ID   LAMA1_MOUSE             Reviewed;        3083 AA.
AC   P19137; F8VQ40;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 2.
DT   24-JAN-2024, entry version 217.
DE   RecName: Full=Laminin subunit alpha-1;
DE   AltName: Full=Laminin A chain;
DE   AltName: Full=Laminin-1 subunit alpha;
DE   AltName: Full=Laminin-3 subunit alpha;
DE   AltName: Full=S-laminin subunit alpha;
DE            Short=S-LAM alpha;
DE   Flags: Precursor;
GN   Name=Lama1; Synonyms=Lama, Lama-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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3182802; DOI=10.1016/s0021-9258(18)37424-6;
RA   Sasaki M., Kleinman H.K., Huber H., Deutzmann R., Yamada Y.;
RT   "Laminin, a multidomain protein. The A chain has a unique globular domain
RT   and homology with the basement membrane proteoglycan and the laminin B
RT   chains.";
RL   J. Biol. Chem. 263:16536-16544(1988).
RN   [2] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-339.
RX   PubMed=3267223; DOI=10.1111/j.1432-1033.1988.tb14045.x;
RA   Hartl L., Oberbaeumer I., Deutzmann R.;
RT   "The N-terminus of laminin A chain is homologous to the B chains.";
RL   Eur. J. Biochem. 173:629-635(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2537-3083, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3181157; DOI=10.1111/j.1432-1033.1988.tb14342.x;
RA   Deutzmann R., Huber J., Schmetz K.A., Oberbaeumer I., Hartl L.;
RT   "Structural study of long arm fragments of laminin. Evidence for repetitive
RT   C-terminal sequences in the A-chain, not present in the B-chains.";
RL   Eur. J. Biochem. 177:35-45(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 25-32, AND PYROGLUTAMATE FORMATION AT GLN-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 alpha5
RT   chains.";
RL   Biochem. J. 362:213-221(2002).
RN   [6]
RP   INTERACTION WITH FBLN1.
RX   PubMed=8354280; DOI=10.1111/j.1432-1033.1993.tb18086.x;
RA   Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.;
RT   "Sequence of extracellular mouse protein BM-90/fibulin and its calcium-
RT   dependent binding to other basement-membrane ligands.";
RL   Eur. J. Biochem. 215:733-740(1993).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1344; ASN-1686; ASN-1718;
RP   ASN-1725; ASN-1763; ASN-1935; ASN-2026; ASN-2045; ASN-2066 AND ASN-2834.
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, 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).
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. Alpha-1 is a
CC       subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3
CC       (laminin-121 or S-laminin).
CC   -!- INTERACTION:
CC       P19137; O18738: DAG1; Xeno; NbExp=2; IntAct=EBI-7176628, EBI-8522926;
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 with
CC       other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domains VI, IV and G are globular.
CC   -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC       {ECO:0000250|UniProtKB:P25391}.
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DR   EMBL; J04064; AAA39410.1; -; mRNA.
DR   EMBL; AC154823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X07737; CAA30561.1; -; mRNA.
DR   EMBL; X13459; CAA31807.1; -; mRNA.
DR   EMBL; M36775; AAA39406.1; -; mRNA.
DR   CCDS; CCDS37681.1; -.
DR   PIR; A31771; MMMSA.
DR   RefSeq; NP_032506.2; NM_008480.2.
DR   PDB; 2JD4; X-ray; 1.90 A; A/B=2705-3083.
DR   PDB; 5MC9; X-ray; 2.13 A; A=2078-2706.
DR   PDB; 8DMK; EM; 3.70 A; A=28-332.
DR   PDBsum; 2JD4; -.
DR   PDBsum; 5MC9; -.
DR   PDBsum; 8DMK; -.
DR   EMDB; EMD-27542; -.
DR   SMR; P19137; -.
DR   BioGRID; 201096; 15.
DR   ComplexPortal; CPX-3008; Laminin-111 complex.
DR   ComplexPortal; CPX-3010; Laminin-121 complex.
