ID LAMA2_HUMAN Reviewed; 3122 AA. AC P24043; Q14736; Q5VUM2; Q93022; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 4. DT 02-SEP-2026, entry version 242. DE RecName: Full=Laminin subunit alpha-2; DE AltName: Full=Laminin M chain; DE AltName: Full=Laminin-12 subunit alpha; DE AltName: Full=Laminin-2 subunit alpha; DE AltName: Full=Laminin-4 subunit alpha; DE AltName: Full=Merosin heavy chain; DE Flags: Precursor; GN Name=LAMA2; Synonyms=LAMM; 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], AND VARIANT VAL-2587. RC TISSUE=Placenta; RX PubMed=8294519; DOI=10.1083/jcb.124.3.381; RA Vuolteenaho R., Nissinen M., Sainio K., Byers M., Eddy R., Hirvonen H., RA Shows T.B., Sariola H., Engvall E., Tryggvason K.; RT "Human laminin M chain (merosin): complete primary structure, chromosomal RT assignment, and expression of the M and A chain in human fetal tissues."; RL J. Cell Biol. 124:381-394(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-2587. RX PubMed=8910357; DOI=10.1074/jbc.271.44.27664; RA Zhang X., Vuolteenaho R., Tryggvason K.; RT "Structure of the human laminin alpha2-chain gene (LAMA2), which is RT affected in congenital muscular dystrophy."; RL J. Biol. Chem. 271:27664-27669(1996). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1360-3122. RX PubMed=7535762; DOI=10.1093/oxfordjournals.jbchem.a124666; RA Hori H., Kanamori T., Mizuta T., Yamaguchi N., Liu Y., Nagai Y.; RT "Human laminin M chain: epitope analysis of its monoclonal antibodies by RT immunoscreening of cDNA clones and tissue expression."; RL J. Biochem. 116:1212-1219(1994). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1981-3122, PARTIAL PROTEIN SEQUENCE, AND RP VARIANT VAL-2587. RC TISSUE=Placenta; RX PubMed=2185464; DOI=10.1073/pnas.87.9.3264; RA Ehrig K., Leivo I., Argraves W.S., Ruoslahti E., Engvall E.; RT "Merosin, a tissue-specific basement membrane protein, is a laminin-like RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3264-3268(1990). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1901; ASN-1916; ASN-1920; RP ASN-2017 AND ASN-2648. 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 [8] RP INVOLVEMENT IN LGMDR23, AND VARIANTS LGMDR23 GLY-152; PRO-243; ARG-284 AND RP SER-2477. RX PubMed=21953594; DOI=10.1002/mus.22132; RA Gavassini B.F., Carboni N., Nielsen J.E., Danielsen E.R., Thomsen C., RA Svenstrup K., Bello L., Maioli M.A., Marrosu G., Ticca A.F., Mura M., RA Marrosu M.G., Soraru G., Angelini C., Vissing J., Pegoraro E.; RT "Clinical and molecular characterization of limb-girdle muscular dystrophy RT due to LAMA2 mutations."; RL Muscle Nerve 44:703-709(2011). RN [9] RP INVOLVEMENT IN LGMDR23, VARIANTS LGMDR23 131-GLN--ASN-3122 DEL AND RP VAL-1496, AND VARIANT SER-199. RX PubMed=24957499; DOI=10.1016/j.nmd.2014.05.008; RA Chan S.H., Foley A.R., Phadke R., Mathew A.A., Pitt M., Sewry C., RA Muntoni F.; RT "Limb girdle muscular dystrophy due to LAMA2 mutations: diagnostic RT difficulties due to associated peripheral neuropathy."; RL Neuromuscul. Disord. 24:677-683(2014). RN [10] RP INVOLVEMENT IN MDC1A, AND VARIANTS MDC1A 95-GLN--ASN-3122 DEL; RP 110-TRP--ASN-3122 DEL; 121-TYR--ASN-3122 DEL; 273-ARG--ASN-3122 DEL; RP 435-ARG--ASN-3122 DEL; TYR-518; 659-SER--ASN-3122 DEL; 744-ARG--ASN-3122 RP DEL; MET-821; 986-TRP--ASN-3122 DEL; 1032-CYS--ASN-3122 DEL; RP 1095-ARG--ASN-3122 DEL; GLY-1311; 1319-ARG--ASN-3122 DEL; RP 1350-ARG--ASN-3122 DEL; 1826-ARG--ASN-3122 DEL; VAL-2172 DEL; RP 2383-ARG--ASN-3122 DEL; 2578-ARG--ASN-3122 DEL; 2604-ARG--ASN-3122 DEL; RP ALA-2633; 2641-GLU--ASN-3122 DEL AND 2755-SER--ASN-3122 DEL. RX PubMed=24611677; DOI=10.1111/cge.12366; RA Xiong H., Tan D., Wang S., Song S., Yang H., Gao K., Liu A., Jiao H., RA Mao B., Ding J., Chang X., Wang J., Wu Y., Yuan Y., Jiang Y., Zhang F., RA Wu H., Wu X.; RT "Genotype/phenotype analysis in Chinese laminin-alpha2 deficient congenital RT muscular dystrophy patients."; RL Clin. Genet. 87:233-243(2015). RN [11] RP VARIANTS GLN-545; HIS-619; LEU-919; HIS-2586 AND LYS-2614. RA Panicker S.G., Mendell J.T., Chen L., Feng B., Sahenk Z., Marzluf G.A., RA Amato A.A., Mendell J.R.; RT "Novel single base polymorphisms and rare sequence variants in the laminin RT 2-chain coding region detected by RNA/SSCP analysis."; RL Hum. Mutat. 13:174-174(1999). RN [12] RP VARIANT MDC1A PRO-2564. RX PubMed=11591858; DOI=10.1212/wnl.57.7.1319; RA He Y., Jones K.J., Vignier N., Morgan G., Chevallay M., Barois A., RA Estournet-Mathiaud B., Hori H., Mizuta T., Tome F.M.S., North K.N., RA Guicheney P.; RT "Congenital muscular dystrophy with primary partial laminin alpha-2 chain RT deficiency: molecular study."; RL Neurology 57:1319-1322(2001). RN [13] RP VARIANTS MDC1A TYR-527 AND ARG-862. RX PubMed=12552556; DOI=10.1002/humu.10157; RA Tezak Z., Prandini P., Boscaro M., Marin A., Devaney J., Marino M., RA Fanin M., Trevisan C.P., Park J., Tyson W., Finkel R., Garcia C., RA Angelini C., Hoffman E.P., Pegoraro E.; RT "Clinical and molecular study in congenital muscular dystrophy with partial RT laminin alpha-2 (LAMA2) deficiency."; RL Hum. Mutat. 