG ETYFDNKPIG LWNFREKEGD CKGCTVSPQV EDSEGTIQFD
GEGYALVSRP IRWYPNISTV MFKFRTFSSS ALLMYLATRD LKDFMSVELS DGHVKVSYDL
GSGMTSVVSN QNHNDGKWKA FTLSRIQKQA NISIVDIDSN QEENVATSSS GNNFGLDLKA
DDKIYFGGLP TLRNLSMKAR PEVNVKKYSG CLKDIEISRT PYNILSSPDY VGVTKGCSLE
NVYTVSFPKP GFVELAAVSI DVGTEINLSF STRNESGIIL LGSGGTLTPP RRKRRQTTQA
YYAIFLNKGR LEVHLSSGTR TMRKIVIKPE PNLFHDGREH SVHVERTRGI FTVQIDEDRR
HMQNLTEEQP IEVKKLFVGG APPEFQPSPL RNIPAFQGCV WNLVINSIPM DFAQPIAFKN
ADIGRCTYQK PREDESEAVP AEVIVQPQPV PTPAFPFPAP TMVHGPCVAE SEPALLTGSK
QFGLSRNSHI AIAFDDTKVK NRLTIELEVR TEAESGLLFY MARINHADFA TVQLRNGFPY
FSYDLGSGDT STMIPTKIND GQWHKIKIVR VKQEGILYVD DASSQTISPK KADILDVVGI
LYVGGLPINY TTRRIGPVTY SLDGCVRNLH MEQAPVDLDQ PTSSFHVGTC FANAESGTYF
DGTGFAKAVG GFKVGLDLLV EFEFRTTRPT GVLLGVSSQK MDGMGIEMID EKLMFHVDNG
AGRFTAIYDA GIPGHMCNGQ WHKVTAKKIK NRLELVVDGN QVDAQSPNSA STSADTNDPV
FVGGFPGGLN QFGLTTNIRF RGCIRSLKLT KGTGKPLEVN FAKALELRGV QPVSCPTT