DR   IntAct; P19137; 5.
DR   MINT; P19137; -.
DR   STRING; 10090.ENSMUSP00000043957; -.
DR   GlyConnect; 2455; 4 N-Linked glycans (3 sites).
DR   GlyCosmos; P19137; 17 sites, 4 glycans.
DR   GlyGen; P19137; 18 sites, 4 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P19137; -.
DR   MetOSite; P19137; -.
DR   PhosphoSitePlus; P19137; -.
DR   SwissPalm; P19137; -.
DR   MaxQB; P19137; -.
DR   PaxDb; 10090-ENSMUSP00000043957; -.
DR   PeptideAtlas; P19137; -.
DR   ProteomicsDB; 265033; -.
DR   ProteomicsDB; 308736; -.
DR   ABCD; P19137; 23 sequenced antibodies.
DR   Antibodypedia; 4123; 364 antibodies from 30 providers.
DR   DNASU; 16772; -.
DR   Ensembl; ENSMUST00000035471.9; ENSMUSP00000043957.8; ENSMUSG00000032796.9.
DR   GeneID; 16772; -.
DR   KEGG; mmu:16772; -.
DR   AGR; MGI:99892; -.
DR   CTD; 284217; -.
DR   MGI; MGI:99892; Lama1.
DR   VEuPathDB; HostDB:ENSMUSG00000032796; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   GeneTree; ENSGT00940000157124; -.
DR   HOGENOM; CLU_000301_0_0_1; -.
DR   InParanoid; P19137; -.
DR   OMA; TVRQHVH; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; P19137; -.
DR   TreeFam; TF335359; -.
DR   BioGRID-ORCS; 16772; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Lama1; mouse.
DR   EvolutionaryTrace; P19137; -.
DR   PRO; PR:P19137; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P19137; Protein.
DR   Bgee; ENSMUSG00000032796; Expressed in glomerular capsule and 184 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0043256; C:laminin complex; IDA:MGI.
DR   GO; GO:0005606; C:laminin-1 complex; IDA:MGI.
DR   GO; GO:0005608; C:laminin-3 complex; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
DR   GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IBA:GO_Central.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
DR   GO; GO:0043010; P:camera-type eye development; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:MGI.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
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:0006468; P:protein phosphorylation; IDA:CACAO.
DR   GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal.
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:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:0061304; P:retinal blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0009888; P:tissue development; IMP:MGI.
DR   CDD; cd00055; EGF_Lam; 15.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 15.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF409; LAMININ SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 17.
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   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00180; EGF_Lam; 16.
DR   SMART; SM00281; LamB; 2.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 14.
DR   PROSITE; PS00022; EGF_1; 11.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS01248; EGF_LAM_1; 15.
DR   PROSITE; PS50027; EGF_LAM_2; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   Genevisible; F8VQ40; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Basement membrane; Cell adhesion; Coiled coil;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Laminin EGF-like domain; Phosphoprotein;
KW   Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:11829758"
FT   CHAIN           25..3083
FT                   /note="Laminin subunit alpha-1"
FT                   /id="PRO_0000017055"
FT   DOMAIN          25..276
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          277..333
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          334..403
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          404..460
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          461..509
FT                   /note="Laminin EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          510..519
FT                   /note="Laminin EGF-like 5; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          523..715
FT                   /note="Laminin IV type A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          716..748
FT                   /note="Laminin EGF-like 5; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          749..797
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          798..855
FT                   /note="Laminin EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          856..908
FT                   /note="Laminin EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          909..957
FT                   /note="Laminin EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          958..1004
FT                   /note="Laminin EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1005..1050
FT                   /note="Laminin EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1051..1096
FT                   /note="Laminin EGF-like 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1097..1156
FT                   /note="Laminin EGF-like 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1157..1166
FT                   /note="Laminin EGF-like 14; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1177..1368
FT                   /note="Laminin IV type A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          1369..1409
FT                   /note="Laminin EGF-like 14; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1410..1458
FT                   /note="Laminin EGF-like 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1459..1515
