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Database: UniProt
Entry: P02468
LinkDB: P02468
Original site: P02468 
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   13-FEB-2019, entry version 188.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3680290;
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;
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;
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
RT   coiled-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-
RT   linked 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
RT   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
RT   chain in solution.";
RL   J. Mol. Biol. 257:658-668(1996).
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. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS
CC       laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-
CC       121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6
CC       (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin),
CC       laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10
CC       (laminin-511) and laminin-11 (laminin-521).
CC   -!- INTERACTION:
CC       P02469:Lamb1; NbExp=4; IntAct=EBI-7059830, EBI-6662997;
CC       P10493:Nid1; NbExp=5; IntAct=EBI-7059830, EBI-1032117;
CC       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
CC       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 and IV are globular.
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   UniGene; Mm.1249; -.
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   ProteinModelPortal; 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   iPTMnet; P02468; -.
DR   PhosphoSitePlus; P02468; -.
DR   EPD; P02468; -.
DR   jPOST; P02468; -.
DR   MaxQB; P02468; -.
DR   PaxDb; P02468; -.
DR   PeptideAtlas; P02468; -.
DR   PRIDE; P02468; -.
DR   MGI; MGI:99914; Lamc1.
DR   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; ENOG410XRDC; LUCA.
DR   HOGENOM; HOG000019301; -.
DR   HOVERGEN; HBG100808; -.
DR   InParanoid; P02468; -.
DR   PhylomeDB; P02468; -.
DR   ChiTaRS; Lamc1; mouse.
DR   EvolutionaryTrace; P02468; -.
DR   PRO; PR:P02468; -.
DR   Proteomes; UP000000589; Unplaced.
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:0005615; C:extracellular space; HDA:BHF-UCL.
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:0043083; C:synaptic cleft; IDA:SynGO.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; ISS:HGNC.
DR   GO; GO:0016477; P:cell migration; ISS:HGNC.
DR   GO; GO:0022617; P:extracellular matrix disassembly; ISS:HGNC.
DR   GO; GO:0031581; P:hemidesmosome assembly; ISS:HGNC.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:HGNC.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
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   Complete proteome; 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       Laminin subunit gamma-1.
FT                                /FTId=PRO_0000017075.
FT   DOMAIN       44    283       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      284    339       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      340    395       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      396    442       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      443    492       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      493    502       Laminin EGF-like 5; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      512    687       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN      688    721       Laminin EGF-like 5; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      722    770       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      771    825       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      826    881       Laminin EGF-like 8; nidogen-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      882    932       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      933    980       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      981   1028       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   REGION     1029   1607       Domain II and I.
FT   COILED     1034   1594       {ECO:0000255}.
FT   MOD_RES    1147   1147       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11047}.
FT   MOD_RES    1491   1491       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11047}.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    132    132       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    574    574       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    648    648       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1020   1020       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1105   1105       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1159   1159       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1173   1173       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1203   1203       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1221   1221       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1239   1239       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1378   1378       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1393   1393       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1437   1437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    284    293       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    286    303       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    305    314       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    340    349       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    342    365       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    368    377       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    380    393       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    396    408       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    398    414       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    416    425       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    428    440       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    443    454       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    445    461       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    463    472       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    475    490       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    722    731       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    724    738       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    740    749       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    752    768       {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       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    935    952       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    954    963       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    966    978       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    981    993       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    983    999       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1001   1010       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1013   1026       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1029   1029       Interchain. {ECO:0000305}.
FT   DISULFID   1032   1032       Interchain. {ECO:0000305}.
FT   DISULFID   1598   1598       Interchain (with beta-1 chain).
FT   CONFLICT    216    216       G -> A (in Ref. 3; AAA39409).
FT                                {ECO:0000305}.
FT   CONFLICT    260    260       E -> D (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    337    337       S -> C (in Ref. 2; AAA39408).
FT                                {ECO:0000305}.
FT   CONFLICT    447    448       LR -> PS (in Ref. 2; AAA39408).
FT                                {ECO:0000305}.
FT   CONFLICT    544    544       D -> Y (in Ref. 2; AAA39408).
FT                                {ECO:0000305}.
FT   CONFLICT    662    662       T -> S (in Ref. 2; AAA39408).
FT                                {ECO:0000305}.
FT   CONFLICT    886    886       Missing (in Ref. 2; AAA39408).
FT                                {ECO:0000305}.
FT   CONFLICT   1158   1158       Missing (in Ref. 2; AAA39408).
FT                                {ECO:0000305}.
FT   CONFLICT   1434   1434       V -> A (in Ref. 2; AAA39408).
