LAMA5_MOUSE
ID LAMA5_MOUSE Reviewed; 3718 AA.
AC Q61001; A2ABW7; Q9JHQ6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Laminin subunit alpha-5;
DE AltName: Full=Laminin-10 subunit alpha;
DE AltName: Full=Laminin-11 subunit alpha;
DE AltName: Full=Laminin-15 subunit alpha;
DE Flags: Precursor;
GN Name=Lama5;
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 [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., 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-92, AND PROTEIN SEQUENCE OF 41-46.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-3718.
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=7499364; DOI=10.1074/jbc.270.48.28523;
RA Miner J.H., Lewis R.M., Sanes J.R.;
RT "Molecular cloning of a novel laminin chain, alpha 5, and widespread
RT expression in adult mouse tissues.";
RL J. Biol. Chem. 270:28523-28526(1995).
RN [4]
RP SEQUENCE REVISION.
RA Miner J.H., Lewis R.M., Sanes J.R.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248; ASN-926; ASN-2198;
RP ASN-2211; ASN-2395; ASN-2425 AND ASN-3623.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
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. Alpha-5 may be the major laminin alpha
CC chain of adult epithelial and/or endothelial basal laminae.
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-5 is a
CC subunit of laminin-10 (laminin-511), laminin-11 (laminin-521) and
CC laminin-15 (laminin-523).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- TISSUE SPECIFICITY: In adult, high levels in heart, lung, and kidney;
CC lower in brain, muscle and testis; very low in liver, gut and skin.
CC Expressed in many tissues in embryonic day 11.
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.
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DR EMBL; AL663027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ293593; CAB99255.1; -; mRNA.
DR EMBL; U37501; AAC53430.1; -; mRNA.
DR CCDS; CCDS38375.1; -.
DR PIR; T10053; T10053.
DR RefSeq; NP_001074640.1; NM_001081171.2.
DR PDB; 2Y38; X-ray; 2.90 A; A=44-433.
DR PDBsum; 2Y38; -.
DR SMR; Q61001; -.
DR BioGRID; 201100; 15.
DR ComplexPortal; CPX-3016; Laminin-511 complex.
DR ComplexPortal; CPX-3017; Laminin-521 complex.
DR ComplexPortal; CPX-3020; Laminin-522 complex.
DR ComplexPortal; CPX-3021; Laminin-523 complex.
DR IntAct; Q61001; 3.
DR MINT; Q61001; -.
DR STRING; 10090.ENSMUSP00000015791; -.
DR GlyConnect; 2458; 7 N-Linked glycans (8 sites).
DR GlyGen; Q61001; 26 sites, 7 N-linked glycans (8 sites).
DR iPTMnet; Q61001; -.
DR PhosphoSitePlus; Q61001; -.
DR EPD; Q61001; -.
DR jPOST; Q61001; -.
DR MaxQB; Q61001; -.
DR PaxDb; Q61001; -.
DR PeptideAtlas; Q61001; -.
DR PRIDE; Q61001; -.
DR ProteomicsDB; 264910; -.
DR Antibodypedia; 14779; 300 antibodies from 32 providers.
DR Ensembl; ENSMUST00000015791; ENSMUSP00000015791; ENSMUSG00000015647.
DR GeneID; 16776; -.
DR KEGG; mmu:16776; -.
DR UCSC; uc008oip.1; mouse.
DR CTD; 3911; -.
DR MGI; MGI:105382; Lama5.
DR VEuPathDB; HostDB:ENSMUSG00000015647; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000156537; -.
DR HOGENOM; CLU_000301_1_0_1; -.
DR InParanoid; Q61001; -.
DR OMA; RDTYQFG; -.
DR OrthoDB; 2342at2759; -.
DR PhylomeDB; Q61001; -.
DR TreeFam; TF335359; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 16776; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Lama5; mouse.
DR EvolutionaryTrace; Q61001; -.
DR PRO; PR:Q61001; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61001; protein.
DR Bgee; ENSMUSG00000015647; Expressed in gastrula and 214 other tissues.
DR Genevisible; Q61001; MM.
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; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043259; C:laminin-10 complex; IPI:MGI.
DR GO; GO:0005610; C:laminin-5 complex; ISO: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; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IDA:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:MGI.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
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:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0036484; P:trunk neural crest cell migration; IMP:MGI.
DR CDD; cd00055; EGF_Lam; 19.
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; 1.
DR Pfam; PF00053; Laminin_EGF; 19.
DR Pfam; PF02210; Laminin_G_2; 5.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00180; EGF_Lam; 22.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; SSF49899; 5.
