ID   LAMB1_MOUSE             Reviewed;        1786 AA.
AC   P02469; E9PXZ9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   16-SEP-2015, entry version 149.
DE   RecName: Full=Laminin subunit beta-1;
DE   AltName: Full=Laminin B1 chain;
DE   AltName: Full=Laminin-1 subunit beta;
DE   AltName: Full=Laminin-10 subunit beta;
DE   AltName: Full=Laminin-12 subunit beta;
DE   AltName: Full=Laminin-2 subunit beta;
DE   AltName: Full=Laminin-6 subunit beta;
DE   AltName: Full=Laminin-8 subunit beta;
DE   Flags: Precursor;
GN   Name=Lamb1; Synonyms=Lamb-1, Lamb1-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3493487; DOI=10.1073/pnas.84.4.935;
RA   Sasaki M., Kato S., Kohno K., Martin G.R., Yamada Y.;
RT   "Sequence of the cDNA encoding the laminin B1 chain reveals a
RT   multidomain protein containing cysteine-rich repeats.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:935-939(1987).
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 1292-1786.
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   [4]
RP   PROTEIN SEQUENCE OF 165-172; 539-547 AND 712-719.
RC   STRAIN=BALB/c; TISSUE=Endothelial cell;
RX   PubMed=9219532; DOI=10.1111/j.1432-1033.1997.t01-1-00727.x;
RA   Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R.,
RA   Sorokin L.M.;
RT   "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of
RT   endothelium.";
RL   Eur. J. Biochem. 246:727-735(1997).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279; ASN-1336 AND
RP   ASN-1343.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC   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   TISSUE SPECIFICITY.
RX   PubMed=23472759; DOI=10.1016/j.ajhg.2013.02.005;
RA   Radmanesh F., Caglayan A.O., Silhavy J.L., Yilmaz C., Cantagrel V.,
RA   Omar T., Rosti B., Kaymakcalan H., Gabriel S., Li M., Sestan N.,
RA   Bilguvar K., Dobyns W.B., Zaki M.S., Gunel M., Gleeson J.G.;
RT   "Mutations in LAMB1 cause cobblestone brain malformation without
RT   muscular or ocular abnormalities.";
RL   Am. J. Hum. Genet. 92:468-474(2013).
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. Involved in the
CC       organization of the laminar architecture of the cerebral cortex
CC       (By similarity). It is probably required for the integrity of the
CC       basement membrane/glia limitans that serves as an anchor point for
CC       the endfeet of radial glial cells and as a physical barrier to
CC       migrating neurons (By similarity). Radial glial cells play a
CC       central role in cerebral cortical development, where they act both
CC       as the proliferative unit of the cerebral cortex and a scaffold
CC       for neurons migrating toward the pial surface (By similarity).
CC       {ECO:0000250}.
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. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS
CC       laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-
CC       311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-
CC       511) and laminin-12 (laminin-213).
CC   -!- INTERACTION:
CC       P31696:AGRN (xeno); NbExp=2; IntAct=EBI-6662997, EBI-457650;
CC       P02468:Lamc1; NbExp=4; IntAct=EBI-6662997, EBI-7059830;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
CC   -!- TISSUE SPECIFICITY: Widely expressed in the embryo. High levels
CC       are detected in the cerebellar basement membrane, at postnatal day
CC       7. {ECO:0000269|PubMed:23472759}.
CC   -!- SIMILARITY: Contains 13 laminin EGF-like domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00460}.
CC   -!- SIMILARITY: Contains 1 laminin IV type B domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00462}.
CC   -!- SIMILARITY: Contains 1 laminin N-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00466}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA39407.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; M15525; AAA39407.1; ALT_INIT; mRNA.
DR   EMBL; CR974423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT571245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X05212; CAA28839.1; -; mRNA.
DR   PIR; A26413; MMMSB1.
DR   RefSeq; XP_006515055.2; XM_006514992.2.
DR   RefSeq; XP_006515056.1; XM_006514993.1.
DR   UniGene; Mm.172674; -.