FT                   /note="Laminin EGF-like 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1516..1562
FT                   /note="Laminin EGF-like 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          2124..2304
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2312..2488
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2493..2679
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2721..2893
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2898..3078
FT                   /note="Laminin G-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1564..2123
FT                   /note="Domain II and I"
FT   COILED          1617..1691
FT                   /evidence="ECO:0000255"
FT   COILED          1723..1809
FT                   /evidence="ECO:0000255"
FT   COILED          1868..1901
FT                   /evidence="ECO:0000255"
FT   MOTIF           1147..1149
FT                   /note="Cell attachment site"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:11829758"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        672
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        1659
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1686
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        1718
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        1725
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        1763
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        1811
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1935
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        2026
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        2045
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        2066
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        2355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2834
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        2923
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        277..286
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        279..297
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        299..308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        311..331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        334..343
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        336..368
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        371..380
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        383..401
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        404..416
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        406..434
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        436..445
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        448..458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        461..474
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        463..478
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        480..489
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        492..507
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        749..758
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        751..764
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        767..776
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        779..795
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        798..813
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        800..823
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        826..835
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        838..853
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        856..870
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        858..877
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        880..889
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        892..906
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        909..921
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        911..928
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        930..939
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        942..955
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        958..970
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        960..976
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        978..987
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        990..1002
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1005..1014
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1007..1021
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1023..1032
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1035..1048
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1051..1063
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1053..1070
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1072..1081
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1084..1094
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1097..1109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1099..1125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1127..1136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1139..1154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1410..1419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1412..1426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1429..1438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1441..1456
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1459..1473