DR PROSITE; PS00022; EGF_1; 19.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS01248; EGF_LAM_1; 19.
DR PROSITE; PS50027; EGF_LAM_2; 21.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
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 Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:11829758"
FT CHAIN 41..3718
FT /note="Laminin subunit alpha-5"
FT /id="PRO_0000017063"
FT DOMAIN 46..304
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 305..363
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 364..433
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 434..479
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 500..546
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 547..592
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 593..637
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 638..682
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 683..728
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 729..781
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 782..833
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 834..855
FT /note="Laminin EGF-like 11; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1443..1488
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1489..1532
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1533..1581
FT /note="Laminin EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1582..1632
FT /note="Laminin EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1633..1642
FT /note="Laminin EGF-like 16; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1646..1831
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 1832..1864
FT /note="Laminin EGF-like 16; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1865..1914
FT /note="Laminin EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1915..1970
FT /note="Laminin EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1971..2024
FT /note="Laminin EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2025..2071
FT /note="Laminin EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2072..2118
FT /note="Laminin EGF-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2119..2168
FT /note="Laminin EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2736..2933
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2947..3119
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3128..3296
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3337..3511
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3518..3689
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 856..1442
FT /note="Domain IV 1 (domain IV B)"
FT REGION 1253..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2735
FT /note="Domain II and I"
FT COILED 2205..2257
FT /evidence="ECO:0000255"
FT COILED 2330..2464
FT /evidence="ECO:0000255"
FT COILED 2604..2621
FT /evidence="ECO:0000255"
FT COILED 2639..2705
FT /evidence="ECO:0000255"
FT MOTIF 1723..1725
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1839..1841
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1263..1277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 905
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2021
