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 23-MAY-2018, entry version 178. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT 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 RT alpha5 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 RT perlecan to heparin, sulfatides, alpha-dystroglycan and several RT extracellular matrix 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, RC Spleen, 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 RT 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 RT molecular basis of alpha-dystroglycan binding to laminins, perlecan, RT and agrin."; RL Mol. Cell 4:783-792(1999). CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin CC is thought to mediate the attachment, migration and organization CC of cells into tissues during embryonic development by interacting CC with other extracellular matrix components. CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three CC different polypeptide chains (alpha, beta, gamma), which are bound CC to each other by disulfide bonds into a cross-shaped molecule CC comprising one long and three short arms with globules at each CC end. Alpha-2 is a subunit of laminin-2 (laminin-211 or merosin), CC laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). CC Interacts with FBLN1, FBLN2 and NID2. CC {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 CC with 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 CC dystrophy (dy2J). CC -!- SEQUENCE CAUTION: CC Sequence=AAC52165.1; Type=Frameshift; Positions=3094; 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 UniGene; Mm.256087; -. 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 ProteinModelPortal; Q60675; -. DR SMR; Q60675; -. DR BioGrid; 201097; 1. DR CORUM; Q60675; -. DR IntAct; Q60675; 1. DR STRING; 10090.ENSMUSP00000090304; -. DR iPTMnet; Q60675; -. DR PhosphoSitePlus; Q60675; -. DR MaxQB; Q60675; -. DR PaxDb; Q60675; -. DR PeptideAtlas; Q60675; -. DR PRIDE; Q60675; -. 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 eggNOG; ENOG410KCXA; Eukaryota. DR eggNOG; COG0419; LUCA. DR GeneTree; ENSGT00780000121851; -. DR HOGENOM; HOG000293201; -. DR HOVERGEN; HBG052298; -. DR InParanoid; Q60675; -. DR KO; K05637; -. DR OMA; TYKPEIK; -. DR OrthoDB; EOG091G005L; -. DR TreeFam; TF335359; -. DR Reactome; R-MMU-3000157; Laminin interactions. DR Reactome; R-MMU-8874081; MET activates PTK2 signaling. DR EvolutionaryTrace; Q60675; -. DR PRO; PR:Q60675; -. DR Proteomes; UP000000589; Chromosome 10. DR Bgee; ENSMUSG00000019899; -. DR CleanEx; MM_LAMA2; -. DR ExpressionAtlas; Q60675; baseline and differential. DR Genevisible; Q60675; MM. DR GO; GO:0005605; C:basal lamina; IDA:MGI. DR GO; GO:0005604; C:basement membrane; IDA:MGI. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0031012; C:extracellular matrix; ISO:MGI. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0042383; C:sarcolemma; IDA:MGI. DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro. DR GO; GO:0007411; P:axon guidance; IGI:MGI. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:MGI. DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro. 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 Gene3D; 2.60.120.1490; -; 1. 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; IPR002049; Laminin_EGF. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR000034; Laminin_IV. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR038684; Laminin_N_sf. 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; 3. 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 Complete proteome; Direct protein sequencing; Disulfide bond; KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:11829758}. FT CHAIN 20 3118 Laminin subunit alpha-2. FT /FTId=PRO_0000017057. FT DOMAIN 31 282 Laminin N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00466}. FT DOMAIN 283 339 Laminin EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 340 409 Laminin EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 410 464 Laminin EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 465 513 Laminin EGF-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 514 523 Laminin EGF-like 5; first part. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 527 719 Laminin IV type A 1. FT {ECO:0000255|PROSITE-ProRule:PRU00458}. FT DOMAIN 720 752 Laminin EGF-like 5; second part. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 753 802 Laminin EGF-like 6. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 803 860 Laminin EGF-like 7. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 861 913 Laminin EGF-like 8. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 914 962 Laminin EGF-like 9. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 963 1009 Laminin EGF-like 10. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1010 1055 Laminin EGF-like 11. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1056 1101 Laminin EGF-like 12. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1102 1161 Laminin EGF-like 13. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1162 1171 Laminin EGF-like 14; first part. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1172 1375 Laminin IV type A 2. FT {ECO:0000255|PROSITE-ProRule:PRU00458}. FT DOMAIN 1376 1415 Laminin EGF-like 14; second part. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1416 1464 Laminin EGF-like 15. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1465 1522 Laminin EGF-like 16. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1523 1569 Laminin EGF-like 17. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 2141 2324 Laminin G-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 2336 2517 Laminin G-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 2522 2706 Laminin G-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 2759 2930 Laminin G-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 2929 3115 Laminin G-like 5. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT REGION 1570 2140 Domain II and I. FT COILED 1662 1863 {ECO:0000255}. FT COILED 1923 2146 {ECO:0000255}. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 85 85 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 299 299 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 359 359 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 376 376 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 466 466 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 742 742 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 919 919 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1031 1031 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1057 1057 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1593 1593 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1610 1610 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1696 1696 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1806 1806 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1897 1897 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1912 1912 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1916 1916 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2013 2013 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2024 2024 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2041 2041 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2122 2122 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2236 2236 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2356 2356 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2431 2431 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2474 2474 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2547 2547 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2554 2554 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2644 2644 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2889 2889 