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1461..1483
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1486..1495
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1498..1513
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1516..1528
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1518..1535
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1537..1546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1549..1560
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1563
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1567
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        2278..2304
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        2464..2488
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        2652..2679
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        2868..2893
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        3047..3078
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   CONFLICT        209
FT                   /note="I -> T (in Ref. 3; CAA30561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        656
FT                   /note="D -> N (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        920
FT                   /note="I -> V (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1122
FT                   /note="G -> S (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1131
FT                   /note="A -> V (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1295
FT                   /note="R -> Q (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1797
FT                   /note="K -> KE (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1964
FT                   /note="S -> G (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1990..1994
FT                   /note="MDNIM -> VDNIT (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2120
FT                   /note="V -> A (in Ref. 1; AAA39410)"
FT                   /evidence="ECO:0000305"
FT   TURN            2084..2088
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   HELIX           2089..2091
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   HELIX           2092..2121
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2126..2131
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2134..2137
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2143..2154
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2160..2166
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2173..2179
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2182..2191
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2193..2198
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2205..2207
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2209..2216
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2219..2226
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2236..2239
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2241..2243
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2254..2259
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2262..2264
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2276..2279
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2295..2299
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2302..2304
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2315..2325
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2333..2341
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2345..2352
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2360..2366
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2369..2378
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2380..2384
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2395..2402
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2405..2412
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2415..2425
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2427..2429
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2441..2445
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2462..2470
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2479..2487
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2495..2506
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2516..2526
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2528..2534
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2550..2556
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2559..2565
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2567..2569
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2573..2577
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2580..2582
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2586..2588
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2590..2597
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2600..2605
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2611..2614
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   HELIX           2617..2619
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2627..2633
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2651..2658
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   HELIX           2665..2667
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2669..2676
FT                   /evidence="ECO:0007829|PDB:5MC9"
FT   STRAND          2731..2735
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2742..2753
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2758..2764
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2768..2777