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 2211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 2365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 2425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 2503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 3673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 305..314
FT /evidence="ECO:0000250"
FT DISULFID 307..327
FT /evidence="ECO:0000250"
FT DISULFID 329..338
FT /evidence="ECO:0000250"
FT DISULFID 341..361
FT /evidence="ECO:0000250"
FT DISULFID 364..373
FT /evidence="ECO:0000250"
FT DISULFID 366..398
FT /evidence="ECO:0000250"
FT DISULFID 401..410
FT /evidence="ECO:0000250"
FT DISULFID 413..431
FT /evidence="ECO:0000250"
FT DISULFID 434..445
FT /evidence="ECO:0000250"
FT DISULFID 436..452
FT /evidence="ECO:0000250"
FT DISULFID 454..463
FT /evidence="ECO:0000250"
FT DISULFID 466..476
FT /evidence="ECO:0000250"
FT DISULFID 500..512
FT /evidence="ECO:0000250"
FT DISULFID 502..521
FT /evidence="ECO:0000250"
FT DISULFID 523..532
FT /evidence="ECO:0000250"
FT DISULFID 535..544
FT /evidence="ECO:0000250"
FT DISULFID 547..559
FT /evidence="ECO:0000250"
FT DISULFID 549..566
FT /evidence="ECO:0000250"
FT DISULFID 568..577
FT /evidence="ECO:0000250"
FT DISULFID 580..590
FT /evidence="ECO:0000250"
FT DISULFID 593..605
FT /evidence="ECO:0000250"
FT DISULFID 595..611
FT /evidence="ECO:0000250"
FT DISULFID 613..622
FT /evidence="ECO:0000250"
FT DISULFID 625..635
FT /evidence="ECO:0000250"
FT DISULFID 638..650
FT /evidence="ECO:0000250"
FT DISULFID 640..656
FT /evidence="ECO:0000250"
FT DISULFID 658..667
FT /evidence="ECO:0000250"
FT DISULFID 670..680
FT /evidence="ECO:0000250"
FT DISULFID 683..695
FT /evidence="ECO:0000250"
FT DISULFID 685..702
FT /evidence="ECO:0000250"
FT DISULFID 704..713
FT /evidence="ECO:0000250"
FT DISULFID 716..731
FT /evidence="ECO:0000250"
FT DISULFID 752..761
FT /evidence="ECO:0000250"
FT DISULFID 764..779
FT /evidence="ECO:0000250"
FT DISULFID 782..796
FT /evidence="ECO:0000250"
FT DISULFID 784..802
FT /evidence="ECO:0000250"
FT DISULFID 804..813
FT /evidence="ECO:0000250"
FT DISULFID 816..831
FT /evidence="ECO:0000250"
FT DISULFID 834..846
FT /evidence="ECO:0000250"
FT DISULFID 836..853
FT /evidence="ECO:0000250"
FT DISULFID 855..864
FT /evidence="ECO:0000250"
FT DISULFID 1443..1455
FT /evidence="ECO:0000250"
FT DISULFID 1445..1462
FT /evidence="ECO:0000250"
FT DISULFID 1464..1473
FT /evidence="ECO:0000250"
FT DISULFID 1476..1486
FT /evidence="ECO:0000250"
FT DISULFID 1489..1496
FT /evidence="ECO:0000250"
FT DISULFID 1491..1503
FT /evidence="ECO:0000250"
FT DISULFID 1505..1514
FT /evidence="ECO:0000250"
FT DISULFID 1517..1530
FT /evidence="ECO:0000250"
FT DISULFID 1533..1548
FT /evidence="ECO:0000250"
FT DISULFID 1535..1555
FT /evidence="ECO:0000250"
FT DISULFID 1557..1566
FT /evidence="ECO:0000250"
FT DISULFID 1569..1579
FT /evidence="ECO:0000250"
FT DISULFID 1582..1594
FT /evidence="ECO:0000250"
FT DISULFID 1584..1601
FT /evidence="ECO:0000250"
FT DISULFID 1603..1612
FT /evidence="ECO:0000250"
FT DISULFID 1615..1630
FT /evidence="ECO:0000250"
FT DISULFID 1865..1874
FT /evidence="ECO:0000250"
FT DISULFID 1867..1881
FT /evidence="ECO:0000250"
FT DISULFID 1884..1893
FT /evidence="ECO:0000250"
FT DISULFID 1896..1912
FT /evidence="ECO:0000250"
FT DISULFID 1915..1930
FT /evidence="ECO:0000250"
FT DISULFID 1917..1939
FT /evidence="ECO:0000250"