DR   PDB; 4AQS; X-ray; 3.11 A; A=22-542.
DR   PDBsum; 4AQS; -.
DR   ProteinModelPortal; P02469; -.
DR   SMR; P02469; 29-492.
DR   BioGrid; 201101; 4.
DR   IntAct; P02469; 7.
DR   MINT; MINT-1206337; -.
DR   STRING; 10090.ENSMUSP00000002979; -.
DR   PhosphoSite; P02469; -.
DR   MaxQB; P02469; -.
DR   PaxDb; P02469; -.
DR   PRIDE; P02469; -.
DR   Ensembl; ENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
DR   GeneID; 16777; -.
DR   CTD; 3912; -.
DR   MGI; MGI:96743; Lamb1.
DR   eggNOG; NOG241384; -.
DR   GeneTree; ENSGT00780000121851; -.
DR   HOVERGEN; HBG052301; -.
DR   InParanoid; P02469; -.
DR   OrthoDB; EOG75XGK0; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-3000157; Laminin interactions.
DR   Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   Reactome; R-MMU-373760; L1CAM interactions.
DR   ChiTaRS; Lamb1; mouse.
DR   PRO; PR:P02469; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; P02469; -.
DR   CleanEx; MM_LAMB1-1; -.
DR   ExpressionAtlas; P02469; baseline and differential.
DR   GO; GO:0005605; C:basal lamina; IDA:MGI.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0043256; C:laminin complex; IDA:MGI.
DR   GO; GO:0005606; C:laminin-1 complex; ISS:HGNC.
DR   GO; GO:0043259; C:laminin-10 complex; ISS:HGNC.
DR   GO; GO:0005607; C:laminin-2 complex; ISS:HGNC.
DR   GO; GO:0043257; C:laminin-8 complex; ISS:HGNC.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; IPI:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; ISS:HGNC.
DR   GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR   GO; GO:0007611; P:learning or memory; NAS:UniProtKB.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:HGNC.
DR   GO; GO:0021812; P:neuronal-glial interaction involved in cerebral cortex radial glia guided migration; ISO:MGI.
DR   GO; GO:0042476; P:odontogenesis; ISS:HGNC.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISS:HGNC.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR013015; Laminin_IV_B.
DR   InterPro; IPR008211; Laminin_N.
DR   Pfam; PF00053; Laminin_EGF; 13.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS00022; EGF_1; 9.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 11.
DR   PROSITE; PS50027; EGF_LAM_2; 13.
DR   PROSITE; PS51116; LAMININ_IVB; 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; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     21
FT   CHAIN        22   1786       Laminin subunit beta-1.
FT                                /FTId=PRO_0000017066.
FT   DOMAIN       31    270       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      271    334       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      335    397       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      398    457       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      458    509       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      510    540       Laminin EGF-like 5; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      549    767       Laminin IV type B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00462}.
FT   DOMAIN      773    820       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      821    866       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      867    916       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      917    975       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      976   1027       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1028   1083       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1084   1131       Laminin EGF-like 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1132   1178       Laminin EGF-like 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   REGION     1179   1397       Domain II.
FT   REGION     1398   1430       Domain alpha.
FT   REGION     1431   1786       Domain I.
FT   COILED     1216   1315       {ECO:0000255}.
FT   COILED     1368   1388       {ECO:0000255}.
FT   COILED     1448   1778       {ECO:0000255}.
FT   MOD_RES     250    250       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1496   1496       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07942}.
FT   MOD_RES    1666   1666       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07942}.