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2780..2786
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2791..2795
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2802..2804
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2806..2813
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2816..2821
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2842..2848
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2867..2874
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2885..2889
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2894..2916
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2922..2931
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2935..2941
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2943..2945
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2947..2953
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2956..2965
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2967..2972
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   HELIX           2979..2981
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2982..2984
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2986..2993
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          2996..3001
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          3004..3008
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          3022..3027
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          3045..3053
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   HELIX           3064..3066
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          3068..3074
FT                   /evidence="ECO:0007829|PDB:2JD4"
FT   STRAND          3078..3080
FT                   /evidence="ECO:0007829|PDB:2JD4"
SQ   SEQUENCE   3083 AA;  338148 MW;  4A7C156E40D85DC7 CRC64;
     MRGSGTGAAL LVLLASVLWV TVRSQQRGLF PAILNLATNA HISANATCGE KGPEMFCKLV
     EHVPGRPVRH AQCRVCDGNS TNPRERHPIS HAIDGTNNWW QSPSIQNGRE YHWVTVTLDL
     RQVFQVAYII IKAANAPRPG NWILERSVDG VKFKPWQYYA VSDTECLTRY KITPRRGPPT
     YRADNEVICT SYYSKLVPLE HGEIHTSLIN GRPSADDPSP QLLEFTSARY IRLRLQRIRT
     LNADLMTLSH RDLRDLDPIV TRRYYYSIKD ISVGGMCICY GHASSCPWDE EAKQLQCQCE
     HNTCGESCDR CCPGYHQQPW RPGTISSGNE CEECNCHNKA KDCYYDSSVA KERRSLNTAG
     QYSGGGVCVN CSQNTTGINC ETCIDQYYRP HKVSPYDDHP CRPCNCDPVG SLSSVCIKDD
     RHADLANGKW PGQCPCRKGY AGDKCDRCQF GYRGFPNCIP CDCRTVGSLN EDPCIEPCLC
     KKNVEGKNCD RCKPGFYNLK ERNPEGCSEC FCFGVSGVCD SLTWSISQVT NMSGWLVTDL
     MSTNKIRSQQ DVLGGHRQIS INNTAVMQRL TSTYYWAAPE AYLGNKLTAF GGFLKYTVSY
     DIPVETVDSD LMSHADIIIK GNGLTISTRA EGLSLQPYEE YFNVVRLVPE NFRDFDTRRE
     IDRDQLMTVL ANVTHLLIRA NYNSAKMALY RLDSVSLDIA SPNAIDLAVA ADVEHCECPQ
     GYTGTSCEAC LPGYYRVDGI LFGGICQPCE CHGHASECDI HGICSVCTHN TTGDHCEQCL
     PGFYGTPSRG TPGDCQPCAC PLSIDSNNFS PTCHLTDGEE VVCDQCAPGY SGSWCERCAD
     GYYGNPTVPG GTCVPCNCSG NVDPLEAGHC DSVTGECLKC LWNTDGAHCE RCADGFYGDA
     VTAKNCRACD CHENGSLSGI CHLETGLCDC KPHVTGQQCD QCLSGYYGLD TGLGCVPCNC
     SVEGSVSDNC TEEGQCHCGP GVSGKQCDRC SHGFYAFQDG GCTPCDCAHT QNNCDPASGE
     CLCPPHTQGL KCEECEEAYW GLDPEQGCQA CNCSAVGSTS AQCDVLSGHC PCKKGFGGQS
     CHQCSLGYRS FPDCVPCGCD LRGTLPDTCD LEQGLCSCSE DGGTCSCKEN AVGPQCSKCQ
     AGTFALRGDN PQGCSPCFCF GLSQLCSELE GYVRTLITLA SDQPLLHVVS QSNLKGTIEG
     VHFQPPDTLL DAEAVRQHIY AEPFYWRLPK QFQGDQLLAY GGKLQYSVAF YSTLGTGTSN
     YEPQVLIKGG RARKHVIYMD APAPENGVRQ DYEVRMKEEF WKYFNSVSEK HVTHSDFMSV
     LSNIDYILIK ASYGQGLQQS RIANISMEVG RKAVELPAEG EAALLLELCV CPPGTAGHSC
     QDCAPGYYRE KLPESGGRGP RPLLAPCVPC NCNNHSDVCD PETGKCLSCR DHTSGDHCEL
     CASGYYGKVT GLPGDCTPCT CPHHPPFSFS PTCVVEGDSD FRCNACLPGY EGQYCERCSA
     GYHGNPRAAG GSCQTCDCNP QGSVHSDCDR ASGQCVCKPG ATGLHCEKCL PRHILMESDC
     VSCDDDCVGP LLNDLDSVGD AVLSLNLTGV SPAPYGILEN LENTTKYFQR YLIKENAKKI
     RAEIQLEGIA EQTENLQKEL TRVLARHQKV NAEMERTSNG TQALATFIEQ LHANIKEITE
     KVATLNQTAR KDFQPPVSAL QSMHQNISSL LGLIKERNFT EMQQNATLEL KAAKDLLSRI
     QKRFQKPQEK LKALKEANSL LSNHSEKLQA AEELLKEAGS KTQESNLLLL LVKANLKEFQ
     EKKLRVQEEQ NVTSELIAKG REWVDAAGTH TAAAQDTLTQ LEHHRDELLL WARKIRSHVD
     DLVMQMSKRR ARDLVHRAEQ HASELQSRAG ALDRDLENVR NVSLNATSAA HVHSNIQTLT
     EEAEMLAADA HKTANKTDLI SESLASRGKA VLQRSSRFLK ESVSTRRKQQ GITMKLDELK
     NLTSQFQESM DNIMKQANDS LAMLRESPGG MREKGRKARE LAAAANESAV KTLEDVLALS
     LRVFNTSEDL SRVNATVQET NDLLHNSTMT TLLAGRKMKD MEMQANLLLD RLKPLKTLEE
     NLSRNLSEIK LLISRARKQV ASIKVAVSAD RDCIRAYQPQ TSSTNYNTLI LNVKTQEPDN
     LLFYLGSSSS SDFLAVEMRR GKVAFLWDLG SGSTRLEFPE VSINNNRWHS IYITRFGNMG
     SLSVKEASAA ENPPVRTSKS PGPSKVLDIN NSTLMFVGGL GGQIKKSPAV KVTHFKGCMG
     EAFLNGKSIG LWNYIEREGK CNGCFGSSQN EDSSFHFDGS GYAMVEKTLR PTVTQIVILF
     STFSPNGLLF YLASNGTKDF LSIELVRGRV KVMVDLGSGP LTLMTDRRYN NGTWYKIAFQ
     RNRKQGLLAV FDAYDTSDKE TKQGETPGAA SDLNRLEKDL IYVGGLPHSK AVRKGVSSRS
     YVGCIKNLEI SRSTFDLLRN SYGVRKGCAL EPIQSVSFLR GGYVEMPPKS LSPESSLLAT
     FATKNSSGIL LVALGKDAEE AGGAQAHVPF FSIMLLEGRI EVHVNSGDGT SLRKALLHAP
     TGSYSDGQEH SISLVRNRRV ITIQVDENSP VEMKLGPLTE GKTIDISNLY IGGLPEDKAT
     PMLKMRTSFH GCIKNVVLDA QLLDFTHATG SEQVELDTCL LAEEPMQSLH REHGELPPEP
     PTLPQPELCA VDTAPGYVAG AHQFGLSQNS HLVLPLNQSD VRKRLQVQLS IRTFASSGLI
     YYVAHQNQMD YATLQLQEGR LHFMFDLGKG RTKVSHPALL SDGKWHTVKT EYIKRKAFMT
     VDGQESPSVT VVGNATTLDV ERKLYLGGLP SHYRARNIGT ITHSIPACIG EIMVNGQQLD
     KDRPLSASAV DRCYVVAQEG TFFEGSGYAA LVKEGYKVRL DLNITLEFRT TSKNGVLLGI
     SSAKVDAIGL EIVDGKVLFH VNNGAGRITA TYQPRAARAL CDGKWHTLQA HKSKHRIVLT
     VDGNSVRAES PHTHSTSADT NDPIYVGGYP AHIKQNCLSS RASFRGCVRN LRLSRGSQVQ
     SLDLSRAFDL QGVFPHSCPG PEP
//