21:103-111(2003). RN [14] RP VARIANT [LARGE SCALE ANALYSIS] ALA-1160. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [15] RP VARIANT MDC1A ARG-2889. RX PubMed=27234031; DOI=10.1111/cge.12810; RA Fattahi Z., Kalhor Z., Fadaee M., Vazehan R., Parsimehr E., Abolhassani A., RA Beheshtian M., Zamani G., Nafissi S., Nilipour Y., Akbari M.R., Kahrizi K., RA Kariminejad A., Najmabadi H.; RT "Improved diagnostic yield of neuromuscular disorders applying clinical RT exome sequencing in patients arising from a consanguineous population."; RL Clin. Genet. 91:386-402(2017). 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-2 is a CC subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 CC or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 CC and NID2. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. Note=Major component. CC -!- TISSUE SPECIFICITY: Placenta, striated muscle, peripheral nerve, CC cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, CC testis, meninges, choroid plexus, and some other regions of the brain; CC not in liver, thymus and bone. CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with CC other laminin chains to form a coiled coil structure. CC -!- DOMAIN: Domains VI, IV and G are globular. CC -!- DISEASE: Merosin-deficient congenital muscular dystrophy 1A (MDC1A) CC [MIM:607855]: Characterized by difficulty walking, hypotonia, proximal CC weakness, hyporeflexia, and white matter hypodensity on MRI. CC {ECO:0000269|PubMed:11591858, ECO:0000269|PubMed:12552556, CC ECO:0000269|PubMed:24611677, ECO:0000269|PubMed:27234031}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 23 CC (LGMDR23) [MIM:618138]: A form of autosomal recessive limb-girdle CC muscular dystrophy, a myopathy characterized by proximal and/or distal CC muscle weakness and atrophy. The age at onset is variable and can range CC from the first to the sixth decade, although later onset is less CC common. LGMDR23 is characterized by slowly progressive proximal muscle CC weakness primarily affecting the lower limbs, increased serum creatine CC kinase, dystrophic features, gait difficulties, and white matter CC abnormalities on brain imaging. Age at onset generally ranges from CC childhood to mid-adulthood. Some patients may have additional CC neurologic features, including executive deficits, seizures, and CC peripheral neuropathy. {ECO:0000269|PubMed:21953594, CC ECO:0000269|PubMed:24957499}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAA63215.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAB18388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAA81394.1; Type=Frameshift; 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; Z26653; CAA81394.1; ALT_FRAME; mRNA. DR EMBL; U66796; AAB18388.1; ALT_SEQ; Genomic_DNA. DR EMBL; U66733; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66734; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66735; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66736; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66737; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66738; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66739; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66740; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66741; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66742; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66743; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66745; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66746; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66747; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66748; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66749; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66750; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66751; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66752; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66753; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66754; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66755; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66756; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66757; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66758; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66759; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66760; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