FT   CARBOHYD    120    120       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    356    356       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    519    519       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    677    677       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1041   1041       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1195   1195       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1279   1279       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1336   1336       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1343   1343       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   1487   1487       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1542   1542       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1643   1643       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    271    280       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    273    298       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    300    309       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    312    332       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    335    344       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    337    362       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    365    374       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    377    395       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    398    411       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    400    426       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    428    437       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    440    455       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    458    472       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    460    479       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    481    490       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    493    507       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    510    522       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    512    529       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    531    540       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    773    785       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    775    792       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    794    803       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    806    818       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    821    833       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    823    840       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    842    851       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    854    864       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    867    876       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    869    883       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    886    895       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    898    914       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    917    933       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    919    944       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    946    955       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    958    973       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    976    990       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    978    997       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1000   1009       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1012   1025       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1028   1040       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1030   1054       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1056   1065       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1068   1081       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1084   1096       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1086   1103       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1105   1114       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1117   1129       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1132   1144       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1134   1151       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1153   1162       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1165   1176       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1179   1179       Interchain. {ECO:0000305}.
FT   DISULFID   1182   1182       Interchain. {ECO:0000305}.
FT   DISULFID   1785   1785       Interchain. {ECO:0000305}.
FT   CONFLICT    159    159       A -> T (in Ref. 1; AAA39407).
FT                                {ECO:0000305}.
FT   CONFLICT    569    569       I -> V (in Ref. 1; AAA39407).
FT                                {ECO:0000305}.
FT   CONFLICT    993    993       E -> D (in Ref. 1; AAA39407).
FT                                {ECO:0000305}.
FT   CONFLICT   1393   1393       V -> A (in Ref. 1; AAA39407 and 3;
FT                                CAA28839). {ECO:0000305}.
FT   CONFLICT   1531   1534       MEMP -> SGNA (in Ref. 1; AAA39407).
FT                                {ECO:0000305}.
FT   CONFLICT   1692   1692       G -> C (in Ref. 3; CAA28839).
FT                                {ECO:0000305}.
FT   CONFLICT   1749   1749       D -> N (in Ref. 3; CAA28839).
FT                                {ECO:0000305}.
FT   HELIX        30     32       {ECO:0000244|PDB:4AQS}.
FT   STRAND       40     43       {ECO:0000244|PDB:4AQS}.
FT   HELIX        47     49       {ECO:0000244|PDB:4AQS}.
FT   STRAND       58     60       {ECO:0000244|PDB:4AQS}.
FT   STRAND       62     67       {ECO:0000244|PDB:4AQS}.
FT   STRAND       69     72       {ECO:0000244|PDB:4AQS}.
FT   STRAND       74     79       {ECO:0000244|PDB:4AQS}.
FT   TURN         87     89       {ECO:0000244|PDB:4AQS}.
FT   HELIX        96     98       {ECO:0000244|PDB:4AQS}.
FT   STRAND      122    142       {ECO:0000244|PDB:4AQS}.
FT   STRAND      146    155       {ECO:0000244|PDB:4AQS}.
FT   STRAND      161    169       {ECO:0000244|PDB:4AQS}.
FT   TURN        170    172       {ECO:0000244|PDB:4AQS}.
FT   STRAND      173    177       {ECO:0000244|PDB:4AQS}.
FT   TURN        200    202       {ECO:0000244|PDB:4AQS}.
FT   STRAND      204    210       {ECO:0000244|PDB:4AQS}.
FT   STRAND      212    214       {ECO:0000244|PDB:4AQS}.
FT   HELIX       222    228       {ECO:0000244|PDB:4AQS}.
FT   STRAND      229    239       {ECO:0000244|PDB:4AQS}.
FT   HELIX       252    255       {ECO:0000244|PDB:4AQS}.
FT   STRAND      261    270       {ECO:0000244|PDB:4AQS}.
FT   STRAND      304    309       {ECO:0000244|PDB:4AQS}.
FT   STRAND      342    346       {ECO:0000244|PDB:4AQS}.
FT   HELIX       348    353       {ECO:0000244|PDB:4AQS}.
FT   STRAND      360    364       {ECO:0000244|PDB:4AQS}.
FT   STRAND      369    371       {ECO:0000244|PDB:4AQS}.
FT   STRAND      381    383       {ECO:0000244|PDB:4AQS}.
FT   STRAND      385    387       {ECO:0000244|PDB:4AQS}.
FT   STRAND      395    397       {ECO:0000244|PDB:4AQS}.
FT   TURN        402    404       {ECO:0000244|PDB:4AQS}.
