ID LAMA4_HUMAN Reviewed; 1823 AA. AC Q16363; Q14731; Q14735; Q15335; Q4LE44; Q5SZG8; Q9BTB8; Q9UE18; Q9UJN9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 4. DT 27-NOV-2024, entry version 221. DE RecName: Full=Laminin subunit alpha-4; DE AltName: Full=Laminin-14 subunit alpha; DE AltName: Full=Laminin-8 subunit alpha; DE AltName: Full=Laminin-9 subunit alpha; DE Flags: Precursor; GN Name=LAMA4; 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 2), AND VARIANTS SER-1117 AND ARG-1119. RC TISSUE=Fetal lung; RX PubMed=7781776; DOI=10.1016/0014-5793(95)00462-i; RA Iivanainen A., Sainio K., Sariola H., Tryggvason K.; RT "Primary structure and expression of a novel human laminin alpha 4 chain."; RL FEBS Lett. 365:183-188(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-498; SER-1117; RP ARG-1119 AND SER-1549. RX PubMed=8706685; DOI=10.1111/j.1432-1033.1996.0813w.x; RA Richards A.J., Al-Imara L., Pope F.M.; RT "The complete cDNA sequence of laminin alpha 4 and its relationship to the RT other human laminin alpha chains."; RL Eur. J. Biochem. 238:813-821(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., RA Okazaki N., Koga H., Nagase T., Ohara O.; RT "Preparation of a set of expression-ready clones of mammalian long cDNAs RT encoding large proteins by the ORF trap cloning method."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Pancreas; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24. RC TISSUE=Heart; RX PubMed=9310354; DOI=10.1111/j.1432-1033.1997.t01-1-00015.x; RA Richards A.J., Luccarini C., Pope F.M.; RT "The structural organisation of LAMA4, the gene encoding laminin alpha4."; RL Eur. J. Biochem. 248:15-23(1997). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 236-1823 (ISOFORM 2), AND VARIANTS HIS-498; RP SER-1117 AND ARG-1119. RC TISSUE=Heart; RX PubMed=7959779; DOI=10.1006/geno.1994.1372; RA Richards A.J., Al-Imara L., Carter N.P., Lloyd J.C., Leversha M.A., RA Pope F.M.; RT "Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a RT partial cDNA encoding a variant laminin A chain."; RL Genomics 22:237-239(1994). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-557; ASN-578; ASN-581; ASN-742; RP ASN-787 AND ASN-810. 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 [10] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-39. RX PubMed=25326458; DOI=10.1074/mcp.m114.043703; RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L., RA Nilsson J., Larson G.; RT "Identification of chondroitin sulfate linkage region glycopeptides reveals RT prohormones as a novel class of proteoglycans."; RL Mol. Cell. Proteomics 14:41-49(2015). RN [11] RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-39. RX PubMed=32337544; DOI=10.1093/glycob/cwaa039; RA Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A., RA Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D., RA Larson G., Salanti A., Clausen T.M.; RT "An affinity chromatography and glycoproteomics workflow to profile the RT chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in RT the placenta and in cancer."; RL Glycobiology 30:989-1002(2020). RN [12] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-39. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). RN [13] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-39. RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617; RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.; RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected RT Correlation Between Glycan Sulfation and Attachment Site Characteristics."; RL Mol. Cell. Proteomics 22:100617-100617(2023). RN [14] RP VARIANT CMD1JJ LEU-950, AND CHARACTERIZATION OF VARIANT CMD1JJ LEU-950. RX PubMed=17646580; DOI=10.1161/circulationaha.107.689984; RA Knoell R., Postel R., Wang J., Kraetzner R., Hennecke G., Vacaru A.M., RA Vakeel P., Schubert C., Murthy K., Rana B.K., Kube D., Knoell G., RA Schaefer K., Hayashi T., Holm T., Kimura A., Schork N., Toliat M.R., RA Nuernberg P., Schultheiss H.P., Schaper W., Schaper J., Bos E., RA Den Hertog J., van Eeden F.J., Peters P.J., Hasenfuss G., Chien K.R., RA Bakkers J.; RT "Laminin-alpha4 and integrin-linked kinase mutations cause human RT cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial RT cells."; RL Circulation 116:515-525(2007). 