LAMA2_HUMAN
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 03-AUG-2022, entry version 223.
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};
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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_000417.2; NM_000426.3.
DR RefSeq; NP_001073291.1; NM_001079823.1.
DR PDB; 4YEP; X-ray; 1.19 A; A/B=1181-1362.
DR PDB; 4YEQ; X-ray; 3.20 A; U=1177-1379.
DR PDBsum; 4YEP; -.
DR PDBsum; 4YEQ; -.
DR SMR; P24043; -.
DR BioGRID; 110102; 18.
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 IntAct; P24043; 13.
DR MINT; P24043; -.
DR STRING; 9606.ENSP00000400365; -.
DR ChEMBL; CHEMBL2364187; -.
DR GlyConnect; 1439; 40 N-Linked glycans (20 sites).
DR GlyGen; P24043; 32 sites, 39 N-linked glycans (20 sites), 2 O-linked glycans (4 sites).
DR iPTMnet; P24043; -.
DR PhosphoSitePlus; P24043; -.
DR BioMuta; LAMA2; -.
DR DMDM; 215274259; -.
DR EPD; P24043; -.
DR jPOST; P24043; -.
DR MassIVE; P24043; -.
DR PaxDb; P24043; -.
DR PeptideAtlas; P24043; -.
DR PRIDE; P24043; -.
DR ProteomicsDB; 54178; -.
DR ABCD; P24043; 1 sequenced antibody.
DR Antibodypedia; 763; 214 antibodies from 33 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 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 neXtProt; NX_P24043; -.
DR OpenTargets; ENSG00000196569; -.
DR Orphanet; 258; Laminin subunit alpha 2-related congenital muscular dystrophy.
DR PharmGKB; PA30271; -.
DR VEuPathDB; HostDB:ENSG00000196569; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000155362; -.
DR InParanoid; P24043; -.
DR OMA; KDYRDDA; -.
DR OrthoDB; 128982at2759; -.
DR PhylomeDB; P24043; -.
DR TreeFam; TF335359; -.
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 SignaLink; P24043; -.
DR SIGNOR; P24043; -.
DR BioGRID-ORCS; 3908; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; LAMA2; human.
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 197 other tissues.
DR ExpressionAtlas; P24043; baseline and differential.
DR Genevisible; P24043; HS.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:0045785; P:positive regulation of cell adhesion; IC:ComplexPortal.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IEA:Ensembl.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC: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:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 15.
DR CDD; cd00110; LamG; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 16.
DR Pfam; PF00054; Laminin_G_1; 4.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
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; SSF49899; 5.
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.
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 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..3062
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; unknown pathological
FT 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; unknown pathological 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)"
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 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
