LAMA5_HUMAN
ID LAMA5_HUMAN Reviewed; 3695 AA.
AC O15230; Q5U4N9; Q8TDF8; Q8WZA7; Q9H1P1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 8.
DT 03-AUG-2022, entry version 217.
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; Synonyms=KIAA0533, KIAA1907;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-401; THR-1258;
RP GLU-1367; SER-1807; MET-1900; ASN-2062 AND TRP-3079.
RX PubMed=11821406; DOI=10.1074/jbc.m111228200;
RA Doi M., Thyboll J., Kortesmaa J., Jansson K., Iivanainen A., Parvardeh M.,
RA Timpl R., Hedin U., Swedenborg J., Tryggvason K.;
RT "Recombinant human laminin-10 (alpha5beta1gamma1). Production,
RT purification, and migration-promoting activity on vascular endothelial
RT cells.";
RL J. Biol. Chem. 277:12741-12748(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-401.
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1934 (ISOFORM 1), AND
RP VARIANTS MET-889; GLU-1367 AND SER-1807.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2051-3695 (ISOFORM 1), AND
RP VARIANTS ASN-2062 AND TRP-3079.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2743-3695 (ISOFORM 1), AND VARIANT TRP-3079.
RC TISSUE=Placenta;
RX PubMed=9271224; DOI=10.1016/s0014-5793(97)00686-8;
RA Durkin M.E., Loechel F., Mattei M.-G., Gilpin B.J., Albrechtsen R.,
RA Wewer U.M.;
RT "Tissue-specific expression of the human laminin alpha5-chain, and mapping
RT of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome
RT 2 near the locus for the ragged (Ra) mutation.";
RL FEBS Lett. 411:296-300(1997).
RN [7]
RP EXPRESSION IN RETINA.
RX PubMed=10964957; DOI=10.1523/jneurosci.20-17-06517.2000;
RA Libby R.T., Champliaud M.-F., Claudepierre T., Xu Y., Gibbons E.P.,
RA Koch M., Burgeson R.E., Hunter D.D., Brunken W.J.;
RT "Laminin expression in adult and developing retinae: evidence of two novel
RT CNS laminins.";
RL J. Neurosci. 20:6517-6528(2000).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2209; ASN-2303; ASN-2423;
RP ASN-2501; ASN-2568; ASN-2707 AND ASN-3107.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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-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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15230-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15230-2; Sequence=VSP_057343, VSP_057344;
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, kidney, skeletal muscle,
CC pancreas, retina and placenta. Little or no expression in brain and
CC liver.
CC -!- DOMAIN: Domain G is globular and is part of the major cell-binding site
CC located in the long arm of the laminin heterotrimer.
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DR EMBL; AF443072; AAM12527.1; -; mRNA.
DR EMBL; AL354836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC085017; AAH85017.1; -; mRNA.
DR EMBL; AB067494; BAB67800.1; -; mRNA.
DR EMBL; AB011105; BAA25459.1; -; mRNA.
DR EMBL; Z95636; CAB09137.1; -; mRNA.
DR CCDS; CCDS33502.1; -. [O15230-1]
DR RefSeq; NP_005551.3; NM_005560.4. [O15230-1]
DR PDB; 5XAU; X-ray; 1.80 A; A/D=2655-3327.
DR PDB; 7CEC; EM; 3.90 A; C=2655-3327.
DR PDBsum; 5XAU; -.
DR PDBsum; 7CEC; -.
DR SMR; O15230; -.
DR BioGRID; 110105; 133.
DR ComplexPortal; CPX-1779; Laminin-511 complex.
DR ComplexPortal; CPX-1780; Laminin-521 complex.
DR ComplexPortal; CPX-1783; Laminin-522 complex.
DR ComplexPortal; CPX-1784; Laminin-523 complex.
DR CORUM; O15230; -.
DR IntAct; O15230; 37.
DR MINT; O15230; -.
DR STRING; 9606.ENSP00000252999; -.
DR ChEMBL; CHEMBL2364187; -.
DR DrugBank; DB06245; Lanoteplase.
DR CarbonylDB; O15230; -.
DR GlyConnect; 1441; 26 N-Linked glycans (11 sites).
DR GlyGen; O15230; 32 sites, 24 N-linked glycans (11 sites), 2 O-linked glycans (7 sites).
DR iPTMnet; O15230; -.
DR PhosphoSitePlus; O15230; -.
DR SwissPalm; O15230; -.
DR BioMuta; LAMA5; -.
DR EPD; O15230; -.
DR jPOST; O15230; -.
DR MassIVE; O15230; -.
DR MaxQB; O15230; -.