FT DISULFID 1941..1950
FT /evidence="ECO:0000250"
FT DISULFID 1953..1968
FT /evidence="ECO:0000250"
FT DISULFID 1971..1986
FT /evidence="ECO:0000250"
FT DISULFID 1973..1993
FT /evidence="ECO:0000250"
FT DISULFID 1996..2005
FT /evidence="ECO:0000250"
FT DISULFID 2008..2022
FT /evidence="ECO:0000250"
FT DISULFID 2025..2035
FT /evidence="ECO:0000250"
FT DISULFID 2027..2042
FT /evidence="ECO:0000250"
FT DISULFID 2044..2053
FT /evidence="ECO:0000250"
FT DISULFID 2056..2069
FT /evidence="ECO:0000250"
FT DISULFID 2072..2083
FT /evidence="ECO:0000250"
FT DISULFID 2074..2090
FT /evidence="ECO:0000250"
FT DISULFID 2092..2101
FT /evidence="ECO:0000250"
FT DISULFID 2104..2116
FT /evidence="ECO:0000250"
FT DISULFID 2119..2126
FT /evidence="ECO:0000250"
FT DISULFID 2121..2133
FT /evidence="ECO:0000250"
FT DISULFID 2135..2144
FT /evidence="ECO:0000250"
FT DISULFID 2147..2166
FT /evidence="ECO:0000250"
FT DISULFID 2169
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2172
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2903..2933
FT /evidence="ECO:0000250"
FT DISULFID 3094..3119
FT /evidence="ECO:0000250"
FT DISULFID 3265..3296
FT /evidence="ECO:0000250"
FT DISULFID 3488..3511
FT /evidence="ECO:0000250"
FT DISULFID 3661..3689
FT /evidence="ECO:0000250"
FT CONFLICT 662
FT /note="Y -> N (in Ref. 3; AAC53430)"
FT /evidence="ECO:0000305"
FT CONFLICT 1171
FT /note="Y -> H (in Ref. 3; AAC53430)"
FT /evidence="ECO:0000305"
FT CONFLICT 2223
FT /note="S -> R (in Ref. 3; AAC53430)"
FT /evidence="ECO:0000305"
FT CONFLICT 2411
FT /note="L -> V (in Ref. 3; AAC53430)"
FT /evidence="ECO:0000305"
FT CONFLICT 2751
FT /note="T -> P (in Ref. 3; AAC53430)"
FT /evidence="ECO:0000305"
FT CONFLICT 3497
FT /note="R -> Q (in Ref. 3; AAC53430)"
FT /evidence="ECO:0000305"
FT CONFLICT 3707
FT /note="Q -> H (in Ref. 3; AAC53430)"
FT /evidence="ECO:0000305"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 148..166
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 173..193
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:2Y38"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 260..270
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:2Y38"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 295..304
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:2Y38"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:2Y38"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:2Y38"
SQ SEQUENCE 3718 AA; 404054 MW; 18542A9661BA82E9 CRC64;
MAKRGGQLCA GSAPGALGPR SPAPRPLLLL LAGLALVGEA RTPGGDGFSL HPPYFNLAEG
ARITASATCG EEAPTRSVSR PTEDLYCKLV GGPVAGGDPN QTIQGQYCDI CTAANSNKAH
PVSNAIDGTE RWWQSPPLSR GLEYNEVNVT LDLGQVFHVA YVLIKFANSP RPDLWVLERS
TDFGHTYQPW QFFASSKRDC LERFGPRTLE RITQDDDVIC TTEYSRIVPL ENGEIVVSLV
NGRPGALNFS YSPLLRDFTK ATNIRLRFLR TNTLLGHLMG KALRDPTVTR RYYYSIKDIS
IGGRCVCHGH ADVCDAKDPL DPFRLQCACQ HNTCGGSCDR CCPGFNQQPW KPATTDSANE
CQSCNCHGHA YDCYYDPEVD RRNASQNQDN VYQGGGVCLD CQHHTTGINC ERCLPGFFRA
PDQPLDSPHV CRPCDCESDF TDGTCEDLTG RCYCRPNFTG ELCAACAEGY TDFPHCYPLP
SFPHNDTREQ VLPAGQIVNC DCNAAGTQGN ACRKDPRLGR CVCKPNFRGA HCELCAPGFH
GPSCHPCQCS SPGVANSLCD PESGQCMCRT GFEGDRCDHC ALGYFHFPLC QLCGCSPAGT
LPEGCDEAGR CQCRPGFDGP HCDRCLPGYH GYPDCHACAC DPRGALDQQC GVGGLCHCRP
GYTGATCQEC SPGFYGFPSC IPCHCSADGS LHTTCDPTTG QCRCRPRVTG LHCDMCVPGA