FT                                {ECO:0000305}.
FT   CONFLICT   1475   1475       R -> K (in Ref. 4; CAA28838).
FT                                {ECO:0000305}.
FT   CONFLICT   1576   1576       D -> N (in Ref. 4; CAA28838).
FT                                {ECO:0000305}.
FT   TURN         55     58       {ECO:0000244|PDB:4AQT}.
FT   STRAND       62     64       {ECO:0000244|PDB:4AQT}.
FT   STRAND       72     75       {ECO:0000244|PDB:4AQT}.
FT   STRAND       87     90       {ECO:0000244|PDB:4AQT}.
FT   STRAND       92     94       {ECO:0000244|PDB:4AQT}.
FT   TURN         95     97       {ECO:0000244|PDB:4AQT}.
FT   HELIX       101    104       {ECO:0000244|PDB:4AQT}.
FT   STRAND      110    112       {ECO:0000244|PDB:4AQT}.
FT   HELIX       121    123       {ECO:0000244|PDB:4AQT}.
FT   STRAND      126    128       {ECO:0000244|PDB:4AQT}.
FT   STRAND      131    153       {ECO:0000244|PDB:4AQT}.
FT   STRAND      156    168       {ECO:0000244|PDB:4AQT}.
FT   STRAND      171    177       {ECO:0000244|PDB:4AQT}.
FT   HELIX       180    184       {ECO:0000244|PDB:4AQT}.
FT   STRAND      202    205       {ECO:0000244|PDB:4AQT}.
FT   STRAND      212    214       {ECO:0000244|PDB:4AQT}.
FT   STRAND      216    221       {ECO:0000244|PDB:4AQT}.
FT   TURN        222    225       {ECO:0000244|PDB:4AQT}.
FT   HELIX       229    234       {ECO:0000244|PDB:4AQT}.
FT   HELIX       236    241       {ECO:0000244|PDB:4AQT}.
FT   STRAND      243    253       {ECO:0000244|PDB:4AQT}.
FT   HELIX       259    261       {ECO:0000244|PDB:4AQT}.
FT   HELIX       265    268       {ECO:0000244|PDB:4AQT}.
FT   STRAND      274    284       {ECO:0000244|PDB:4AQT}.
FT   STRAND      293    295       {ECO:0000244|PDB:4AQT}.
FT   STRAND      301    303       {ECO:0000244|PDB:4AQT}.
FT   STRAND      309    311       {ECO:0000244|PDB:4AQT}.
FT   HELIX       342    344       {ECO:0000244|PDB:4AQT}.
FT   STRAND      349    351       {ECO:0000244|PDB:4AQT}.
FT   HELIX       353    358       {ECO:0000244|PDB:4AQT}.
FT   STRAND      363    365       {ECO:0000244|PDB:4AQT}.
FT   TURN        369    371       {ECO:0000244|PDB:4AQT}.
FT   STRAND      372    374       {ECO:0000244|PDB:4AQT}.
FT   STRAND      382    385       {ECO:0000244|PDB:4AQT}.
FT   STRAND      779    781       {ECO:0000244|PDB:1KLO}.
FT   STRAND      783    785       {ECO:0000244|PDB:1KLO}.
FT   STRAND      788    790       {ECO:0000244|PDB:1KLO}.
FT   STRAND      797    799       {ECO:0000244|PDB:1KLO}.
FT   STRAND      809    812       {ECO:0000244|PDB:1KLO}.
FT   STRAND      816    819       {ECO:0000244|PDB:1NPE}.
FT   STRAND      821    825       {ECO:0000244|PDB:1KLO}.
FT   STRAND      834    837       {ECO:0000244|PDB:1TLE}.
FT   TURN        842    844       {ECO:0000244|PDB:1KLO}.
FT   STRAND      846    849       {ECO:0000244|PDB:1TLE}.
FT   TURN        856    859       {ECO:0000244|PDB:1KLO}.
FT   STRAND      866    868       {ECO:0000244|PDB:1KLO}.
FT   HELIX       875    877       {ECO:0000244|PDB:1KLO}.
FT   STRAND      878    881       {ECO:0000244|PDB:1KLO}.
FT   TURN        886    888       {ECO:0000244|PDB:1KLO}.
FT   HELIX       890    892       {ECO:0000244|PDB:1KLO}.
FT   TURN        898    900       {ECO:0000244|PDB:1KLO}.
FT   STRAND      909    911       {ECO:0000244|PDB:1KLO}.
FT   HELIX       924    926       {ECO:0000244|PDB:1KLO}.
FT   HELIX      1555   1593       {ECO:0000244|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
//
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