DR PaxDb; O15230; -.
DR PeptideAtlas; O15230; -.
DR PRIDE; O15230; -.
DR ProteomicsDB; 48522; -. [O15230-1]
DR Antibodypedia; 14779; 300 antibodies from 32 providers.
DR DNASU; 3911; -.
DR Ensembl; ENST00000252999.7; ENSP00000252999.3; ENSG00000130702.15. [O15230-1]
DR GeneID; 3911; -.
DR KEGG; hsa:3911; -.
DR MANE-Select; ENST00000252999.7; ENSP00000252999.3; NM_005560.6; NP_005551.3.
DR UCSC; uc002ycq.5; human. [O15230-1]
DR CTD; 3911; -.
DR DisGeNET; 3911; -.
DR GeneCards; LAMA5; -.
DR HGNC; HGNC:6485; LAMA5.
DR HPA; ENSG00000130702; Low tissue specificity.
DR MalaCards; LAMA5; -.
DR MIM; 601033; gene.
DR neXtProt; NX_O15230; -.
DR OpenTargets; ENSG00000130702; -.
DR Orphanet; 521450; LAMA5-related multisystemic syndrome.
DR PharmGKB; PA30274; -.
DR VEuPathDB; HostDB:ENSG00000130702; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000156537; -.
DR HOGENOM; CLU_000301_1_0_1; -.
DR InParanoid; O15230; -.
DR OMA; RDTYQFG; -.
DR OrthoDB; 2342at2759; -.
DR PhylomeDB; O15230; -.
DR TreeFam; TF335359; -.
DR PathwayCommons; O15230; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR SignaLink; O15230; -.
DR SIGNOR; O15230; -.
DR BioGRID-ORCS; 3911; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; LAMA5; human.
DR GeneWiki; Laminin,_alpha_5; -.
DR GenomeRNAi; 3911; -.
DR Pharos; O15230; Tbio.
DR PRO; PR:O15230; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O15230; protein.
DR Bgee; ENSG00000130702; Expressed in right uterine tube and 181 other tissues.
DR ExpressionAtlas; O15230; baseline and differential.
DR Genevisible; O15230; HS.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043259; C:laminin-10 complex; IDA:UniProtKB.
DR GO; GO:0043260; C:laminin-11 complex; TAS:BHF-UCL.
DR GO; GO:0005610; C:laminin-5 complex; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IBA:GO_Central.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0036484; P:trunk neural crest cell migration; IEA:Ensembl.
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 InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 19.
DR Pfam; PF02210; Laminin_G_2; 4.
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; 21.
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; 3.
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; Alternative splicing; Basement membrane; Cell adhesion;
KW Coiled coil; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..3695
FT /note="Laminin subunit alpha-5"
FT /id="PRO_0000017062"
FT DOMAIN 41..299
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 300..358
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 359..428
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 429..474
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 494..540
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 541..586
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 587..631
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 632..676
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 677..722
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 723..775
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 776..828
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 829..850
FT /note="Laminin EGF-like 11; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1438..1483
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1484..1527
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1528..1576
FT /note="Laminin EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1577..1627
FT /note="Laminin EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1628..1637
FT /note="Laminin EGF-like 16; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1641..1830
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 1831..1863
FT /note="Laminin EGF-like 16; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1864..1912
FT /note="Laminin EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1913..1968
FT /note="Laminin EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1969..2022
FT /note="Laminin EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2023..2069
FT /note="Laminin EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2070..2116
FT /note="Laminin EGF-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2117..2166
FT /note="Laminin EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2736..2929
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2941..3115
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3124..3292
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3340..3513
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3520..3692
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 851..1437
FT /note="Domain IV 1 (domain IV B)"
FT REGION 1251..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2167..2735
FT /note="Domain II and I"
FT REGION 3224..3244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2203..2221
FT /evidence="ECO:0000255"
FT COILED 2335..2466