66761; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66762; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66763; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66764; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66765; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66766; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66768; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66769; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66770; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66771; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66772; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66773; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66774; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66775; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66776; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66777; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66778; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66779; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66780; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66781; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66782; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66783; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66784; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66785; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66786; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66787; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66788; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66789; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66790; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66791; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66792; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66793; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66794; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; U66795; AAB18388.1; JOINED; Genomic_DNA. DR EMBL; AL583853; CAH70492.1; -; Genomic_DNA. DR EMBL; AL356124; CAH70492.1; JOINED; Genomic_DNA. DR EMBL; AL445439; CAH70492.1; JOINED; Genomic_DNA. DR EMBL; AL513527; CAH70492.1; JOINED; Genomic_DNA. DR EMBL; AL590613; CAH70492.1; JOINED; Genomic_DNA. DR EMBL; AL669984; CAH70492.1; JOINED; Genomic_DNA. DR EMBL; AL590613; CAH70771.1; -; Genomic_DNA. DR EMBL; AL356124; CAH70771.1; JOINED; Genomic_DNA. DR EMBL; AL445439; CAH70771.1; JOINED; Genomic_DNA. DR EMBL; AL513527; CAH70771.1; JOINED; Genomic_DNA. DR EMBL; AL583853; CAH70771.1; JOINED; Genomic_DNA. DR EMBL; AL669984; CAH70771.1; JOINED; Genomic_DNA. DR EMBL; AL445439; CAH72952.1; -; Genomic_DNA. DR EMBL; AL356124; CAH72952.1; JOINED; Genomic_DNA. DR EMBL; AL513527; CAH72952.1; JOINED; Genomic_DNA. DR EMBL; AL583853; CAH72952.1; JOINED; Genomic_DNA. DR EMBL; AL590613; CAH72952.1; JOINED; Genomic_DNA. DR EMBL; AL669984; CAH72952.1; JOINED; Genomic_DNA. DR EMBL; AL513527; CAI15185.1; -; Genomic_DNA. DR EMBL; AL356124; CAI15185.1; JOINED; Genomic_DNA. DR EMBL; AL445439; CAI15185.1; JOINED; Genomic_DNA. DR EMBL; AL583853; CAI15185.1; JOINED; Genomic_DNA. DR EMBL; AL590613; CAI15185.1; JOINED; Genomic_DNA. DR EMBL; AL669984; CAI15185.1; JOINED; Genomic_DNA. DR EMBL; AL669984; CAI16682.1; -; Genomic_DNA. DR EMBL; AL356124; CAI16682.1; JOINED; Genomic_DNA. DR EMBL; AL445439; CAI16682.1; JOINED; Genomic_DNA. DR EMBL; AL513527; CAI16682.1; JOINED; Genomic_DNA. DR EMBL; AL583853; CAI16682.1; JOINED; Genomic_DNA. DR EMBL; AL590613; CAI16682.1; JOINED; Genomic_DNA. DR EMBL; AL356124; CAI22470.1; -; Genomic_DNA. DR EMBL; AL445439; CAI22470.1; JOINED; Genomic_DNA. DR EMBL; AL513527; CAI22470.1; JOINED; Genomic_DNA. DR EMBL; AL583853; CAI22470.1; JOINED; Genomic_DNA. DR EMBL; AL590613; CAI22470.1; JOINED; Genomic_DNA. DR EMBL; AL669984; CAI22470.1; JOINED; Genomic_DNA. DR EMBL; AL589927; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M59832; AAA63215.1; ALT_FRAME; mRNA. DR CCDS; CCDS5138.1; -. DR PIR; PX0082; MMHUMH. DR RefSeq; NP_000417.3; NM_000426.4. DR RefSeq; NP_001073291.2; NM_001079823.2. DR PDB; 4YEP; X-ray; 1.19 A; A/B=1181-1362. DR PDB; 4YEQ; X-ray; 3.20 A; U=1177-1379. DR SMR; P24043; -. DR BioGRID; 110102; 29. DR ComplexPortal; CPX-1771; Laminin-211 complex. DR ComplexPortal; CPX-1773; Laminin-221 complex. DR ComplexPortal; CPX-1781; Laminin-213 complex. DR DIP; DIP-42562N; -. DR FunCoup; P24043; 607. DR IntAct; P24043; 14. DR MINT; P24043; -. DR NDEx; IQUERY-CP-LAMA2; 14 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000400365; -. DR ChEMBL; CHEMBL2364187; -. DR UniLectin; P24043; -. DR GlyConnect; P24043; 42 N-Linked glycans (20 sites). DR GlyCosmos; P24043; 31 sites, 40 glycans. DR GlyGen; P24043; 