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 283 292 {ECO:0000250}. FT DISULFID 285 303 {ECO:0000250}. FT DISULFID 305 314 {ECO:0000250}. FT DISULFID 317 337 {ECO:0000250}. FT DISULFID 340 349 {ECO:0000250}. FT DISULFID 342 374 {ECO:0000250}. FT DISULFID 377 386 {ECO:0000250}. FT DISULFID 389 407 {ECO:0000250}. FT DISULFID 410 422 {ECO:0000250}. FT DISULFID 412 438 {ECO:0000250}. FT DISULFID 440 449 {ECO:0000250}. FT DISULFID 452 462 {ECO:0000250}. FT DISULFID 465 478 {ECO:0000250}. FT DISULFID 467 482 {ECO:0000250}. FT DISULFID 484 493 {ECO:0000250}. FT DISULFID 496 511 {ECO:0000250}. FT DISULFID 753 762 {ECO:0000250}. FT DISULFID 755 769 {ECO:0000250}. FT DISULFID 772 781 {ECO:0000250}. FT DISULFID 784 800 {ECO:0000250}. FT DISULFID 803 818 {ECO:0000250}. FT DISULFID 805 828 {ECO:0000250}. FT DISULFID 831 840 {ECO:0000250}. FT DISULFID 843 858 {ECO:0000250}. FT DISULFID 861 875 {ECO:0000250}. FT DISULFID 863 882 {ECO:0000250}. FT DISULFID 885 894 {ECO:0000250}. FT DISULFID 897 911 {ECO:0000250}. FT DISULFID 914 926 {ECO:0000250}. FT DISULFID 916 933 {ECO:0000250}. FT DISULFID 935 944 {ECO:0000250}. FT DISULFID 947 960 {ECO:0000250}. FT DISULFID 963 975 {ECO:0000250}. FT DISULFID 965 981 {ECO:0000250}. FT DISULFID 983 992 {ECO:0000250}. FT DISULFID 995 1007 {ECO:0000250}. FT DISULFID 1010 1019 {ECO:0000250}. FT DISULFID 1012 1026 {ECO:0000250}. FT DISULFID 1028 1037 {ECO:0000250}. FT DISULFID 1040 1053 {ECO:0000250}. FT DISULFID 1056 1068 {ECO:0000250}. FT DISULFID 1058 1075 {ECO:0000250}. FT DISULFID 1077 1086 {ECO:0000250}. FT DISULFID 1089 1099 {ECO:0000250}. FT DISULFID 1102 1114 {ECO:0000250}. FT DISULFID 1104 1130 {ECO:0000250}. FT DISULFID 1132 1141 {ECO:0000250}. FT DISULFID 1144 1159 {ECO:0000250}. FT DISULFID 1378 1387 {ECO:0000250}. FT DISULFID 1416 1425 {ECO:0000250}. FT DISULFID 1418 1432 {ECO:0000250}. FT DISULFID 1435 1444 {ECO:0000250}. FT DISULFID 1447 1462 {ECO:0000250}. FT DISULFID 1465 1480 {ECO:0000250}. FT DISULFID 1467 1490 {ECO:0000250}. FT DISULFID 1493 1502 {ECO:0000250}. FT DISULFID 1505 1520 {ECO:0000250}. FT DISULFID 1523 1535 {ECO:0000250}. FT DISULFID 1525 1542 {ECO:0000250}. FT DISULFID 1544 1553 {ECO:0000250}. FT DISULFID 1556 1567 {ECO:0000250}. FT DISULFID 1570 1570 Interchain. {ECO:0000305}. FT DISULFID 1574 1574 Interchain. {ECO:0000305}. FT DISULFID 2298 2324 {ECO:0000250}. FT DISULFID 2491 2517 {ECO:0000250}. FT DISULFID 2679 2706 {ECO:0000250}. FT DISULFID 2905 2930 {ECO:0000250}. FT DISULFID 3083 3115 {ECO:0000250}. FT CONFLICT 616 616 I -> L (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 646 646 I -> V (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 678 682 ERVLM -> GEILI (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 704 704 A -> P (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 853 853 I -> V (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 908 908 A -> T (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 917 917 N -> D (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 925 925 I -> D (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 1694 1694 Q -> K (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 1840 1840 R -> Q (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2205 2205 D -> I (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2214 2215 EY -> GF (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2523 2523 Y -> N (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2642 2642 M -> I (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2729 2729 P -> S (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2739 2739 A -> V (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2773 2773 A -> V (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2802 2802 A -> G (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2810 2810 A -> G (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2820 2820 Y -> F (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2829 