YNFPYCEAGS CHPAGLAPAN PALPETQAPC MCRAHVEGPS CDRCKPGYWG LSASNPEGCT
RCSCDPRGTL GGVTECQGNG QCFCKAHVCG KTCAACKDGF FGLDYADYFG CRSCRCDVGG
ALGQGCEPKT GACRCRPNTQ GPTCSEPAKD HYLPDLHHMR LELEEAATPE GHAVRFGFNP
LEFENFSWRG YAHMMAIQPR IVARLNVTSP DLFRLVFRYV NRGSTSVNGQ ISVREEGKLS
SCTNCTEQSQ PVAFPPSTEP AFVTVPQRGF GEPFVLNPGI WALLVEAEGV LLDYVVLLPS
TYYEAALLQH RVTEACTYRP SALHSTENCL VYAHLPLDGF PSAAGTEALC RHDNSLPRPC
PTEQLSPSHP PLATCFGSDV DIQLEMAVPQ PGQYVLVVEY VGEDSHQEMG VAVHTPQRAP
QQGVLNLHPC PYSSLCRSPA RDTQHHLAIF YLDSEASIRL TAEQAHFFLH SVTLVPVEEF
STEFVEPRVF CVSSHGTFNP SSAACLASRF PKPPQPIILK DCQVLPLPPD LPLTQSQELS
PGAPPEGPQP RPPTAVDPNA EPTLLRHPQG TVVFTTQVPT LGRYAFLLHG YQPVHPSFPV
EVLINGGRIW QGHANASFCP HGYGCRTLVL CEGQTMLDVT DNELTVTVRV PEGRWLWLDY
VLIVPEDAYS SSYLQEEPLD KSYDFISHCA TQGYHISPSS SSPFCRNAAT SLSLFYNNGA
LPCGCHEVGA VSPTCEPFGG QCPCRGHVIG RDCSRCATGY WGFPNCRPCD CGARLCDELT
GQCICPPRTV PPDCLVCQPQ SFGCHPLVGC EECNCSGPGV QELTDPTCDM DSGQCRCRPN
VAGRRCDTCA PGFYGYPSCR PCDCHEAGTM ASVCDPLTGQ CHCKENVQGS RCDQCRVGTF
SLDAANPKGC TRCFCFGATE RCGNSNLARH EFVDMEGWVL LSSDRQVVPH EHRPEIELLH
ADLRSVADTF SELYWQAPPS YLGDRVSSYG GTLHYELHSE TQRGDIFIPY ESRPDVVLQG
NQMSIAFLEL AYPPPGQVHR GQLQLVEGNF RHLETHNPVS REELMMVLAG LEQLQIRALF
SQTSSSVSLR RVVLEVASEA GRGPPASNVE LCMCPANYRG DSCQECAPGY YRDTKGLFLG
RCVPCQCHGH SDRCLPGSGI CVGCQHNTEG DQCERCRPGF VSSDPSNPAS PCVSCPCPLA
VPSNNFADGC VLRNGRTQCL CRPGYAGASC ERCAPGFFGN PLVLGSSCQP CDCSGNGDPN
MIFSDCDPLT GACRGCLRHT TGPHCERCAP GFYGNALLPG NCTRCDCSPC GTETCDPQSG
RCLCKAGVTG QRCDRCLEGY FGFEQCQGCR PCACGPAAKG SECHPQSGQC HCQPGTTGPQ
CLECAPGYWG LPEKGCRRCQ CPRGHCDPHT GHCTCPPGLS GERCDTCSQQ HQVPVPGKPG
GHGIHCEVCD HCVVLLLDDL ERAGALLPAI REQLQGINAS SAAWARLHRL NASIADLQSK
LRSPPGPRYQ AAQQLQTLEQ QSISLQQDTE RLGSQATGVQ GQAGQLLDTT ESTLGRAQKL
LESVRAVGRA LNELASRMGQ GSPGDALVPS GEQLRWALAE VERLLWDMRT RDLGAQGAVA
EAELAEAQRL MARVQEQLTS FWEENQSLAT HIRDQLAQYE SGLMDLREAL NQAVNTTREA
EELNSRNQER LKEALQWKQE LSQDNATLKA TLQAASLILG HVSELLQGID QAKEDLEHLA
ASLDGAWTPL LKRMQAFSPA SSKVDLVEAA EAHAQKLNQL AINLSGIILG INQDRFIQRA
VEASNAYSSI LQAVQAAEDA AGQALRQASR TWEMVVQRGL AAGARQLLAN SSALEETILG
HQGRLGLAQG RLQAAGIQLH NVWARKNQLA AQIQEAQAML AMDTSETSEK IAHAKAVAAE
ALSTATHVQS QLQGMQKNVE RWQSQLGGLQ GQDLSQVERD ASSSVSTLEK TLPQLLAKLS
RLENRGVHNA SLALSANIGR VRKLIAQARS AASKVKVSMK FNGRSGVRLR TPRDLADLAA
YTALKFHIQS PVPAPEPGKN TGDHFVLYMG SRQATGDYMG VSLRNQKVHW VYRLGKAGPT
TLSIDENIGE QFAAVSIDRT LQFGHMSVTV EKQMVHEIKG DTVAPGSEGL LNLHPDDFVF
YVGGYPSNFT PPEPLRFPGY LGCIEMETLN EEVVSLYNFE QTFMLDTAVD KPCARSKATG
DPWLTDGSYL DGSGFARISF EKQFSNTKRF DQELRLVSYN GIIFFLKQES QFLCLAVQEG
TLVLFYDFGS GLKKADPLQP PQALTAASKA IQVFLLAGNR KRVLVRVERA TVFSVDQDNM
LEMADAYYLG GVPPEQLPLS LRQLFPSGGS VRGCIKGIKA LGKYVDLKRL NTTGISFGCT
ADLLVGRTMT FHGHGFLPLA LPDVAPITEV VYSGFGFRGT QDNNLLYYRT SPDGPYQVSL
REGHVTLRFM NQEVETQRVF ADGAPHYVAF YSNVTGVWLY VDDQLQLVKS HERTTPMLQL
QPEEPSRLLL GGLPVSGTFH NFSGCISNVF VQRLRGPQRV FDLHQNMGSV NVSVGCTPAQ
LIETSRATAQ KVSRRSRQPS QDLACTTPWL PGTIQDAYQF GGPLPSYLQF VGISPSHRNR
LHLSMLVRPH AASQGLLLST APMSGRSPSL VLFLNHGHFV AQTEGPGPRL QVQSRQHSRA
GQWHRVSVRW GMQQIQLVVD GSQTWSQKAL HHRVPRAERP QPYTLSVGGL PASSYSSKLP
VSVGFSGCLK KLQLDKRPLR TPTQMVGVTP CVSGPLEDGL FFPGSEGVVT LELPKAKMPY
VSLELEMRPL AAAGLIFHLG QALATPYMQL KVLTEQVLLQ ANDGAGEFST WVTYPKLCDG
RWHRVAVIMG RDTLRLEVDT QSNHTTGRLP ESLAGSPALL HLGSLPKSST ARPELPAYRG
CLRKLLINGA PVNVTASVQI QGAVGMRGCP SGTLALSKQG KALTQRQAKP SVSPLLWH
