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-MAR-2024, entry version 217.
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};
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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; 28.
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, 42 N-linked glycans (10 sites), 2 O-linked glycans (2 sites).
DR   iPTMnet; Q16363; -.
DR   PhosphoSitePlus; Q16363; -.
DR   SwissPalm; Q16363; -.
DR   BioMuta; LAMA4; -.
DR   DMDM; 292495093; -.
DR   EPD; Q16363; -.
DR   jPOST; Q16363; -.
DR   MassIVE; Q16363; -.
DR   MaxQB; 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; 430 antibodies from 29 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   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   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.
DR   Genevisible; Q16363; HS.
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; Reference proteome;
KW   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
//