LAMA1_MOUSE
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 03-AUG-2022, entry version 209.
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 PDBsum; 2JD4; -.
DR PDBsum; 5MC9; -.
DR SMR; P19137; -.
DR BioGRID; 201096; 15.
DR ComplexPortal; CPX-3008; Laminin-111 complex.
DR ComplexPortal; CPX-3010; Laminin-121 complex.
DR IntAct; P19137; 4.
DR MINT; P19137; -.
DR STRING; 10090.ENSMUSP00000043957; -.
DR GlyConnect; 2455; 4 N-Linked glycans (3 sites).
DR GlyGen; P19137; 17 sites, 4 N-linked glycans (3 sites).
DR iPTMnet; P19137; -.
DR PhosphoSitePlus; P19137; -.
DR MaxQB; P19137; -.
DR PaxDb; P19137; -.
DR PeptideAtlas; P19137; -.
DR PRIDE; P19137; -.
DR ProteomicsDB; 265033; -.
DR ProteomicsDB; 308736; -.
DR ABCD; P19137; 23 sequenced antibodies.
DR Antibodypedia; 4123; 339 antibodies from 30 providers.
DR DNASU; 16772; -.
DR Ensembl; ENSMUST00000035471; ENSMUSP00000043957; ENSMUSG00000032796.
DR GeneID; 16772; -.
DR KEGG; mmu:16772; -.
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; WVAARCQ; -.
DR OrthoDB; 128982at2759; -.
DR PhylomeDB; P19137; -.
DR TreeFam; TF335359; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 16772; 1 hit in 75 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 181 other tissues.
DR Genevisible; F8VQ40; MM.
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; IC:ComplexPortal.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
DR GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO: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; 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:0006468; P:protein phosphorylation; IDA:CACAO.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC: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 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 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 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; SSF49899; 5.
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.
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
