ID LAMC1_MOUSE Reviewed; 1607 AA. AC P02468; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 2. DT 24-JAN-2024, entry version 209. DE RecName: Full=Laminin subunit gamma-1; DE AltName: Full=Laminin B2 chain; DE AltName: Full=Laminin-1 subunit gamma; DE AltName: Full=Laminin-10 subunit gamma; DE AltName: Full=Laminin-11 subunit gamma; DE AltName: Full=Laminin-2 subunit gamma; DE AltName: Full=Laminin-3 subunit gamma; DE AltName: Full=Laminin-4 subunit gamma; DE AltName: Full=Laminin-6 subunit gamma; DE AltName: Full=Laminin-7 subunit gamma; DE AltName: Full=Laminin-8 subunit gamma; DE AltName: Full=Laminin-9 subunit gamma; DE AltName: Full=S-laminin subunit gamma; DE Short=S-LAM gamma; DE Flags: Precursor; GN Name=Lamc1; Synonyms=Lamb-2, Lamc-1; 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]. RX PubMed=3680290; DOI=10.1016/s0021-9258(18)45498-1; RA Sasaki M., Yamada Y.; RT "The laminin B2 chain has a multidomain structure homologous to the B1 RT chain."; RL J. Biol. Chem. 262:17111-17117(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3167041; DOI=10.1021/bi00414a038; RA Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.; RT "Primary structure of the mouse laminin B2 chain and comparison with RT laminin B1."; RL Biochemistry 27:5198-5204(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239. RX PubMed=2836421; DOI=10.1016/s0021-9258(18)68489-3; RA Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.; RT "The laminin B2 chain promoter contains unique repeat sequences and is RT active in transient transfection."; RL J. Biol. Chem. 263:8384-8389(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1607. RX PubMed=6209134; DOI=10.1002/j.1460-2075.1984.tb02140.x; RA Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.; RT "Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled- RT coil alpha-helix."; RL EMBO J. 3:2355-2362(1984). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-648; ASN-1105; ASN-1203; RP ASN-1221 AND ASN-1393. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 expression."; RL Cell 143:1174-1189(2010). RN [7] RP INTERACTION WITH SVEP1. RX PubMed=36792666; DOI=10.1038/s41467-023-36486-0; RA Elenbaas J.S., Pudupakkam U., Ashworth K.J., Kang C.J., Patel V., RA Santana K., Jung I.H., Lee P.C., Burks K.H., Amrute J.M., Mecham R.P., RA Halabi C.M., Alisio A., Di Paola J., Stitziel N.O.; RT "SVEP1 is an endogenous ligand for the orphan receptor PEAR1."; RL Nat. Commun. 14:850-850(2023). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932. RX PubMed=8648630; DOI=10.1006/jmbi.1996.0191; RA Stetefeld J., Mayer U., Timpl R., Huber R.; RT "Crystal structure of three consecutive laminin-type epidermal growth RT factor-like (LE) modules of laminin gamma1 chain harboring the nidogen RT binding site."; RL J. Mol. Biol. 257:644-657(1996). RN [9] RP STRUCTURE BY NMR OF 824-881. RX PubMed=8648631; DOI=10.1006/jmbi.1996.0192; RA Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R., RA Holak T.A.; RT "Structure of the nidogen binding LE module of the laminin gamma1 chain in RT solution."; RL J. Mol. Biol. 257:658-668(1996). 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. Gamma-1 is a CC subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin- CC 211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 CC (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), CC laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), CC laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 CC (laminin-521). Interacts with SVEP1 (PubMed:36792666). CC {ECO:0000269|PubMed:36792666}. CC -!- INTERACTION: CC P02468; P02469: Lamb1; NbExp=4; IntAct=EBI-7059830, EBI-6662997; CC P02468; P10493: Nid1; NbExp=5; IntAct=EBI-7059830, EBI-1032117; CC P02468; Q9JI33: Ntn4; NbExp=2; IntAct=EBI-7059830, EBI-15755373; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major component). CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with CC other laminin chains to form a coiled coil structure. CC -!- DOMAIN: Domains VI and IV are globular. 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; X05211; CAA28838.1; -; mRNA. DR EMBL; J03484; AAA39405.1; -; mRNA. DR EMBL; J02930; AAA39408.1; -; mRNA. DR EMBL; J03749; AAA39409.1; -; Genomic_DNA. DR CCDS; CCDS15370.1; -. DR PIR; A28469; MMMSB2. DR PIR; S55783; S55783. DR PDB; 1KLO; X-ray; 2.10 A; A=771-932. DR PDB; 1NPE; X-ray; 2.30 A; B=769-932. DR PDB; 1TLE; NMR; -; A=824-881. DR PDB; 4AQT; X-ray; 3.20 A; A=33-395. DR PDB; 5MC9; X-ray; 2.13 A; C=1548-1607. DR PDBsum; 1KLO; -. DR PDBsum; 1NPE; -. DR PDBsum; 1TLE; -. DR PDBsum; 4AQT; -. DR PDBsum; 5MC9; -. DR AlphaFoldDB; P02468; -. DR SMR; P02468; -. DR ComplexPortal; CPX-3008; Laminin-111 complex. DR ComplexPortal; CPX-3009; Laminin-211 complex. DR ComplexPortal; CPX-3010; Laminin-121 complex. DR ComplexPortal; CPX-3011; Laminin-221 complex. DR ComplexPortal; CPX-3013; Laminin-311 complex variant A. DR ComplexPortal; CPX-3014; Laminin-321 complex. DR ComplexPortal; CPX-3015; Laminin-411 complex. DR ComplexPortal; CPX-3016; Laminin-511 complex. DR ComplexPortal; CPX-3017; Laminin-521 complex. DR ComplexPortal; CPX-3031; Laminin-421 complex. DR ComplexPortal; CPX-3167; Laminin-311 complex variant B. DR DIP; DIP-41793N; -. DR IntAct; P02468; 11. DR MINT; P02468; -. DR STRING; 10090.ENSMUSP00000027752; -. DR GlyConnect; 2461; 22 N-Linked glycans (10 sites). DR GlyCosmos; P02468; 14 sites, 26 glycans. DR GlyGen; P02468; 16 sites, 21 N-linked glycans (10 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P02468; -. DR PhosphoSitePlus; P02468; -. DR SwissPalm; P02468; -. DR EPD; P02468; -. DR jPOST; P02468; -. DR MaxQB; P02468; -. DR PaxDb; 10090-ENSMUSP00000027752; -. DR PeptideAtlas; P02468; -. DR ProteomicsDB; 265036; -. DR Pumba; P02468; -. DR AGR; MGI:99914; -. DR MGI; MGI:99914; Lamc1. DR eggNOG; KOG1836; Eukaryota. DR InParanoid; P02468; -. DR PhylomeDB; P02468; -. DR ChiTaRS; Lamc1; mouse. DR EvolutionaryTrace; P02468; -. DR PRO; PR:P02468; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P02468; Protein. 