35 sites, 112 N-linked glycans (22 sites), 2 O-linked glycans (4 sites). DR iPTMnet; P24043; -. DR PhosphoSitePlus; P24043; -. DR BioMuta; LAMA2; -. DR DMDM; 215274259; -. DR jPOST; P24043; -. DR MassIVE; P24043; -. DR PaxDb; 9606-ENSP00000400365; -. DR PeptideAtlas; P24043; -. DR ProteomicsDB; 54178; -. DR ABCD; P24043; 1 sequenced antibody. DR Antibodypedia; 763; 210 antibodies from 35 providers. DR DNASU; 3908; -. DR Ensembl; ENST00000421865.3; ENSP00000400365.2; ENSG00000196569.14. DR GeneID; 3908; -. DR KEGG; hsa:3908; -. DR MANE-Select; ENST00000421865.3; ENSP00000400365.2; NM_000426.4; NP_000417.3. DR UCSC; uc063rgy.1; human. DR AGR; HGNC:6482; -. DR ClinPGx; PA30271; -. DR CTD; 3908; -. DR DisGeNET; 3908; -. DR GeneCards; LAMA2; -. DR GeneReviews; LAMA2; -. DR HGNC; HGNC:6482; LAMA2. DR HPA; ENSG00000196569; Tissue enhanced (placenta). DR MalaCards; LAMA2; -. DR MIM; 156225; gene. DR MIM; 607855; phenotype. DR MIM; 618138; phenotype. DR OpenTargets; ENSG00000196569; -. DR Orphanet; 258; Laminin subunit alpha 2-related congenital muscular dystrophy. DR Orphanet; 565837; Laminin subunit alpha 2-related limb-girdle muscular dystrophy R23. DR VEuPathDB; HostDB:ENSG00000196569; -. DR eggNOG; KOG1836; Eukaryota. DR GeneTree; ENSGT00940000155362; -. DR InParanoid; P24043; -. DR OMA; SHSRINF; -. DR OrthoDB; 10011303at2759; -. DR PAN-GO; P24043; 5 GO annotations based on evolutionary models. DR PhylomeDB; P24043; -. DR PathwayCommons; P24043; -. 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 Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination. DR Reactome; R-HSA-9638630; Attachment of bacteria to epithelial cells. DR Reactome; R-HSA-9913351; Formation of the dystrophin-glycoprotein complex (DGC). DR Reactome; R-HSA-9925563; Developmental Lineage of Pancreatic Ductal Cells. DR SignaLink; P24043; -. DR SIGNOR; P24043; -. DR Agora; ENSG00000196569; -. DR BioGRID-ORCS; 3908; 10 hits in 1158 CRISPR screens. DR ChiTaRS; LAMA2; human. DR EvolutionaryTrace; P24043; -. DR GeneWiki; Laminin,_alpha_2; -. DR GenomeRNAi; 3908; -. DR Pharos; P24043; Tbio. DR PRO; PR:P24043; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P24043; protein. DR Bgee; ENSG00000196569; Expressed in mucosa of stomach and 199 other cell types or tissues. DR ExpressionAtlas; P24043; baseline and differential. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005607; C:laminin-211 trimer; TAS:GO_Central. DR GO; GO:0043261; C:laminin-213 trimer; TAS:GO_Central. DR GO; GO:0005609; C:laminin-221 trimer; TAS:GO_Central. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl. DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0045785; P:positive regulation of cell adhesion; NAS:ComplexPortal. DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; NAS:ComplexPortal. DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal. DR GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal. 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:0014037; P:Schwann cell differentiation; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd00055; EGF_Lam; 15. DR CDD; cd00110; LamG; 5. DR FunFam; 2.10.25.10:FF:000106; Heparan sulfate proteoglycan 2; 1. DR FunFam; 2.10.25.10:FF:000074; Laminin subunit alpha; 1. DR FunFam; 2.10.25.10:FF:000069; Laminin subunit alpha 1; 1. DR FunFam; 2.10.25.10:FF:000082; Laminin subunit alpha 1; 1. DR FunFam; 2.10.25.10:FF:000242; Laminin subunit alpha 1; 1. DR FunFam; 2.10.25.10:FF:000512; Laminin subunit alpha 1; 1. DR FunFam; 1.10.287.950:FF:000005; Laminin subunit alpha 2; 1. DR FunFam; 2.10.25.10:FF:000189; Laminin subunit alpha 2; 1. DR FunFam; 2.10.25.10:FF:000250; Laminin subunit alpha 2; 1. DR FunFam; 2.10.25.10:FF:000315; Laminin subunit alpha 2; 1. DR FunFam; 2.170.300.10:FF:000008; Laminin subunit alpha 2; 1. DR FunFam; 2.60.120.200:FF:000052; Laminin subunit alpha 2; 1. DR FunFam; 2.60.120.200:FF:000057; Laminin subunit alpha 2; 1. DR FunFam; 2.60.120.200:FF:000061; Laminin subunit alpha 2; 1. DR FunFam; 2.60.120.200:FF:000063; Laminin subunit alpha 2; 1. DR FunFam; 2.60.120.200:FF:000065; Laminin subunit alpha 2; 1. DR FunFam; 2.60.120.260:FF:000017; Laminin subunit alpha 2; 1. DR FunFam; 2.10.25.10:FF:000051; Laminin subunit alpha 4; 1. DR FunFam; 2.10.25.10:FF:000094; Laminin subunit alpha-2; 1. DR FunFam; 2.10.25.10:FF:000128; laminin subunit alpha-2 isoform X1; 2. DR FunFam; 2.10.25.10:FF:000461; laminin subunit alpha-2 isoform X1; 1. DR FunFam; 2.170.300.10:FF:000026; laminin subunit alpha-2 isoform X2; 1. 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; 13. DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000742; EGF. DR InterPro; IPR050440; Laminin/Netrin_ECM. DR InterPro; IPR009254; Laminin_aI. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR000034; Laminin_IV. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR002049; LE_dom. DR InterPro; IPR056863; LMN_ATRN_NET-like_EGF. DR PANTHER; PTHR10574:SF291; LAMININ SUBUNIT ALPHA-2; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00053; EGF_laminin; 13. DR Pfam; PF24973; EGF_LMN_ATRN; 2. DR Pfam; PF00052; Laminin_B; 2. DR Pfam; PF00054; Laminin_G_1; 4. DR Pfam; PF02210; Laminin_G_2; 1. DR Pfam; PF06008; Laminin_I; 1. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00181; EGF; 8. DR SMART; SM00180; EGF_Lam; 16. DR SMART; SM00281; LamB; 2. DR SMART; SM00282; LamG; 5. DR SMART; SM00136; LamNT; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5. DR SUPFAM; SSF57196; EGF/Laminin; 13. DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1. DR PROSITE; PS00022; EGF_1; 11. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS01248; EGF_LAM_1; 14. DR PROSITE; PS50027; EGF_LAM_2; 15. DR PROSITE; PS50025; LAM_G_DOMAIN; 5. DR PROSITE; PS51115; LAMININ_IVA; 2. DR PROSITE; PS51117; LAMININ_NTER; 1. DR PDBsum; 4YEP; -. DR PDBsum; 4YEQ; -. PE 1: Evidence at protein level; KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil; KW Congenital muscular dystrophy; Direct protein sequencing; Disease variant; KW Disulfide bond; Extracellular matrix; Glycoprotein; KW Laminin EGF-like domain; Limb-girdle muscular dystrophy; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..3122 FT /note="Laminin subunit alpha-2" FT /id="PRO_0000017056" FT DOMAIN 35..286 FT /note="Laminin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466" FT DOMAIN 287..343 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 344..413 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 414..468 FT /note="Laminin EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 469..517 FT /note="Laminin EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 518..527 FT /note="Laminin EGF-like 5; first part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 531..723 FT /note="Laminin IV type A 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458" FT DOMAIN 724..756 FT /note="Laminin EGF-like 5; second part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 757..806 FT /note="Laminin EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 807..864 FT /note="Laminin EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 865..917 FT /note="Laminin EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 918..966 FT /note="Laminin EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 967..1013 FT /note="Laminin EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1014..1059 FT /note="Laminin EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1060..1105 FT /note="Laminin EGF-like 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1106..1165 FT /note="Laminin EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1166..1175 FT /note="Laminin EGF-like 14; first part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1176..1379 FT /note="Laminin IV type A 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458" FT DOMAIN 1380..1419 FT /note="Laminin EGF-like 14; second part" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1420..1468 FT /note="Laminin EGF-like 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1469..1526 FT /note="Laminin EGF-like 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1527..1573 FT /note="Laminin EGF-like 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 2145..2328 FT /note="Laminin G-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 2340..2521 FT /note="Laminin G-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 2526..2710 FT /note="Laminin G-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 2763..2934 FT /note="Laminin G-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 2939..3110 FT /note="Laminin G-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT REGION 1574..2144 FT /note="Domain II and I" FT REGION 3043..3063 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1630..2150 FT /evidence="ECO:0000255" FT COMPBIAS 3043..3060 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 55 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 89 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 303 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 363 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 380 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 470 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 746 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1061 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1597 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1614 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1700 