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 02-OCT-2024, entry version 229. 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). RN [12] RP VARIANTS NPHS26 TRP-747; GLY-1001 AND SER-2948, AND INVOLVEMENT IN NPHS26. RX PubMed=29534211; DOI=10.1093/ndt/gfy028; RA Braun D.A., Warejko J.K., Ashraf S., Tan W., Daga A., Schneider R., RA Hermle T., Jobst-Schwan T., Widmeier E., Majmundar A.J., Nakayama M., RA Schapiro D., Rao J., Schmidt J.M., Hoogstraten C.A., Hugo H., RA Bakkaloglu S.A., Kari J.A., El Desoky S., Daouk G., Mane S., Lifton R.P., RA Shril S., Hildebrandt F.; RT "Genetic variants in the LAMA5 gene in pediatric nephrotic syndrome."; RL Nephrol. Dial. Transplant. 34:485-493(2019). RN [13] RP VARIANT NPHS26 LEU-286, AND CHARACTERIZATION OF VARIANT NPHS26 LEU-286. RX PubMed=32439764; DOI=10.1242/dev.189183; RA Jones L.K., Lam R., McKee K.K., Aleksandrova M., Dowling J., RA Alexander S.I., Mallawaarachchi A., Cottle D.L., Short K.M., Pais L., RA Miner J.H., Mallett A.J., Simons C., McCarthy H., Yurchenco P.D., RA Smyth I.M.; RT "A mutation affecting laminin alpha 5 polymerisation gives rise to a RT syndromic developmental disorder."; RL Development 147:0-0(2020). RN [14] RP VARIANTS BBDS2 THR-1405 AND CYS-2053, INVOLVEMENT IN BBDS2, TISSUE RP SPECIFICITY, AND FUNCTION. RX PubMed=33242826; DOI=10.1016/j.ebiom.2020.103075; RA Barad M., Csukasi F., Bosakova M., Martin J.H., Zhang W., Paige Taylor S., RA Lachman R.S., Zieba J., Bamshad M., Nickerson D., Chong J.X., Cohn D.H., RA Krejci P., Krakow D., Duran I.; RT "Biallelic mutations in LAMA5 disrupts a skeletal noncanonical focal RT adhesion pathway and produces a distinct bent bone dysplasia."; RL EBioMedicine 62:103075-103075(2020). RN [15] RP VARIANTS NPHS26 VAL-498; 2720-ARG--ALA-3695 DEL; HIS-2800 AND RP 3078-ARG--ALA-3695 DEL, AND INVOLVEMENT IN NPHS26. RX PubMed=35419533; DOI=10.34067/kid.0004952021; RA Taniguchi Y., Nagano C., Sekiguchi K., Tashiro A., Sugawara N., RA Sakaguchi H., Umeda C., Aoto Y., Ishiko S., Rossanti R., Sakakibara N., RA Horinouchi T., Yamamura T., Kondo A., Nagai S., Nagase H., Iijima K., RA Miner J.H., Nozu K.; RT "Clear Evidence of LAMA5 Gene Biallelic Truncating Variants Causing RT Infantile Nephrotic Syndrome."; RL Kidney360 2:1968-1978(2021). 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. Plays a role in the regulation of CC skeletogenesis, through a mechanism that involves integrin-mediated CC signaling and PTK2B/PYK2 (PubMed:33242826). CC {ECO:0000269|PubMed:33242826}. 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. Expressed in muscle, ligaments, periosteum, trabecular bone and CC throughout the cartilage, particularly in the growth plate and in CC articular chondrocytes (PubMed:33242826). CC {ECO:0000269|PubMed:33242826}. 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. CC -!- DISEASE: Nephrotic syndrome 26 (NPHS26) [MIM:620049]: A form of CC nephrotic syndrome, a renal disease clinically characterized by severe CC proteinuria, resulting in complications such as hypoalbuminemia, CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic CC changes such as focal segmental glomerulosclerosis and diffuse CC mesangial proliferation. Some affected individuals have an inherited CC steroid-resistant form that progresses to end-stage renal failure. CC NPHS26 is an autosomal recessive form characterized by onset of CC proteinuria in the first months or years of life. Some patients respond CC to steroids, whereas others show steroid resistance and progression to CC end-stage renal disease. {ECO:0000269|PubMed:29534211, CC ECO:0000269|PubMed:32439764, ECO:0000269|PubMed:35419533}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Bent bone dysplasia syndrome 2 (BBDS2) [MIM:620076]: An CC autosomal recessive bone dysplasia characterized by defects in both the CC axial and appendicular skeleton, with radiographic findings showing CC undermineralized bone and a distinct angulation of the mid femoral CC shaft. Extraskeletal features include facial dysmorphisms, abnormally CC formed ears with tags, wide spaced nipples, and atrial septal defects. CC Elbow fusions, ulnar flexion contractions at the wrist, bilateral CC talipes equinovarus, and failure to mount a respiratory effort at birth CC suggest abnormalities in muscle function. CC {ECO:0000269|PubMed:33242826}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-30342; -. DR SMR; O15230; -. DR BioGRID; 110105; 147. 