2831 DTS -> STR (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2878 2878 V -> G (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2946 2946 A -> G (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2953 2953 K -> I (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 2976 2976 V -> I (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 3011 3011 G -> E (in Ref. 1; AAC52165). FT {ECO:0000305}. FT CONFLICT 3022 3022 H -> Y (in Ref. 1; AAC52165). FT {ECO:0000305}. FT STRAND 2151 2154 {ECO:0000244|PDB:2WJS}. FT STRAND 2163 2173 {ECO:0000244|PDB:2WJS}. FT STRAND 2177 2183 {ECO:0000244|PDB:2WJS}. FT STRAND 2190 2196 {ECO:0000244|PDB:2WJS}. FT STRAND 2199 2208 {ECO:0000244|PDB:2WJS}. FT STRAND 2210 2214 {ECO:0000244|PDB:2WJS}. FT STRAND 2226 2233 {ECO:0000244|PDB:2WJS}. FT STRAND 2236 2246 {ECO:0000244|PDB:2WJS}. FT TURN 2247 2250 {ECO:0000244|PDB:2WJS}. FT STRAND 2256 2259 {ECO:0000244|PDB:2WJS}. FT STRAND 2274 2279 {ECO:0000244|PDB:2WJS}. FT STRAND 2297 2299 {ECO:0000244|PDB:2WJS}. FT STRAND 2303 2308 {ECO:0000244|PDB:2WJS}. FT STRAND 2316 2319 {ECO:0000244|PDB:2WJS}. FT STRAND 2337 2348 {ECO:0000244|PDB:2WJS}. FT STRAND 2357 2367 {ECO:0000244|PDB:2WJS}. FT STRAND 2369 2377 {ECO:0000244|PDB:2WJS}. FT STRAND 2381 2390 {ECO:0000244|PDB:2WJS}. FT STRAND 2393 2399 {ECO:0000244|PDB:2WJS}. FT STRAND 2404 2408 {ECO:0000244|PDB:2WJS}. FT STRAND 2415 2417 {ECO:0000244|PDB:2WJS}. FT STRAND 2419 2426 {ECO:0000244|PDB:2WJS}. FT STRAND 2429 2436 {ECO:0000244|PDB:2WJS}. FT TURN 2437 2439 {ECO:0000244|PDB:2WJS}. FT STRAND 2442 2448 {ECO:0000244|PDB:2WJS}. FT STRAND 2463 2467 {ECO:0000244|PDB:2WJS}. FT STRAND 2489 2497 {ECO:0000244|PDB:2WJS}. FT STRAND 2500 2502 {ECO:0000244|PDB:2WJS}. FT HELIX 2504 2506 {ECO:0000244|PDB:2WJS}. FT STRAND 2511 2516 {ECO:0000244|PDB:2WJS}. FT STRAND 2524 2526 {ECO:0000244|PDB:2WJS}. FT STRAND 2528 2530 {ECO:0000244|PDB:2WJS}. FT STRAND 2532 2535 {ECO:0000244|PDB:2WJS}. FT STRAND 2544 2553 {ECO:0000244|PDB:2WJS}. FT STRAND 2555 2562 {ECO:0000244|PDB:2WJS}. FT STRAND 2581 2587 {ECO:0000244|PDB:2WJS}. FT STRAND 2590 2596 {ECO:0000244|PDB:2WJS}. FT STRAND 2603 2607 {ECO:0000244|PDB:2WJS}. FT STRAND 2614 2618 {ECO:0000244|PDB:2WJS}. FT STRAND 2620 2626 {ECO:0000244|PDB:2WJS}. FT STRAND 2628 2638 {ECO:0000244|PDB:2WJS}. FT STRAND 2641 2644 {ECO:0000244|PDB:2WJS}. FT STRAND 2656 2659 {ECO:0000244|PDB:2WJS}. FT STRAND 2678 2685 {ECO:0000244|PDB:2WJS}. FT STRAND 2696 2700 {ECO:0000244|PDB:2WJS}. FT STRAND 2760 2762 {ECO:0000244|PDB:1OKQ}. FT STRAND 2769 2773 {ECO:0000244|PDB:5IK4}. FT HELIX 2776 2779 {ECO:0000244|PDB:5IK4}. FT STRAND 2780 2791 {ECO:0000244|PDB:5IK4}. FT STRAND 2796 2802 {ECO:0000244|PDB:5IK4}. FT STRAND 2806 2815 {ECO:0000244|PDB:5IK4}. FT STRAND 2818 2827 {ECO:0000244|PDB:5IK4}. FT STRAND 2829 2833 {ECO:0000244|PDB:5IK4}. FT STRAND 2840 2842 {ECO:0000244|PDB:5IK4}. FT STRAND 2844 2851 {ECO:0000244|PDB:5IK4}. FT STRAND 2854 2859 {ECO:0000244|PDB:5IK4}. FT STRAND 2862 2867 {ECO:0000244|PDB:5IK4}. FT STRAND 2869 2871 {ECO:0000244|PDB:5IK4}. FT STRAND 2879 2885 {ECO:0000244|PDB:5IK4}. FT STRAND 2903 2914 {ECO:0000244|PDB:5IK4}. FT STRAND 2922 2926 {ECO:0000244|PDB:5IK4}. FT STRAND 2931 2952 {ECO:0000244|PDB:5IK4}. FT STRAND 2955 2969 {ECO:0000244|PDB:5IK4}. FT STRAND 2971 2977 {ECO:0000244|PDB:5IK4}. FT STRAND 2979 2981 {ECO:0000244|PDB:5IK4}. FT STRAND 2983 2989 {ECO:0000244|PDB:5IK4}. FT STRAND 2992 3001 {ECO:0000244|PDB:5IK4}. FT STRAND 3003 3008 {ECO:0000244|PDB:5IK4}. FT HELIX 3015 3017 {ECO:0000244|PDB:1QU0}. FT STRAND 3018 3020 {ECO:0000244|PDB:5IK4}. FT STRAND 3022 3029 {ECO:0000244|PDB:5IK4}. FT STRAND 3032 3037 {ECO:0000244|PDB:5IK4}. FT STRAND 3040 3045 {ECO:0000244|PDB:5IK4}. FT STRAND 3058 3063 {ECO:0000244|PDB:5IK4}. FT STRAND 3081 3094 {ECO:0000244|PDB:5IK4}. FT HELIX 3101 3103 {ECO:0000244|PDB:5IK4}. FT STRAND 3105 3116 {ECO:0000244|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 //