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 24-JAN-2024, entry version 213. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q60675; 29 sites, 11 glycans. DR GlyGen; Q60675; 29 sites, 11 N-linked glycans (7 sites). DR iPTMnet; Q60675; -. DR PhosphoSitePlus; Q60675; -. DR SwissPalm; Q60675; -. DR CPTAC; non-CPTAC-3655; -. DR CPTAC; non-CPTAC-3835; -. DR MaxQB; Q60675; -. DR PaxDb; 10090-ENSMUSP00000090304; -. DR PeptideAtlas; Q60675; -. DR ProteomicsDB; 265034; -. DR Pumba; Q60675; -. DR ABCD; Q60675; 1 sequenced antibody. DR Antibodypedia; 763; 239 antibodies from 33 providers. DR DNASU; 16773; -. DR Ensembl; ENSMUST00000092639.12; ENSMUSP00000090304.6; ENSMUSG00000019899.18. DR GeneID; 16773; -. DR KEGG; mmu:16773; -. DR UCSC; uc007esf.2; mouse. DR AGR; MGI:99912; -. 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; SHSRINF; -. DR OrthoDB; 90222at2759; -. DR PhylomeDB; Q60675; -. DR TreeFam; TF335359; -. DR BioGRID-ORCS; 16773; 2 hits in 75 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 188 other cell types or 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:0043197; C:dendritic spine; ISO:MGI. 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; NAS: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; NAS:ComplexPortal. DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; NAS:ComplexPortal. DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal. DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:MGI. DR GO; GO:0110011; P:regulation of basement membrane organization; NAS: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:0014037; P:Schwann cell differentiation; IEA:Ensembl. DR GO; GO:0009888; P:tissue development; IBA:GO_Central. DR CDD; cd00055; EGF_Lam; 16. DR CDD; cd00110; LamG; 5. DR Gene3D; 2.60.120.200; -; 5. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 15. 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 PANTHER; PTHR10574:SF291; LAMININ SUBUNIT ALPHA-2; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00052; Laminin_B; 2. DR Pfam; PF00053; Laminin_EGF; 15. 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 PRINTS; PR00011; EGFLAMININ. 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; Concanavalin A-like lectins/glucanases; 5. DR SUPFAM; SSF57196; EGF/Laminin; 11. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 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 //