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; 87. DR MINT; O15230; -. DR STRING; 9606.ENSP00000252999; -. DR ChEMBL; CHEMBL2364187; -. DR DrugBank; DB06245; Lanoteplase. DR UniLectin; O15230; -. DR CarbonylDB; O15230; -. DR GlyConnect; 1441; 26 N-Linked glycans (11 sites). DR GlyCosmos; O15230; 31 sites, 26 glycans. DR GlyGen; O15230; 34 sites, 26 N-linked glycans (11 sites), 3 O-linked glycans (9 sites). DR iPTMnet; O15230; -. DR PhosphoSitePlus; O15230; -. DR SwissPalm; O15230; -. DR BioMuta; LAMA5; -. DR jPOST; O15230; -. DR MassIVE; O15230; -. DR PaxDb; 9606-ENSP00000252999; -. DR PeptideAtlas; O15230; -. DR ProteomicsDB; 48522; -. [O15230-1] DR Pumba; O15230; -. DR Antibodypedia; 14779; 308 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 AGR; HGNC:6485; -. 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 MIM; 620049; phenotype. DR MIM; 620076; phenotype. 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; ISHCAAH; -. DR OrthoDB; 90222at2759; -. 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; 11 hits in 1156 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 183 other cell types or tissues. DR ExpressionAtlas; O15230; baseline and differential. 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:0098965; C:extracellular matrix of synaptic cleft; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. 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; IEA:Ensembl. 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:0005178; F:integrin binding; IDA:UniProtKB. 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: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; IEA:Ensembl. 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:0099173; P:postsynapse organization; 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:0048705; P:skeletal system morphogenesis; IMP:UniProtKB. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL. DR GO; GO:0036484; P:trunk neural crest cell migration; IEA:Ensembl. DR CDD; cd00055; EGF_Lam; 19. 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; 18. 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; IPR050440; Laminin/Netrin_ECM. 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 PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00052; Laminin_B; 1. DR Pfam; PF00053; Laminin_EGF; 20. DR Pfam; PF00054; Laminin_G_1; 1. 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 PRINTS; PR00011; EGFLAMININ. 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; Concanavalin A-like lectins/glucanases; 5. DR SUPFAM; SSF57196; EGF/Laminin; 19. 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; Disease variant; Disulfide bond; Extracellular matrix; KW Glycoprotein; Laminin EGF-like domain; Proteomics identification; KW 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 286 FT /note="R -> L (in NPHS26; dbSNP:rs962267864)" FT /evidence="ECO:0000269|PubMed:32439764" FT /id="VAR_087702" 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 498 FT /note="A -> V (in NPHS26; uncertain significance; FT dbSNP:rs139957521)" FT /evidence="ECO:0000269|PubMed:35419533" FT /id="VAR_087703" FT VARIANT 747 FT /note="R -> W (in NPHS26; uncertain significance; FT dbSNP:rs370940497)" FT /evidence="ECO:0000269|PubMed:29534211" FT /id="VAR_087704" FT VARIANT 889 FT /note="V -> M (in dbSNP:rs6062223)" FT /evidence="ECO:0000269|PubMed:11572484" FT /id="VAR_030847" FT VARIANT 1001 FT /note="E -> G (in NPHS26; uncertain significance; FT dbSNP:rs1601356283)" FT /evidence="ECO:0000269|PubMed:29534211" FT /id="VAR_087705" 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 1405 FT /note="A -> T (in BBDS2; uncertain significance; FT dbSNP:rs779995373)" FT /evidence="ECO:0000269|PubMed:33242826" FT /id="VAR_087706" 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 -> C (in BBDS2; uncertain significance; FT dbSNP:rs201815547)" FT /evidence="ECO:0000269|PubMed:33242826" FT /id="VAR_087707" 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 2720..3695 FT /note="Missing (in NPHS26)" FT /evidence="ECO:0000269|PubMed:35419533" FT /id="VAR_087708" FT VARIANT 2800 FT /note="R -> H (in NPHS26; uncertain significance; FT dbSNP:rs142801594)" FT /evidence="ECO:0000269|PubMed:35419533" FT /id="VAR_087709" FT VARIANT 2948 FT /note="G -> S (in NPHS26; uncertain significance; FT dbSNP:rs529211517)" FT /evidence="ECO:0000269|PubMed:29534211" FT /id="VAR_087710" FT VARIANT 3078..3695 FT /note="Missing (in NPHS26)" FT /evidence="ECO:0000269|PubMed:35419533" FT /id="VAR_087711" 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 //