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:0005606; C:laminin-1 complex; ISO:MGI. DR GO; GO:0043259; C:laminin-10 complex; IPI:MGI. 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:0043083; C:synaptic cleft; IDA:SynGO. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:HGNC-UCL. DR GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI. DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; ISS:HGNC-UCL. DR GO; GO:0016477; P:cell migration; ISS:HGNC-UCL. DR GO; GO:0006325; P:chromatin organization; IMP:MGI. DR GO; GO:0022617; P:extracellular matrix disassembly; ISS:HGNC-UCL. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0035315; P:hair cell differentiation; IMP:MGI. DR GO; GO:0071335; P:hair follicle cell proliferation; IMP:MGI. DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI. DR GO; GO:0031581; P:hemidesmosome assembly; ISS:HGNC-UCL. DR GO; GO:0031175; P:neuron projection development; IDA:MGI. 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:0065003; P:protein-containing complex assembly; ISS:HGNC-UCL. DR GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI. DR GO; GO:0009888; P:tissue development; IBA:GO_Central. DR GO; GO:0048729; P:tissue morphogenesis; IMP:MGI. DR CDD; cd00055; EGF_Lam; 10. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 9. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000034; Laminin_IV. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR002049; LE_dom. DR PANTHER; PTHR10574:SF270; LAMININ SUBUNIT GAMMA-1; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00052; Laminin_B; 1. DR Pfam; PF00053; Laminin_EGF; 11. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00181; EGF; 9. DR SMART; SM00180; EGF_Lam; 10. DR SMART; SM00281; LamB; 1. DR SMART; SM00136; LamNT; 1. DR SUPFAM; SSF57196; EGF/Laminin; 10. DR PROSITE; PS00022; EGF_1; 8. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS01248; EGF_LAM_1; 10. DR PROSITE; PS50027; EGF_LAM_2; 10. DR PROSITE; PS51115; LAMININ_IVA; 1. DR PROSITE; PS51117; LAMININ_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil; KW Disulfide bond; Extracellular matrix; Glycoprotein; KW Laminin EGF-like domain; Phosphoprotein; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..33 FT CHAIN 34..1607 FT /note="Laminin subunit gamma-1" FT /id="PRO_0000017075" FT DOMAIN 44..283 FT /note="Laminin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466" FT DOMAIN 284..339 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 340..395 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 396..442 FT /note="Laminin EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 443..492 FT /note="Laminin EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 493..502 FT /note="Laminin EGF-like 5; first part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 512..687 FT /note="Laminin IV type A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458" FT DOMAIN 688..721 FT /note="Laminin EGF-like 5; second part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 722..770 FT /note="Laminin EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 771..825 FT /note="Laminin EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 826..881 FT /note="Laminin EGF-like 8; nidogen-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 882..932 FT /note="Laminin EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 933..980 FT /note="Laminin EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 981..1028 FT /note="Laminin EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT REGION 1029..1607 FT /note="Domain II and I" FT COILED 1034..1594 FT /evidence="ECO:0000255" FT MOD_RES 1147 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11047" FT MOD_RES 1491 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11047" FT CARBOHYD 58 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 132 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 574 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 648 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1020 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1173 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1203 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1221 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1239 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1378 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1393 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1437 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 284..293 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 286..303 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 305..314 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 340..349 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 342..365 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 368..377 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 380..393 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 396..408 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 398..414 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 416..425 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 428..440 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 443..454 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 445..461 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 463..472 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 475..490 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 722..731 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 724..738 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 740..749 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 