FT /evidence="ECO:0000255"
FT COILED 2510..2670
FT /evidence="ECO:0000255"
FT MOTIF 1722..1724
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1838..1840
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 3107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 3209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 300..309
FT /evidence="ECO:0000250"
FT DISULFID 302..322
FT /evidence="ECO:0000250"
FT DISULFID 324..333
FT /evidence="ECO:0000250"
FT DISULFID 336..356
FT /evidence="ECO:0000250"
FT DISULFID 359..368
FT /evidence="ECO:0000250"
FT DISULFID 361..393
FT /evidence="ECO:0000250"
FT DISULFID 396..405
FT /evidence="ECO:0000250"
FT DISULFID 408..426
FT /evidence="ECO:0000250"
FT DISULFID 429..440
FT /evidence="ECO:0000250"
FT DISULFID 431..447
FT /evidence="ECO:0000250"
FT DISULFID 449..458
FT /evidence="ECO:0000250"
FT DISULFID 461..471
FT /evidence="ECO:0000250"
FT DISULFID 494..506
FT /evidence="ECO:0000250"
FT DISULFID 496..515
FT /evidence="ECO:0000250"
FT DISULFID 517..526
FT /evidence="ECO:0000250"
FT DISULFID 529..538
FT /evidence="ECO:0000250"
FT DISULFID 541..553
FT /evidence="ECO:0000250"
FT DISULFID 543..560
FT /evidence="ECO:0000250"
FT DISULFID 562..571
FT /evidence="ECO:0000250"
FT DISULFID 574..584
FT /evidence="ECO:0000250"
FT DISULFID 587..599
FT /evidence="ECO:0000250"
FT DISULFID 589..605
FT /evidence="ECO:0000250"
FT DISULFID 607..616
FT /evidence="ECO:0000250"
FT DISULFID 619..629
FT /evidence="ECO:0000250"
FT DISULFID 632..644
FT /evidence="ECO:0000250"
FT DISULFID 634..650
FT /evidence="ECO:0000250"
FT DISULFID 652..661
FT /evidence="ECO:0000250"
FT DISULFID 664..674
FT /evidence="ECO:0000250"
FT DISULFID 677..689
FT /evidence="ECO:0000250"
FT DISULFID 679..696
FT /evidence="ECO:0000250"
FT DISULFID 698..707
FT /evidence="ECO:0000250"
FT DISULFID 710..725
FT /evidence="ECO:0000250"
FT DISULFID 746..755
FT /evidence="ECO:0000250"
FT DISULFID 758..773
FT /evidence="ECO:0000250"
FT DISULFID 776..790
FT /evidence="ECO:0000250"
FT DISULFID 778..797
FT /evidence="ECO:0000250"
FT DISULFID 799..808
FT /evidence="ECO:0000250"
FT DISULFID 811..826
FT /evidence="ECO:0000250"
FT DISULFID 829..841
FT /evidence="ECO:0000250"
FT DISULFID 831..848
FT /evidence="ECO:0000250"
FT DISULFID 850..859
FT /evidence="ECO:0000250"
FT DISULFID 1438..1450
FT /evidence="ECO:0000250"
FT DISULFID 1440..1457
FT /evidence="ECO:0000250"
FT DISULFID 1459..1468
FT /evidence="ECO:0000250"
FT DISULFID 1471..1481
FT /evidence="ECO:0000250"
FT DISULFID 1484..1491
FT /evidence="ECO:0000250"
FT DISULFID 1486..1498
FT /evidence="ECO:0000250"
FT DISULFID 1500..1509
FT /evidence="ECO:0000250"
FT DISULFID 1512..1525
FT /evidence="ECO:0000250"
FT DISULFID 1528..1543
FT /evidence="ECO:0000250"
FT DISULFID 1530..1550
FT /evidence="ECO:0000250"
FT DISULFID 1552..1561
FT /evidence="ECO:0000250"
FT DISULFID 1564..1574
FT /evidence="ECO:0000250"
FT DISULFID 1577..1589
FT /evidence="ECO:0000250"
FT DISULFID 1579..1596
FT /evidence="ECO:0000250"
FT DISULFID 1598..1607
FT /evidence="ECO:0000250"
FT DISULFID 1610..1625
FT /evidence="ECO:0000250"
FT DISULFID 1864..1873
FT /evidence="ECO:0000250"
FT DISULFID 1866..1880
FT /evidence="ECO:0000250"
FT DISULFID 1883..1892
FT /evidence="ECO:0000250"
FT DISULFID 1895..1910
FT /evidence="ECO:0000250"
FT DISULFID 1913..1928
FT /evidence="ECO:0000250"
FT DISULFID 1915..1937
FT /evidence="ECO:0000250"
FT DISULFID 1939..1948
FT /evidence="ECO:0000250"
FT DISULFID 1951..1966
FT /evidence="ECO:0000250"
FT DISULFID 1969..1984
FT /evidence="ECO:0000250"
FT DISULFID 1971..1991
FT /evidence="ECO:0000250"
FT DISULFID 1994..2003
FT /evidence="ECO:0000250"
FT DISULFID 2006..2020
FT /evidence="ECO:0000250"
FT DISULFID 2023..2033
FT /evidence="ECO:0000250"
FT DISULFID 2025..2040
FT /evidence="ECO:0000250"
FT DISULFID 2042..2051
FT /evidence="ECO:0000250"
FT DISULFID 2054..2067
FT /evidence="ECO:0000250"
FT DISULFID 2070..2081
FT /evidence="ECO:0000250"
FT DISULFID 2072..2088
FT /evidence="ECO:0000250"
FT DISULFID 2090..2099
FT /evidence="ECO:0000250"
FT DISULFID 2102..2114
FT /evidence="ECO:0000250"
FT DISULFID 2117..2124
FT /evidence="ECO:0000250"
FT DISULFID 2119..2131
FT /evidence="ECO:0000250"
FT DISULFID 2133..2142
FT /evidence="ECO:0000250"
FT DISULFID 2145..2164
FT /evidence="ECO:0000250"
FT DISULFID 2167
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2170
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2899..2929
FT /evidence="ECO:0000250"
FT DISULFID 3090..3115
FT /evidence="ECO:0000250"
FT DISULFID 3261..3292
FT /evidence="ECO:0000250"
FT DISULFID 3490..3513
FT /evidence="ECO:0000250"
FT DISULFID 3664..3692
FT /evidence="ECO:0000250"
FT VAR_SEQ 493..561
FT /note="NCDCSAAGTQGNACRKDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPCQCS
FT SPGVADDRCDPDTGQCR -> SGVSLCRPGWSAVARSRLTSTSASWVRAILLPQSPEWL
FT GLQAPATTPGQFFVFLVETGFHHVGQAGLEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057343"
