LAMC1_MOUSE
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 25-MAY-2022, entry version 202.
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, 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 expression.";
RL Cell 143:1174-1189(2010).
RN [7]
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 [8]
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).
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; 10.
DR MINT; P02468; -.
DR STRING; 10090.ENSMUSP00000027752; -.
DR GlyConnect; 2461; 22 N-Linked glycans (10 sites).
DR GlyGen; P02468; 14 sites, 21 N-linked glycans (10 sites).
DR iPTMnet; P02468; -.
DR PhosphoSitePlus; P02468; -.
DR EPD; P02468; -.
DR jPOST; P02468; -.
DR MaxQB; P02468; -.
DR PaxDb; P02468; -.
DR PeptideAtlas; P02468; -.
DR PRIDE; P02468; -.
DR ProteomicsDB; 265036; -.
DR MGI; MGI:99914; Lamc1.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; P02468; -.
DR PhylomeDB; P02468; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
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:0031012; C:extracellular matrix; ISO:MGI.
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; IC: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; 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:0065003; P:protein-containing complex assembly; ISS:HGNC-UCL.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC: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 InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00180; EGF_Lam; 10.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
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