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-4 is a CC subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and CC laminin-14 (laminin-423). CC -!- INTERACTION: CC Q16363-3; P05067: APP; NbExp=3; IntAct=EBI-17719490, EBI-77613; CC Q16363-3; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-17719490, EBI-10244780; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. Secreted {ECO:0000269|PubMed:25326458, CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=Major CC basement membrane component. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q16363-1; Sequence=Displayed; CC Name=2; CC IsoId=Q16363-2; Sequence=VSP_017542; CC Name=3; CC IsoId=Q16363-3; Sequence=VSP_038853, VSP_038854; CC -!- TISSUE SPECIFICITY: Detected in placenta (at protein level) CC (PubMed:32337544). Detected in fibroblasts and urine (at protein level) CC (PubMed:25326458, PubMed:36213313, PubMed:37453717). In adult, strong CC expression in heart, lung, ovary small and large intestines, placenta, CC liver; weak or no expression in skeletal muscle, kidney, pancreas, CC testis, prostate, brain. High expression in fetal lung and kidney. CC Expression in fetal and newborn tissues is observed in certain CC mesenchymal cells in tissues such as smooth muscle and dermis. CC {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:32337544, CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. 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: Domain G is globular. CC -!- DISEASE: Cardiomyopathy, dilated, 1JJ (CMD1JJ) [MIM:615235]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. {ECO:0000269|PubMed:17646580}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- CAUTION: Gene LAMA4 was formerly called LAMA3. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE06109.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; S78569; AAB34635.1; -; mRNA. DR EMBL; X91171; CAA62596.1; -; mRNA. DR EMBL; X70904; CAA50261.1; -; mRNA. DR EMBL; AB210027; BAE06109.1; ALT_INIT; mRNA. DR EMBL; BT006690; AAP35336.1; -; mRNA. DR EMBL; AL590106; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z99289; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004241; AAH04241.1; -; mRNA. DR EMBL; Y14240; CAA74636.1; -; Genomic_DNA. DR EMBL; X76939; CAA54258.1; -; mRNA. DR CCDS; CCDS34514.1; -. [Q16363-2] DR CCDS; CCDS43491.1; -. [Q16363-1] DR CCDS; CCDS43492.1; -. [Q16363-3] DR PIR; S68960; S68960. DR RefSeq; NP_001098676.2; NM_001105206.2. DR RefSeq; NP_001098677.2; NM_001105207.2. DR RefSeq; NP_001098678.1; NM_001105208.2. [Q16363-3] DR RefSeq; NP_001098679.1; NM_001105209.2. [Q16363-3] DR RefSeq; NP_002281.3; NM_002290.4. DR RefSeq; XP_005267040.2; XM_005266983.3. DR RefSeq; XP_005267041.2; XM_005266984.3. DR AlphaFoldDB; Q16363; -. DR SMR; Q16363; -. DR BioGRID; 110104; 37. DR ComplexPortal; CPX-1777; Laminin-411 complex. DR ComplexPortal; CPX-1778; Laminin-421 complex. DR ComplexPortal; CPX-1782; Laminin-423 complex. DR CORUM; Q16363; -. DR IntAct; Q16363; 35. DR MINT; Q16363; -. DR STRING; 9606.ENSP00000230538; -. DR ChEMBL; CHEMBL2364187; -. DR GlyConnect; 1440; 42 N-Linked glycans (10 sites). DR GlyCosmos; Q16363; 20 sites, 43 glycans. DR GlyGen; Q16363; 22 sites, 150 N-linked glycans (11 sites), 2 O-linked glycans (2 sites). DR iPTMnet; Q16363; -. DR PhosphoSitePlus; Q16363; -. DR SwissPalm; Q16363; -. DR BioMuta; LAMA4; -. DR DMDM; 292495093; -. DR jPOST; Q16363; -. DR MassIVE; Q16363; -. DR PaxDb; 9606-ENSP00000230538; -. DR PeptideAtlas; Q16363; -. DR ProteomicsDB; 60862; -. [Q16363-1] DR ProteomicsDB; 60863; -. [Q16363-2] DR ProteomicsDB; 60864; -. [Q16363-3] DR Pumba; Q16363; -. DR Antibodypedia; 2846; 357 antibodies from 28 providers. DR DNASU; 3910; -. DR Ensembl; ENST00000368638.5; ENSP00000357627.4; ENSG00000112769.20. [Q16363-3] DR Ensembl; ENST00000453937.2; ENSP00000398226.2; ENSG00000112769.20. [Q16363-3] DR Ensembl; ENST00000455073.1; ENSP00000408604.1; ENSG00000112769.20. [Q16363-3] DR GeneID; 3910; -. DR KEGG; hsa:3910; -. DR UCSC; uc010kdz.3; human. [Q16363-1] DR AGR; HGNC:6484; -. DR CTD; 3910; -. DR DisGeNET; 3910; -. DR GeneCards; LAMA4; -. DR HGNC; HGNC:6484; LAMA4. DR HPA; ENSG00000112769; Low tissue specificity. DR MalaCards; LAMA4; -. DR MIM; 600133; gene. DR MIM; 615235; phenotype. DR neXtProt; NX_Q16363; -. DR OpenTargets; ENSG00000112769; -. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR PharmGKB; PA30273; -. DR VEuPathDB; HostDB:ENSG00000112769; -. DR eggNOG; KOG1836; Eukaryota. DR GeneTree; ENSGT00940000159970; -. DR HOGENOM; CLU_2095989_0_0_1; -. DR InParanoid; Q16363; -. DR OrthoDB; 90222at2759; -. DR PhylomeDB; Q16363; -. DR TreeFam; TF335359; -. DR PathwayCommons; Q16363; -. 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-8874081; MET activates PTK2 signaling. DR SignaLink; Q16363; -. DR SIGNOR; Q16363; -. DR BioGRID-ORCS; 3910; 12 hits in 1156 CRISPR screens. DR ChiTaRS; LAMA4; human. DR GeneWiki; Laminin,_alpha_4; -. DR GenomeRNAi; 3910; -. DR Pharos; Q16363; Tbio. DR PRO; PR:Q16363; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q16363; protein. DR Bgee; ENSG00000112769; Expressed in lower esophagus muscularis layer and 183 other cell types or tissues. DR ExpressionAtlas; Q16363; baseline and differential. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL. DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab. 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 CDD; cd00055; EGF_Lam; 3. DR CDD; cd00110; LamG; 5. DR FunFam; 2.10.25.10:FF:000051; Laminin subunit alpha 4; 1. DR FunFam; 2.10.25.10:FF:000491; Laminin subunit alpha 4; 1. DR FunFam; 2.10.25.10:FF:000569; Laminin subunit alpha 4; 1. DR FunFam; 2.60.120.200:FF:000053; Laminin subunit alpha 4; 1. DR FunFam; 2.60.120.200:FF:000058; Laminin subunit alpha 4; 1. DR FunFam; 2.60.120.200:FF:000064; Laminin subunit alpha 4; 1. DR FunFam; 2.60.120.200:FF:000066; Laminin subunit alpha 4; 1. DR FunFam; 2.60.120.200:FF:000087; Laminin subunit alpha 4; 1. DR Gene3D; 2.60.120.200; -; 5. DR Gene3D; 2.10.25.10; Laminin; 3. 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; IPR002049; LE_dom. DR InterPro; IPR050372; Neurexin-related_CASP. DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1. DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1. DR Pfam; PF00053; Laminin_EGF; 3. DR Pfam; PF02210; Laminin_G_2; 5. DR Pfam; PF06008; Laminin_I; 1. DR Pfam; PF06009; Laminin_II; 1. DR SMART; SM00181; EGF; 3. DR SMART; SM00180; EGF_Lam; 3. DR SMART; SM00282; LamG; 5. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5. DR SUPFAM; SSF57196; EGF/Laminin; 3. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01248; EGF_LAM_1; 3. DR PROSITE; PS50027; EGF_LAM_2; 3. DR PROSITE; PS50025; LAM_G_DOMAIN; 5. PE 1: Evidence at protein level; KW Alternative splicing; Basement membrane; Cardiomyopathy; Cell adhesion; KW Coiled coil; Disease variant; Disulfide bond; Extracellular matrix; KW Glycoprotein; Laminin EGF-like domain; Proteoglycan; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..1823 FT /note="Laminin subunit alpha-4" FT /id="PRO_0000017060" FT DOMAIN 82..131 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 132..186 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 187..240 FT /note="Laminin EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 241..255 FT /note="Laminin EGF-like 4; truncated" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 833..1035 FT /note="Laminin G-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 1047..1227 FT /note="Laminin G-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 1234..1402 FT /note="Laminin G-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 1469..1640 FT /note="Laminin G-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 1647..1820 FT /note="Laminin G-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT REGION 256..832 FT /note="Domain II and I" FT REGION 1419..1440 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 320..403 FT /evidence="ECO:0000255" FT COILED 473..528 FT /evidence="ECO:0000255" FT COILED 581..614 FT /evidence="ECO:0000255" FT COILED 662..724 FT /evidence="ECO:0000255" FT COILED 777..806 FT /evidence="ECO:0000255" FT MOTIF 724..726 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT CARBOHYD 39 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458, FT ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313, FT ECO:0000269|PubMed:37453717" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 215 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 315 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 465 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 531 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 557 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 578 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 581 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 638 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 646 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 742 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 758 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 761 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 787 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 810 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1093 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1288 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1366 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1418 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 82..91 FT /evidence="ECO:0000250" FT DISULFID 84..98 FT /evidence="ECO:0000250" FT DISULFID 101..110 FT /evidence="ECO:0000250" FT DISULFID 113..129 FT /evidence="ECO:0000250" FT DISULFID 132..146 FT /evidence="ECO:0000250" FT DISULFID 134..155 FT /evidence="ECO:0000250" FT DISULFID 157..166 FT /evidence="ECO:0000250" FT DISULFID 169..184 FT /evidence="ECO:0000250" FT DISULFID 187..202 FT /evidence="ECO:0000250" FT DISULFID 189..209 FT /evidence="ECO:0000250" FT DISULFID 212..221 FT /evidence="ECO:0000250" FT DISULFID 224..238 FT /evidence="ECO:0000250" FT DISULFID 273 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 276 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1005..1035 FT /evidence="ECO:0000250" FT DISULFID 1201..1227 FT /evidence="ECO:0000250" FT DISULFID 1370..1402 FT /evidence="ECO:0000250" FT DISULFID 1617..1640 FT /evidence="ECO:0000250" FT DISULFID 1792..1820 FT /evidence="ECO:0000250" FT VAR_SEQ 66..120 FT /note="KCNAGFFHTLSGECVPCDCNGNSNECLDGSGYCVHCQRNTTGEHCEKCLDGY FT IGD -> VQCPCHCHPAGAPAPPRAVPHSSFSLSPPLSSPQCLESFTWARSVRKLEIKS FT FPL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_038853" FT VAR_SEQ 121..1823 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_038854" FT