752..768 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 771..779 FT DISULFID 773..790 FT DISULFID 793..802 FT DISULFID 805..823 FT DISULFID 826..840 FT DISULFID 828..847 FT DISULFID 850..859 FT DISULFID 862..879 FT DISULFID 882..896 FT DISULFID 884..903 FT DISULFID 905..914 FT DISULFID 917..930 FT DISULFID 933..945 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 935..952 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 954..963 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 966..978 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 981..993 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 983..999 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1001..1010 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1013..1026 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1029 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1032 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1598 FT /note="Interchain (with beta-1 chain)" FT CONFLICT 216 FT /note="G -> A (in Ref. 3; AAA39409)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="E -> D (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="S -> C (in Ref. 2; AAA39408)" FT /evidence="ECO:0000305" FT CONFLICT 447..448 FT /note="LR -> PS (in Ref. 2; AAA39408)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="D -> Y (in Ref. 2; AAA39408)" FT /evidence="ECO:0000305" FT CONFLICT 662 FT /note="T -> S (in Ref. 2; AAA39408)" FT /evidence="ECO:0000305" FT CONFLICT 886 FT /note="Missing (in Ref. 2; AAA39408)" FT /evidence="ECO:0000305" FT CONFLICT 1158 FT /note="Missing (in Ref. 2; AAA39408)" FT /evidence="ECO:0000305" FT CONFLICT 1434 FT /note="V -> A (in Ref. 2; AAA39408)" FT /evidence="ECO:0000305" FT CONFLICT 1475 FT /note="R -> K (in Ref. 4; CAA28838)" FT /evidence="ECO:0000305" FT CONFLICT 1576 FT /note="D -> N (in Ref. 4; CAA28838)" FT /evidence="ECO:0000305" FT TURN 55..58 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 72..75 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:4AQT" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 101..104 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 131..153 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 156..168 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 171..177 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:4AQT" FT TURN 222..225 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 229..234 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 236..241 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 243..253 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 274..284 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 349..351 FT /evidence="ECO:0007829|PDB:4AQT" FT HELIX 353..358 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:4AQT" FT TURN 369..371 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 382..385 FT /evidence="ECO:0007829|PDB:4AQT" FT STRAND 779..781 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 783..785 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 788..790 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 797..799 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 809..812 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 816..819 FT /evidence="ECO:0007829|PDB:1NPE" FT STRAND 821..825 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 834..837 FT /evidence="ECO:0007829|PDB:1TLE" FT TURN 842..844 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 846..849 FT /evidence="ECO:0007829|PDB:1TLE" FT TURN 856..859 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 866..868 FT /evidence="ECO:0007829|PDB:1KLO" FT HELIX 875..877 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 878..881 FT /evidence="ECO:0007829|PDB:1KLO" FT TURN 886..888 FT /evidence="ECO:0007829|PDB:1KLO" FT HELIX 890..892 FT /evidence="ECO:0007829|PDB:1KLO" FT TURN 898..900 FT /evidence="ECO:0007829|PDB:1KLO" FT STRAND 909..911 FT /evidence="ECO:0007829|PDB:1KLO" FT HELIX 924..926 FT /evidence="ECO:0007829|PDB:1KLO" FT HELIX 1555..1593 FT /evidence="ECO:0007829|PDB:5MC9" SQ SEQUENCE 1607 AA; 177298 MW; 81B7B08E4869F242 CRC64; MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP EFVNAAFNVT VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG AAFLTDYNNQ ADTTWWQSQT MLAGVQYPNS INLTLHLGKA FDITYVRLKF HTSRPESFAI YKRTREDGPW IPYQYYSGSC ENTYSKANRG FIRTGGDEQQ ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE WVTATDIRVT LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY FDPELYRSTG HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP VGSLSTQCDS YGRCSCKPGV MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS TDECNVETGR CVCKDNVEGF NCERCKPGFF NLESSNPKGC TPCFCFGHSS VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS DRQDIAVISD SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT SIKIRGTYSE RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE TCLPGYRRET PSLGPYSPCV LCTCNGHSET CDPETGVCDC RDNTAGPHCE KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA IVPKTKEVVC THCPTGTAGK RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC NRLTGECLKC IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG QCECQPGITG QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE CREGFVGNRC DQCEENYFYN RSWPGCQECP ACYRLVKDKA AEHRVKLQEL ESLIANLGTG DDMVTDQAFE DRLKEAEREV TDLLREAQEV KDVDQNLMDR LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE QLIEIASREL EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR VHEEAKRAGD KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ KLKDYEDLRE DMRGKEHEVK NLLEKGKAEQ QTADQLLARA DAAKALAEEA AKKGRSTLQE ANDILNNLKD FDRRVNDNKT AAEEALRRIP AINRTIAEAN EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS TKADAERTFG EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS DLDRKVSDLE SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN TPSIEKP //