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1810 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1901 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1916 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1920 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2017 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2028 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2045 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2126 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2360 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2435 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2478 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2551 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2558 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2648 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2868 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2893 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 287..296 FT /evidence="ECO:0000250" FT DISULFID 289..307 FT /evidence="ECO:0000250" FT DISULFID 309..318 FT /evidence="ECO:0000250" FT DISULFID 321..341 FT /evidence="ECO:0000250" FT DISULFID 344..353 FT /evidence="ECO:0000250" FT DISULFID 346..378 FT /evidence="ECO:0000250" FT DISULFID 381..390 FT /evidence="ECO:0000250" FT DISULFID 393..411 FT /evidence="ECO:0000250" FT DISULFID 414..426 FT /evidence="ECO:0000250" FT DISULFID 416..442 FT /evidence="ECO:0000250" FT DISULFID 444..453 FT /evidence="ECO:0000250" FT DISULFID 456..466 FT /evidence="ECO:0000250" FT DISULFID 469..482 FT /evidence="ECO:0000250" FT DISULFID 471..486 FT /evidence="ECO:0000250" FT DISULFID 488..497 FT /evidence="ECO:0000250" FT DISULFID 500..515 FT /evidence="ECO:0000250" FT DISULFID 757..766 FT /evidence="ECO:0000250" FT DISULFID 759..773 FT /evidence="ECO:0000250" FT DISULFID 776..785 FT /evidence="ECO:0000250" FT DISULFID 788..804 FT /evidence="ECO:0000250" FT DISULFID 807..822 FT /evidence="ECO:0000250" FT DISULFID 809..832 FT /evidence="ECO:0000250" FT DISULFID 835..844 FT /evidence="ECO:0000250" FT DISULFID 847..862 FT /evidence="ECO:0000250" FT DISULFID 865..879 FT /evidence="ECO:0000250" FT DISULFID 867..886 FT /evidence="ECO:0000250" FT DISULFID 889..898 FT /evidence="ECO:0000250" FT DISULFID 901..915 FT /evidence="ECO:0000250" FT DISULFID 918..930 FT /evidence="ECO:0000250" FT DISULFID 920..937 FT /evidence="ECO:0000250" FT DISULFID 939..948 FT /evidence="ECO:0000250" FT DISULFID 951..964 FT /evidence="ECO:0000250" FT DISULFID 967..979 FT /evidence="ECO:0000250" FT DISULFID 969..985 FT /evidence="ECO:0000250" FT DISULFID 987..996 FT /evidence="ECO:0000250" FT DISULFID 999..1011 FT /evidence="ECO:0000250" FT DISULFID 1014..1023 FT /evidence="ECO:0000250" FT DISULFID 1016..1030 FT /evidence="ECO:0000250" FT DISULFID 1032..1041 FT /evidence="ECO:0000250" FT DISULFID 1044..1057 FT /evidence="ECO:0000250" FT DISULFID 1060..1072 FT /evidence="ECO:0000250" FT DISULFID 1062..1079 FT /evidence="ECO:0000250" FT DISULFID 1081..1090 FT /evidence="ECO:0000250" FT DISULFID 1093..1103 FT /evidence="ECO:0000250" FT DISULFID 1106..1118 FT /evidence="ECO:0000250" FT DISULFID 1108..1134 FT /evidence="ECO:0000250" FT DISULFID 1136..1145 FT /evidence="ECO:0000250" FT DISULFID 1148..1163 FT /evidence="ECO:0000250" FT DISULFID 1420..1429 FT /evidence="ECO:0000250" FT DISULFID 1422..1436 FT /evidence="ECO:0000250" FT DISULFID 1439..1448 FT /evidence="ECO:0000250" FT DISULFID 1451..1466 FT /evidence="ECO:0000250" FT DISULFID 1469..1484 FT /evidence="ECO:0000250" FT DISULFID 1471..1494 FT /evidence="ECO:0000250" FT DISULFID 1497..1506 FT /evidence="ECO:0000250" FT DISULFID 1509..1524 FT /evidence="ECO:0000250" FT DISULFID 1527..1539 FT /evidence="ECO:0000250" FT DISULFID 1529..1546 FT /evidence="ECO:0000250" FT DISULFID 1548..1557 FT /evidence="ECO:0000250" FT DISULFID 1560..1571 FT /evidence="ECO:0000250" FT DISULFID 1574 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1578 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 2302..2328 FT /evidence="ECO:0000250" FT DISULFID 2495..2521 FT /evidence="ECO:0000250" FT DISULFID 2683..2710 FT /evidence="ECO:0000250" FT DISULFID 2909..2934 FT /evidence="ECO:0000250" FT VARIANT 95..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081607" FT VARIANT 96 FT /note="R -> S (in dbSNP:rs34626728)" FT /id="VAR_047713" FT VARIANT 110..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081608" FT VARIANT 121..