FT   HELIX       407    409       {ECO:0000244|PDB:4AQS}.
FT   HELIX       417    419       {ECO:0000244|PDB:4AQS}.
FT   TURN        434    437       {ECO:0000244|PDB:4AQS}.
FT   STRAND      454    457       {ECO:0000244|PDB:4AQS}.
FT   TURN        462    464       {ECO:0000244|PDB:4AQS}.
FT   TURN        474    476       {ECO:0000244|PDB:4AQS}.
FT   TURN        488    490       {ECO:0000244|PDB:4AQS}.
SQ   SEQUENCE   1786 AA;  197090 MW;  E7F258170C3626DD CRC64;
     MGLLQVFAFG VLALWGTRVC AQEPEFSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK
     PEPYCIVSHL QEDKKCFICD SRDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN
     VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKAW GVYRYFAYDC ESSFPGISTG
     PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL
     HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVNEEV EGMVHGHCMC
     RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SSSCHFDMAV FLATGNVSGG
     VCDNCQHNTM GRNCEQCKPF YFQHPERDIR DPNLCEPCTC DPAGSENGGI CDGYTDFSVG
     LIAGQCRCKL HVEGERCDVC KEGFYDLSAE DPYGCKSCAC NPLGTIPGGN PCDSETGYCY
     CKRLVTGQRC DQCLPQHWGL SNDLDGCRPC DCDLGGALNN SCSEDSGQCS CLPHMIGRQC
     NEVESGYYFT TLDHYIYEAE EANLGPGVIV VERQYIQDRI PSWTGPGFVR VPEGAYLEFF
     IDNIPYSMEY EILIRYEPQL PDHWEKAVIT VQRPGKIPAS SRCGNTVPDD DNQVVSLSPG
     SRYVVLPRPV CFEKGMNYTV RLELPQYTAS GSDVESPYTF IDSLVLMPYC KSLDIFTVGG
     SGDGEVTNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALIHQTG LACECDPQGS
     LSSVCDPNGG QCQCRPNVVG RTCNRCAPGT FGFGPNGCKP CDCHLQGSAS AFCDAITGQC
     HCFQGIYARQ CDRCLPGYWG FPSCQPCQCN GHALDCDTVT GECLSCQDYT TGHNCERCLA
     GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY IGSRCDDCAS
     GFFGNPSDFG GSCQPCQCHH NIDTTDPEAC DKETGRCLKC LYHTEGDHCQ LCQYGYYGDA
     LRQDCRKCVC NYLGTVKEHC NGSDCHCDKA TGQCSCLPNV IGQNCDRCAP NTWQLASGTG
     CGPCNCNAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE
     TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDAII GELTNRTHKF
     LEKAKALKIS GVIGPYRETV DSVEKKVNEI KDILAQSPAA EPLKNIGILF EEAEKLTKDV
     TEKMAQVEVK LTDTASQSNS TAGELGALQA EAESLDKTVK ELAEQLEFIK NSDIQGALDS
     ITKYFQMSLE AEKRVNASTT DPNSTVEQSA LTRDRVEDLM LERESPFKEQ QEEQARLLDE
     LAGKLQSLDL SAVAQMTCGT PPGADCSESE CGGPNCRTDE GEKKCGGPGC GGLVTVAHSA
     WQKAMDFDRD VLSALAEVEQ LSKMVSEAKV RADEAKQNAQ DVLLKTNATK EKVDKSNEDL
     RNLIKQIRNF LTEDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VETLSQVEVI
     LQQSAADIAR AELLLEEAKR ASKSATDVKV TADMVKEALE EAEKAQVAAE KAIKQADEDI
     QGTQNLLTSI ESETAASEET LTNASQRISK LERNVEELKR KAAQNSGEAE YIEKVVYSVK
     QNADDVKKTL DGELDEKYKK VESLIAQKTE ESADARRKAE LLQNEAKTLL AQANSKLQLL
     EDLERKYEDN QKYLEDKAQE LVRLEGEVRS LLKDISEKVA VYSTCL
//