VAR_SEQ 266..272 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7781776, FT ECO:0000303|PubMed:7959779, ECO:0000303|PubMed:8706685" FT /id="VSP_017542" FT VARIANT 94 FT /note="G -> S (in dbSNP:rs35349917)" FT /id="VAR_056140" FT VARIANT 154 FT /note="R -> W (in dbSNP:rs11757455)" FT /id="VAR_056141" FT VARIANT 283 FT /note="A -> E (in dbSNP:rs9400522)" FT /id="VAR_061348" FT VARIANT 492 FT /note="L -> H (in dbSNP:rs3752579)" FT /id="VAR_056142" FT VARIANT 498 FT /note="Y -> H (in dbSNP:rs1050348)" FT /evidence="ECO:0000269|PubMed:7959779, FT ECO:0000269|PubMed:8706685" FT /id="VAR_025550" FT VARIANT 950 FT /note="P -> L (in CMD1JJ; loss of integrin-binding FT capacity)" FT /evidence="ECO:0000269|PubMed:17646580" FT /id="VAR_069708" FT VARIANT 1117 FT /note="G -> S (in dbSNP:rs2032567)" FT /evidence="ECO:0000269|PubMed:7781776, FT ECO:0000269|PubMed:7959779, ECO:0000269|PubMed:8706685" FT /id="VAR_025551" FT VARIANT 1119 FT /note="P -> R (in dbSNP:rs1050349)" FT /evidence="ECO:0000269|PubMed:7781776, FT ECO:0000269|PubMed:7959779, ECO:0000269|PubMed:8706685" FT /id="VAR_025552" FT VARIANT 1549 FT /note="N -> S (in dbSNP:rs12110554)" FT /evidence="ECO:0000269|PubMed:8706685" FT /id="VAR_056143" FT VARIANT 1815 FT /note="V -> I (in dbSNP:rs3734292)" FT /id="VAR_056144" FT CONFLICT 143 FT /note="A -> P (in Ref. 1; AAB34635)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="L -> F (in Ref. 1; AAB34635)" FT /evidence="ECO:0000305" FT CONFLICT 283 FT /note="A -> D (in Ref. 1; AAB34635, 2; CAA62596, 3; FT BAE06109 and 8; CAA54258)" FT /evidence="ECO:0000305" FT CONFLICT 1064 FT /note="T -> P (in Ref. 1; AAB34635)" FT /evidence="ECO:0000305" SQ SEQUENCE 1823 AA; 202524 MW; 25BFB6120C2A86F1 CRC64; MALSSAWRSV LPLWLLWSAA CSRAASGDDN AFPFDIEGSS AVGRQDPPET SEPRVALGRL PPAAEKCNAG FFHTLSGECV PCDCNGNSNE CLDGSGYCVH CQRNTTGEHC EKCLDGYIGD SIRGAPQFCQ PCPCPLPHLA NFAESCYRKN GAVRCICNEN YAGPNCERCA PGYYGNPLLI GSTCKKCDCS GNSDPNLIFE DCDEVTGQCR NCLRNTTGFK CERCAPGYYG DARIAKNCAV CNCGGGPCDS VTGECLEEGF EPPTGMDCPT ISCDKCVWDL TDALRLAALS IEEGKSGVLS VSSGAAAHRH VNEINATIYL LKTKLSEREN QYALRKIQIN NAENTMKSLL SDVEELVEKE NQASRKGQLV QKESMDTINH ASQLVEQAHD MRDKIQEINN KMLYYGEEHE LSPKEISEKL VLAQKMLEEI RSRQPFFTQR ELVDEEADEA YELLSQAESW QRLHNETRTL FPVVLEQLDD YNAKLSDLQE ALDQALNYVR DAEDMNRATA ARQRDHEKQQ ERVREQMEVV NMSLSTSADS LTTPRLTLSE LDDIIKNASG IYAEIDGAKS ELQVKLSNLS NLSHDLVQEA IDHAQDLQQE ANELSRKLHS SDMNGLVQKA LDASNVYENI VNYVSEANET AEFALNTTDR IYDAVSGIDT QIIYHKDESE NLLNQARELQ AKAESSSDEA VADTSRRVGG ALARKSALKT RLSDAVKQLQ AAERGDAQQR LGQSRLITEE ANRTTMEVQQ ATAPMANNLT NWSQNLQHFD SSAYNTAVNS ARDAVRNLTE VVPQLLDQLR TVEQKRPASN VSASIQRIRE LIAQTRSVAS KIQVSMMFDG QSAVEVHSRT SMDDLKAFTS LSLYMKPPVK RPELTETADQ FILYLGSKNA KKEYMGLAIK NDNLVYVYNL GTKDVEIPLD SKPVSSWPAY FSIVKIERVG KHGKVFLTVP SLSSTAEEKF IKKGEFSGDD SLLDLDPEDT VFYVGGVPSN FKLPTSLNLP GFVGCLELAT LNNDVISLYN FKHIYNMDPS TSVPCARDKL AFTQSRAASY FFDGSGYAVV RDITRRGKFG QVTRFDIEVR TPADNGLILL MVNGSMFFRL EMRNGYLHVF YDFGFSGGPV HLEDTLKKAQ INDAKYHEIS IIYHNDKKMI LVVDRRHVKS MDNEKMKIPF TDIYIGGAPP EILQSRALRA HLPLDINFRG CMKGFQFQKK DFNLLEQTET LGVGYGCPED SLISRRAYFN GQSFIASIQK ISFFDGFEGG FNFRTLQPNG LLFYYASGSD VFSISLDNGT VIMDVKGIKV QSVDKQYNDG LSHFVISSVS PTRYELIVDK SRVGSKNPTK GKIEQTQASE KKFYFGGSPI SAQYANFTGC ISNAYFTRVD RDVEVEDFQR YTEKVHTSLY ECPIESSPLF LLHKKGKNLS KPKASQNKKG GKSKDAPSWD PVALKLPERN TPRNSHCHLS NSPRAIEHAY QYGGTANSRQ EFEHLKGDFG AKSQFSIRLR TRSSHGMIFY VSDQEENDFM TLFLAHGRLV YMFNVGHKKL KIRSQEKYND GLWHDVIFIR ERSSGRLVID GLRVLEESLP PTEATWKIKG PIYLGGVAPG KAVKNVQINS IYSFSGCLSN LQLNGASITS ASQTFSVTPC FEGPMETGTY FSTEGGYVVL DESFNIGLKF EIAFEVRPRS SSGTLVHGHS VNGEYLNVHM KNGQVIVKVN NGIRDFSTSV TPKQSLCDGR WHRITVIRDS NVVQLDVDSE VNHVVGPLNP KPIDHREPVF VGGVPESLLT PRLAPSKPFT GCIRHFVIDG HPVSFSKAAL VSGAVSINSC PAA //