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081609" FT VARIANT 131..3122 FT /note="Missing (in LGMDR23)" FT /evidence="ECO:0000269|PubMed:24957499" FT /id="VAR_081610" FT VARIANT 152 FT /note="W -> G (in LGMDR23)" FT /evidence="ECO:0000269|PubMed:21953594" FT /id="VAR_081611" FT VARIANT 199 FT /note="C -> S (in dbSNP:rs886043693)" FT /evidence="ECO:0000269|PubMed:24957499" FT /id="VAR_081612" FT VARIANT 240 FT /note="Y -> H (in dbSNP:rs3778142)" FT /id="VAR_047714" FT VARIANT 243 FT /note="L -> P (in LGMDR23; dbSNP:rs1562273395)" FT /evidence="ECO:0000269|PubMed:21953594" FT /id="VAR_081613" FT VARIANT 273..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081614" FT VARIANT 284 FT /note="G -> R (in LGMDR23; decreased protein abundance in FT patient cells)" FT /evidence="ECO:0000269|PubMed:21953594" FT /id="VAR_081615" FT VARIANT 435..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081616" FT VARIANT 518 FT /note="C -> Y (in MDC1A; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081617" FT VARIANT 527 FT /note="C -> Y (in MDC1A; dbSNP:rs121913574)" FT /evidence="ECO:0000269|PubMed:12552556" FT /id="VAR_015743" FT VARIANT 545 FT /note="L -> Q (in dbSNP:rs118083923)" FT /evidence="ECO:0000269|Ref.11" FT /id="VAR_004165" FT VARIANT 619 FT /note="R -> H (in dbSNP:rs3816665)" FT /evidence="ECO:0000269|Ref.11" FT /id="VAR_004166" FT VARIANT 644 FT /note="H -> D (in dbSNP:rs35879899)" FT /id="VAR_047715" FT VARIANT 659..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081618" FT VARIANT 744..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081619" FT VARIANT 821 FT /note="T -> M (in MDC1A; uncertain significance; FT dbSNP:rs117422805)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081620" FT VARIANT 862 FT /note="C -> R (in MDC1A; dbSNP:rs121913573)" FT /evidence="ECO:0000269|PubMed:12552556" FT /id="VAR_015744" FT VARIANT 919 FT /note="R -> L (in dbSNP:rs35277491)" FT /evidence="ECO:0000269|Ref.11" FT /id="VAR_004167" FT VARIANT 986..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081621" FT VARIANT 1032..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081622" FT VARIANT 1095..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081623" FT VARIANT 1138 FT /note="V -> M (in dbSNP:rs2306942)" FT /id="VAR_047716" FT VARIANT 1160 FT /note="P -> A (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035819" FT VARIANT 1205 FT /note="T -> A (in dbSNP:rs35889149)" FT /id="VAR_047717" FT VARIANT 1311 FT /note="W -> G (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081624" FT VARIANT 1319..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081625" FT VARIANT 1350..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081626" FT VARIANT 1496 FT /note="A -> V (in LGMDR23; decreased protein abundance in FT patient cells; dbSNP:rs147077184)" FT /evidence="ECO:0000269|PubMed:24957499" FT /id="VAR_081627" FT VARIANT 1561 FT /note="K -> Q (in dbSNP:rs4143752)" FT /id="VAR_047718" FT VARIANT 1826..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081628" FT VARIANT 1945 FT /note="A -> T (in dbSNP:rs3828736)" FT /id="VAR_047719" FT VARIANT 2172 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081629" FT VARIANT 2383..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081630" FT VARIANT 2477 FT /note="R -> S (in LGMDR23; dbSNP:rs34367843)" FT /evidence="ECO:0000269|PubMed:21953594" FT /id="VAR_081631" FT VARIANT 2564 FT /note="L -> P (in MDC1A; dbSNP:rs121913570)" FT /evidence="ECO:0000269|PubMed:11591858" FT /id="VAR_015745" FT VARIANT 2578..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081632" FT VARIANT 2586 FT /note="Y -> H" FT /evidence="ECO:0000269|Ref.11" FT /id="VAR_004168" FT VARIANT 2587 FT /note="A -> V (in dbSNP:rs2229848)" FT /evidence="ECO:0000269|PubMed:2185464, FT ECO:0000269|PubMed:8294519, ECO:0000269|PubMed:8910357" FT /id="VAR_047720" FT VARIANT 2604..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081633" FT VARIANT 2614 FT /note="E -> K" FT /evidence="ECO:0000269|Ref.11" FT /id="VAR_004169" FT VARIANT 2633 FT /note="G -> A (in MDC1A; dbSNP:rs2114849222)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081634" FT VARIANT 2636 FT /note="T -> A (in dbSNP:rs2244008)" FT /id="VAR_047721" FT VARIANT 2641..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081635" FT VARIANT 2755..3122 FT /note="Missing (in MDC1A)" FT /evidence="ECO:0000269|PubMed:24611677" FT /id="VAR_081636" FT VARIANT 2889 FT /note="G -> R (in MDC1A; dbSNP:rs886039896)" FT /evidence="ECO:0000269|PubMed:27234031" FT /id="VAR_076560" FT VARIANT 3029 FT /note="T -> A (in dbSNP:rs34551216)" FT /id="VAR_047722" FT CONFLICT 588 FT /note="A -> R (in Ref. 2; AAB18388)" FT /evidence="ECO:0000305" FT CONFLICT 1740 FT /note="A -> D (in Ref. 4)" FT /evidence="ECO:0000305" FT CONFLICT 1827 FT /note="Q -> G (in Ref. 4)" FT /evidence="ECO:0000305" FT CONFLICT 1981 FT /note="A -> V (in Ref. 5; AAA63215)" FT /evidence="ECO:0000305" FT CONFLICT 2437 FT /note="S -> Y (in Ref. 2; AAB18388)" FT /evidence="ECO:0000305" FT CONFLICT 2624 FT /note="H -> R (in Ref. 5; AAA63215)" FT /evidence="ECO:0000305" FT CONFLICT 2807 FT /note="R -> A (in Ref. 1; CAA81394 and 2; AAB18388)" FT /evidence="ECO:0000305" FT CONFLICT 2969 FT /note="R -> A (in Ref. 1; CAA81394 and 2; AAB18388)" FT /evidence="ECO:0000305" FT STRAND 1184..1186 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1197..1199 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1210..1213 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1216..1220 FT /evidence="ECO:0007829|PDB:4YEP" FT HELIX 1221..1230 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1232..1236 FT /evidence="ECO:0007829|PDB:4YEP" FT HELIX 1239..1241 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1242..1244 FT /evidence="ECO:0007829|PDB:4YEQ" FT HELIX 1246..1248 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1252..1265 FT /evidence="ECO:0007829|PDB:4YEP" FT TURN 1267..1270 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1273..1280 FT /evidence="ECO:0007829|PDB:4YEP" FT TURN 1281..1283 FT /evidence="ECO:0007829|PDB:4YEQ" FT STRAND 1285..1289 FT /evidence="ECO:0007829|PDB:4YEP" FT HELIX 1292..1295 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1300..1308 FT /evidence="ECO:0007829|PDB:4YEP" FT HELIX 1326..1334 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1336..1342 FT /evidence="ECO:0007829|PDB:4YEP" FT STRAND 1346..1361 FT /evidence="ECO:0007829|PDB:4YEP" SQ SEQUENCE 3122 AA; 343905 MW; E2C13BD6FC1B7BAC CRC64; MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA LITTNATCGE KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT NAIDGKNTWW QSPSIKNGIE YHYVTITLDL QQVFQIAYVI VKAANSPRPG NWILERSLDD VEYKPWQYHA VTDTECLTLY NIYPRTGPPS YAKDDEVICT SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY IRLRFQRIRT LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA EECYYDENVA RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP KGVSPNYPRP CQPCHCDPIG SLNEVCVKDE KHARRGLAPG SCHCKTGFGG VSCDRCARGY TGYPDCKACN CSGLGSKNED PCFGPCICKE NVEGGDCSRC KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM SGWYLTDLPG RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT NVLLLKEESF TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL SSVNLESAVS YPTDGSIAAA VEVCQCPPGY TGSSCESCWP RHRRVNGTIF GGICEPCQCF GHAESCDDVT GECLNCKDHT GGPYCDKCLP GFYGEPTKGT SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT GPRCERCAEG YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK CKAGTFGLQS ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA HGYFNFQEGG CTACECSHLG NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG HSITTGCKAC NCSTVGSLDF QCNVNTGQCN CHPKFSGAKC TECSRGHWNY PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV EGIHCDRCRP GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG GKLKYAIYFE AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT RHEIEMTEKE WKYYGDDPRV HRTVTREDFL DILYDIHYIL IKATYGNFMR QSRISEISME VAEQGRGTTM TPPADLIEKC DCPLGYSGLS CEACLPGFYR LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ HHTAGDFCER CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP GATGRKCDGC KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG PLPAPYKMLY GLENMTQELK HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL LTRATKVTAD GEQTGQDAER TNTRAKSLGE FIKELARDAE AVNEKAIKLN ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA EDELVAAEAL LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN SIIDYVEDIQ TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL NDSSAVLDGI LDEAKNISFN ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH EATKLATGPR GLLKEDAKGC LQKSFRILNE AKKLANDVKE NEDHLNGLKT RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK ARQANDTAKD VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS GGDCIRTYKP EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR KGKVSFLWDV GSGVGRVEYP DLTIDDSYWY RIVASRTGRN GTISVRALDG PKASIVPSTH HSTSPPGYTI LDVDANAMLF VGGLTGKLKK ADAVRVITFT GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT IQFDGEGYAL VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA TSSSGNNFGL DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE ISRTPYNILS SPDYVGVTKG CSLENVYTVS FPKPGFVELS PVPIDVGTEI NLSFSTKNES GIILLGSGGT PAPPRRKRRQ TGQAYYAILL NRGRLEVHLS TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD ENRRYMQNLT VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP CAAESEPALL IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG LLFYMARINH ADFATVQLRN GLPYFSYDLG SGDTHTMIPT KINDGQWHKI KIMRSKQEGI LYVDGASNRT ISPKKADILD VVGMLYVGGL PINYTTRRIG PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR GTYFDGTGFA KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS PNPASTSADT NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP LEVNFAKALE LRGVQPVSCP AN //