FT VAR_SEQ 562..3695
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057344"
FT VARIANT 401
FT /note="T -> A (in dbSNP:rs4925229)"
FT /evidence="ECO:0000269|PubMed:11821406,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047887"
FT VARIANT 889
FT /note="V -> M (in dbSNP:rs6062223)"
FT /evidence="ECO:0000269|PubMed:11572484"
FT /id="VAR_030847"
FT VARIANT 1258
FT /note="M -> T (in dbSNP:rs3810548)"
FT /evidence="ECO:0000269|PubMed:11821406"
FT /id="VAR_030848"
FT VARIANT 1367
FT /note="K -> E (in dbSNP:rs2427286)"
FT /evidence="ECO:0000269|PubMed:11572484,
FT ECO:0000269|PubMed:11821406"
FT /id="VAR_030849"
FT VARIANT 1434
FT /note="G -> A (in dbSNP:rs17750870)"
FT /id="VAR_030850"
FT VARIANT 1667
FT /note="R -> W (in dbSNP:rs13039398)"
FT /id="VAR_030851"
FT VARIANT 1671
FT /note="T -> M (in dbSNP:rs944893)"
FT /id="VAR_047888"
FT VARIANT 1717
FT /note="H -> Y (in dbSNP:rs875379)"
FT /id="VAR_030852"
FT VARIANT 1807
FT /note="F -> S (in dbSNP:rs2427284)"
FT /evidence="ECO:0000269|PubMed:11572484,
FT ECO:0000269|PubMed:11821406"
FT /id="VAR_030853"
FT VARIANT 1900
FT /note="V -> M (in dbSNP:rs2427283)"
FT /evidence="ECO:0000269|PubMed:11821406"
FT /id="VAR_030854"
FT VARIANT 1908
FT /note="A -> T (in dbSNP:rs11698080)"
FT /id="VAR_030855"
FT VARIANT 2036
FT /note="H -> R (in dbSNP:rs6143021)"
FT /id="VAR_030856"
FT VARIANT 2053
FT /note="R -> H (in dbSNP:rs3737137)"
FT /id="VAR_030857"
FT VARIANT 2062
FT /note="D -> N (in dbSNP:rs2274934)"
FT /evidence="ECO:0000269|PubMed:11821406,
FT ECO:0000269|PubMed:9628581"
FT /id="VAR_030858"
FT VARIANT 2226
FT /note="R -> H (in dbSNP:rs2297587)"
FT /id="VAR_030859"
FT VARIANT 3079
FT /note="R -> W (in dbSNP:rs944895)"
FT /evidence="ECO:0000269|PubMed:11821406,
FT ECO:0000269|PubMed:9271224, ECO:0000269|PubMed:9628581"
FT /id="VAR_030860"
FT CONFLICT 956
FT /note="T -> A (in Ref. 1; AAM12527)"
FT /evidence="ECO:0000305"
FT HELIX 2677..2700
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 2707..2731
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2737..2742
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2744..2747
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 2754..2756
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2759..2767
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2780..2786
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2792..2800
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2803..2809
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2815..2819
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2829..2836
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2839..2846
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2848..2850
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2852..2859
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2861..2863
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2875..2879
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 2889..2891
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2897..2905
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2914..2920
FT /evidence="ECO:0007829|PDB:5XAU"
FT TURN 2923..2925
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 2938..2942
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2944..2955
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2962..2972
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2975..2984
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2987..2994
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 2997..3006
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3025..3032
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3034..3036
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3038..3043
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3046..3052
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 3057..3059
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3062..3066
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 3070..3072
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 3075..3080
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3088..3096
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 3103..3105
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3109..3113
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 3117..3120
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3124..3136
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3147..3154
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3158..3167
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3170..3177
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3180..3185
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3188..3191
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3198..3200
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3202..3209
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3212..3217
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3220..3225
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3240..3248
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3259..3267
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3270..3272
FT /evidence="ECO:0007829|PDB:5XAU"
FT STRAND 3285..3291
FT /evidence="ECO:0007829|PDB:5XAU"
SQ SEQUENCE 3695 AA; 399737 MW; B13C479B55282E3C CRC64;
MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF NLAEGARIAA
SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG QYCDICTAAN SNKAHPASNA
IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ VFHVAYVLIK FANSPRPDLW VLERSMDFGR
TYQPWQFFAS SKRDCLERFG PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG
AMNFSYSPLL REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC
VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA NSANECQSCN
CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT TGVNCERCLP GFYRSPNHPL
DSPHVCRRCN CESDFTDGTC EDLTGRCYCR PNFSGERCDV CAEGFTGFPS CYPTPSSSND
TREQVLPAGQ IVNCDCSAAG TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP
CQCSSPGVAD DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD
EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC RCRPGYTGTA
CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP RVTGLRCDTC VPGAYNFPYC
EAGSCHPAGL APVDPALPEA QVPCMCRAHV EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL
RGTLGGVAEC QPGTGQCFCK PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS
CEPRTGVCRC RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN
FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE EGRSATCANC
TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV EAEGVLLDYV VLLPSAYYEA
ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL PLDGFPSAAG LEALCRQDNS LPRPCPTEQL
SPSHPPLITC TGSDVDVQLQ VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL
SLHPCLYSTL CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV
EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH AQDLTPAMSP
AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA FLLHGYQPAH PTFPVEVLIN
AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA LLDVTHSELT VTVRVPKGRW LWLDYVLVVP
ENVYSFGYLR EEPLDKSYDF ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC
HEVGATGPTC EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC
PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC KCRPNVTGRR
CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE NVQGPKCDQC SLGTFSLDAA
NPKGCTRCFC FGATERCRSS SYTRQEFVDM EGWVLLSTDR QVVPHERQPG TEMLRADLRH
VPEAVPEAFP ELYWQAPPSY LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN
QMSITFLEPA YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS
QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY RDVKGLFLGR
CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV SSRDDPSAPC VSCPCPLSVP
SNNFAEGCVL RGGRTQCLCK PGYAGASCER CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL
FSDCDPLTGA CRGCLRHTTG PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC
LCKAGVTGRR CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR
ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ VPVPGGPVGH
SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM AWARLHRLNA SIADLQSQLR
SPLGPRHETA QQLEVLEQQS TSLGQDARRL GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA
AIRAVDRTLS ELMSQTGHLG LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA
ELAAAQRLLA RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE
LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA KEELERLAAS
LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL NLSSIILDVN QDRLTQRAIE
ASNAYSRILQ AVQAAEDAAG QALQQADHTW ATVVRQGLVD RAQQLLANST ALEEAMLQEQ
QRLGLVWAAL QGARTQLRDV RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ
DTATRVQSQL QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL
ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP RDLADLAAYT
ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR DKKVHWVYQL GEAGPAVLSI
DEDIGEQFAA VSLDRTLQFG HMSVTVERQM IQETKGDTVA PGAEGLLNLR PDDFVFYVGG
YPSTFTPPPL LRFPGYRGCI EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL
TDGSYLDGTG FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL
LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS VEQDNDLELA
DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY VDLKRLNTTG VSAGCTADLL
VGRAMTFHGH GFLRLALSNV APLTGNVYSG FGFHSAQDSA LLYYRASPDG LCQVSLQQGR
VSLQLLRTEV KTQAGFADGA PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG
PPRLLLGGLP ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT
PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH LEFVGILARH
RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH FVAQMEGLGT RLRAQSRQRS
RPGRWHKVSV RWEKNRILLV TDGARAWSQE GPHRQHQGAE HPQPHTLFVG GLPASSHSSK
LPVTVGFSGC VKRLRLHGRP LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL
PDVGLELEVR PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL
CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE PMAVQPWPPA
YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA
