CO6A1_HUMAN
ID CO6A1_HUMAN Reviewed; 1028 AA.
AC P12109; O00117; O00118; Q14040; Q14041; Q16258; Q7Z645; Q9BSA8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Collagen alpha-1(VI) chain;
DE Flags: Precursor;
GN Name=COL6A1;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fibroblast;
RX PubMed=2551668; DOI=10.1002/j.1460-2075.1989.tb03598.x;
RA Chu M.-L., Pan T.-C., Conway D., Kuo H.J., Glanville R.W., Timpl R.,
RA Mann K., Deutzmann R.;
RT "Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human type VI
RT collagen reveals internal triplication of globular domains similar to the A
RT domains of von Willebrand factor and two alpha 2(VI) chain variants that
RT differ in the carboxy terminus.";
RL EMBO J. 8:1939-1946(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Ovary;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-380 AND 383-1028.
RX PubMed=8168508; DOI=10.1111/j.1432-1033.1994.tb18727.x;
RA Tillet E., Wiedemann H., Golbik R., Pan T.-C., Zhang R.Z., Mann K.,
RA Chu M.-L., Timpl R.;
RT "Recombinant expression and structural and binding properties of alpha
RT 1(VI) and alpha 2(VI) chains of human collagen type VI.";
RL Eur. J. Biochem. 221:177-185(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-268 AND 593-1028.
RX PubMed=9107679; DOI=10.1007/s003359900436;
RA Trikka D., Davis T., Lapenta V., Brahe C., Kessling A.M.;
RT "Human COL6A1: genomic characterization of the globular domains, structural
RT and evolutionary comparison with COL6A2.";
RL Mamm. Genome 8:342-345(1997).
RN [5]
RP PROTEIN SEQUENCE OF 246-258.
RX PubMed=6852033; DOI=10.1111/j.1432-1033.1983.tb07427.x;
RA Jander R., Rauterberg J., Glanville R.W.;
RT "Further characterization of the three polypeptide chains of bovine and
RT human short-chain collagen (intima collagen).";
RL Eur. J. Biochem. 133:39-46(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 257-592.
RX PubMed=3198591; DOI=10.1016/s0021-9258(18)37327-7;
RA Chu M.-L., Conway D., Pan T.-C., Baldwin C., Mann K., Deutzmann R.,
RA Timpl R.;
RT "Amino acid sequence of the triple-helical domain of human collagen type
RT VI.";
RL J. Biol. Chem. 263:18601-18606(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-592.
RX PubMed=1765372; DOI=10.1016/0888-7543(91)90111-q;
RA Saitta B., Wang Y.-M., Renkart L., Zhang R.-Z., Pan T.-C., Timpl R.,
RA Chu M.-L.;
RT "The exon organization of the triple-helical coding regions of the human
RT alpha 1(VI) and alpha 2(VI) collagen genes is highly similar.";
RL Genomics 11:145-153(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 422-482.
RX PubMed=3665927; DOI=10.1111/j.1432-1033.1987.tb13422.x;
RA Chu M.-L., Mann K., Deutzmann R., Pribula-Conway D., Hsu-Chen C.-C.,
RA Bernard M.P., Timpl R.;
RT "Characterization of three constituent chains of collagen type VI by
RT peptide sequences and cDNA clones.";
RL Eur. J. Biochem. 168:309-317(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 422-481.
RC TISSUE=Placenta;
RX PubMed=3348212;
RA Weil D., Mattei M.-G., Passage E., N'Guyen V.C., Pribula-Conway D.,
RA Mann K., Deutzmann R., Timpl R., Chu M.-L.;
RT "Cloning and chromosomal localization of human genes encoding the three
RT chains of type VI collagen.";
RL Am. J. Hum. Genet. 42:435-445(1988).
RN [10]
RP PROTEIN SEQUENCE OF 693-711; 737-757; 939-957 AND 991-1005, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-516; ASN-804 AND
RP ASN-896.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP VARIANT BTHLM1 VAL-305.
RX PubMed=8782832; DOI=10.1038/ng0996-113;
RA Joebsis G.J., Keizers H., Vreijling J.P., de Visser M., Speer M.C.,
RA Wolterman R.A., Baas F., Bohlhuis P.A.;
RT "Type VI collagen mutations in Bethlem myopathy, an autosomal dominant
RT myopathy with contractures.";
RL Nat. Genet. 14:113-115(1996).
RN [16]
RP VARIANTS BTHLM1 ARG-121 AND ASP-341.
RX PubMed=11865138; DOI=10.1212/wnl.58.4.593;
RA Scacheri P.C., Gillanders E.M., Subramony S.H., Vedanarayanan V.,
RA Crowe C.A., Thakore N., Bingler M., Hoffman E.P.;
RT "Novel mutations in collagen VI genes: expansion of the Bethlem myopathy
RT phenotype.";
RL Neurology 58:593-602(2002).
RN [17]
RP VARIANTS UCMD1 ARG-284 AND ARG-290, AND VARIANTS ASN-116 AND LEU-890.
RX PubMed=16130093; DOI=10.1002/ana.20586;
RA Giusti B., Lucarini L., Pietroni V., Lucioli S., Bandinelli B.,
RA Sabatelli P., Squarzoni S., Petrini S., Gartioux C., Talim B., Roelens F.,
RA Merlini L., Topaloglu H., Bertini E., Guicheney P., Pepe G.;
RT "Dominant and recessive COL6A1 mutations in Ullrich scleroatonic muscular
RT dystrophy.";
RL Ann. Neurol. 58:400-410(2005).
RN [18]
RP VARIANTS BTHLM1 LEU-274; ARG-290; VAL-341 AND THR-571, VARIANTS UCMD1
RP ARG-281 AND ARG-284, AND VARIANTS ASN-116; HIS-850; MET-881 AND LEU-890.
RX PubMed=15689448; DOI=10.1136/jmg.2004.023754;
RA Lampe A.K., Dunn D.M., von Niederhausern A.C., Hamil C., Aoyagi A.,
RA Laval S.H., Marie S.K., Chu M.-L., Swoboda K., Muntoni F., Bonnemann C.G.,
RA Flanigan K.M., Bushby K.M.D., Weiss R.B.;
RT "Automated genomic sequence analysis of the three collagen VI genes:
RT applications to Ullrich congenital muscular dystrophy and Bethlem
RT myopathy.";
RL J. Med. Genet. 42:108-120(2005).
RN [19]
RP VARIANTS BTHLM1 ASP-272; ARG-275; ARG-290 AND VAL-341.
RX PubMed=15955946; DOI=10.1212/01.wnl.0000163990.00057.66;
RA Lucioli S., Giusti B., Mercuri E., Vanegas O.C., Lucarini L., Pietroni V.,
RA Urtizberea A., Ben Yaou R., de Visser M., van der Kooi A.J., Boennemann C.,
RA Iannaccone S.T., Merlini L., Bushby K., Muntoni F., Bertini E., Chu M.-L.,
RA Pepe G.;
RT "Detection of common and private mutations in the COL6A1 gene of patients
RT with Bethlem myopathy.";
RL Neurology 64:1931-1937(2005).
RN [20]
RP CHARACTERIZATION OF VARIANT UCMD1 ARG-284.
RX PubMed=17785674; DOI=10.1212/01.wnl.0000271386.89878.22;
RA Kawahara G., Okada M., Morone N., Ibarra C.A., Nonaka I., Noguchi S.,
RA Hayashi Y.K., Nishino I.;
RT "Reduced cell anchorage may cause sarcolemma-specific collagen VI
RT deficiency in Ullrich disease.";
RL Neurology 69:1043-1049(2007).
RN [21]
RP INVOLVEMENT IN LIMB-GIRDLE MUSCULAR DYSTROPHY, AND VARIANT ALA-43.
RX PubMed=30345904; DOI=10.1152/physiolgenomics.00036.2018;
RA Saha M., Reddy H.M., Salih M., Estrella E., Jones M.D., Mitsuhashi S.,
RA Cho K.A., Suzuki-Hatano S., Rizzo S.A., Hamad M.H., Mukhtar M.M.,
RA Hamed A.A., Elseed M.A., Lek M., Valkanas E., MacArthur D.G., Kunkel L.M.,
RA Pacak C.A., Draper I., Kang P.B.;
RT "The impact of PYROXD1 deficiency on cellular respiration and correlations
RT with genetic analyses of limb-girdle muscular dystrophy in Saudi Arabia and
RT Sudan.";
RL Physiol. Genomics 50:929-939(2018).
CC -!- FUNCTION: Collagen VI acts as a cell-binding protein.
CC -!- SUBUNIT: Trimers composed of three different chains: alpha-1(VI),
CC alpha-2(VI), and alpha-3(VI) or alpha-5(VI) or alpha-6(VI).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- DISEASE: Bethlem myopathy 1 (BTHLM1) [MIM:158810]: A benign proximal
CC myopathy characterized by early childhood onset and joint contractures
CC most frequently affecting the elbows and ankles.
CC {ECO:0000269|PubMed:11865138, ECO:0000269|PubMed:15689448,
CC ECO:0000269|PubMed:15955946, ECO:0000269|PubMed:8782832}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Ullrich congenital muscular dystrophy 1 (UCMD1) [MIM:254090]:
CC A congenital myopathy characterized by muscle weakness and multiple
CC joint contractures, generally noted at birth or early infancy. The
CC clinical course is more severe than in Bethlem myopathy.
CC {ECO:0000269|PubMed:15689448, ECO:0000269|PubMed:16130093,
CC ECO:0000269|PubMed:17785674}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A mutation in COL6A1 is the cause of autosomal recessive
CC limb-girdle muscular dystrophy. The affected individual with a
CC homozygous recessive COL6A1 mutation showed progressive muscle weakness
CC with an onset at the age of 4 years and loss of ambulation at the age
CC of 15 years. Muscle biopsy showed end stage dystrophy.
CC {ECO:0000269|PubMed:30345904}.
CC -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
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DR EMBL; X15879; CAA33888.1; -; mRNA.
DR EMBL; X15880; CAA33889.1; -; mRNA.
DR EMBL; BC005159; AAH05159.2; -; mRNA.
DR EMBL; BC052575; AAH52575.1; -; mRNA.
DR EMBL; X99109; CAA67559.1; -; Genomic_DNA.
DR EMBL; X99135; CAA67576.1; -; Genomic_DNA.
DR EMBL; X99136; CAA67576.1; JOINED; Genomic_DNA.
DR EMBL; M20776; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S75420; AAB20835.2; -; Genomic_DNA.
DR EMBL; S75385; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75388; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75390; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75392; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75394; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75396; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75398; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75400; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75402; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75404; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75406; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75408; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75410; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75412; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75414; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75416; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; S75418; AAB20835.2; JOINED; Genomic_DNA.
DR EMBL; X06194; CAA29555.1; -; mRNA.
DR EMBL; M27447; AAA52055.1; -; mRNA.
DR CCDS; CCDS13727.1; -.
DR PIR; S05377; CGHU1A.
DR RefSeq; NP_001839.2; NM_001848.2.
DR AlphaFoldDB; P12109; -.
DR SMR; P12109; -.
DR BioGRID; 107688; 132.
DR ComplexPortal; CPX-1736; Collagen type VI trimer.
DR IntAct; P12109; 37.
DR MINT; P12109; -.
DR STRING; 9606.ENSP00000355180; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyConnect; 1129; 30 N-Linked glycans (3 sites).
DR GlyGen; P12109; 8 sites, 29 N-linked glycans (3 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; P12109; -.
DR MetOSite; P12109; -.
DR PhosphoSitePlus; P12109; -.
DR BioMuta; COL6A1; -.
DR DMDM; 125987811; -.
DR REPRODUCTION-2DPAGE; IPI00291136; -.
DR REPRODUCTION-2DPAGE; P12109; -.
DR EPD; P12109; -.
DR jPOST; P12109; -.
DR MassIVE; P12109; -.
DR MaxQB; P12109; -.
DR PaxDb; P12109; -.
DR PeptideAtlas; P12109; -.
DR PRIDE; P12109; -.
DR ProteomicsDB; 52829; -.
DR Antibodypedia; 10507; 391 antibodies from 39 providers.
DR DNASU; 1291; -.
DR Ensembl; ENST00000361866.8; ENSP00000355180.3; ENSG00000142156.16.
DR GeneID; 1291; -.
DR KEGG; hsa:1291; -.
DR MANE-Select; ENST00000361866.8; ENSP00000355180.3; NM_001848.3; NP_001839.2.
DR UCSC; uc002zhu.2; human.
DR CTD; 1291; -.
DR DisGeNET; 1291; -.
DR GeneCards; COL6A1; -.
DR GeneReviews; COL6A1; -.
DR HGNC; HGNC:2211; COL6A1.
DR HPA; ENSG00000142156; Low tissue specificity.
DR MalaCards; COL6A1; -.
DR MIM; 120220; gene.
DR MIM; 158810; phenotype.
DR MIM; 254090; phenotype.
DR neXtProt; NX_P12109; -.
DR OpenTargets; ENSG00000142156; -.
DR Orphanet; 610; Bethlem myopathy.
DR Orphanet; 75840; Congenital muscular dystrophy, Ullrich type.
DR PharmGKB; PA26727; -.
DR VEuPathDB; HostDB:ENSG00000142156; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000162889; -.
DR HOGENOM; CLU_009158_1_0_1; -.
DR InParanoid; P12109; -.
DR OMA; TTQICID; -.
DR OrthoDB; 140989at2759; -.
DR PhylomeDB; P12109; -.
DR TreeFam; TF331207; -.
DR PathwayCommons; P12109; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; P12109; -.
DR SIGNOR; P12109; -.
DR BioGRID-ORCS; 1291; 25 hits in 1083 CRISPR screens.
DR ChiTaRS; COL6A1; human.
DR GeneWiki; Collagen,_type_VI,_alpha_1; -.
DR GenomeRNAi; 1291; -.
DR Pharos; P12109; Tbio.
DR PRO; PR:P12109; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P12109; protein.
DR Bgee; ENSG00000142156; Expressed in stromal cell of endometrium and 203 other tissues.
DR ExpressionAtlas; P12109; baseline and differential.
DR Genevisible; P12109; HS.
DR GO; GO:0005589; C:collagen type VI trimer; NAS:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IPI:MGI.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; ISS:BHF-UCL.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF00092; VWA; 3.
DR SMART; SM00327; VWA; 3.
DR SUPFAM; SSF53300; SSF53300; 3.
DR PROSITE; PS50234; VWFA; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Collagen; Congenital muscular dystrophy;
KW Direct protein sequencing; Disease variant; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Limb-girdle muscular dystrophy;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..1028
FT /note="Collagen alpha-1(VI) chain"
FT /id="PRO_0000005758"
FT DOMAIN 37..235
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 615..805
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 829..1021
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 20..256
FT /note="N-terminal globular domain"
FT REGION 254..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..592
FT /note="Triple-helical region"
FT REGION 593..1028
FT /note="C-terminal globular domain"
FT MOTIF 262..264
FT /note="Cell attachment site"
FT MOTIF 442..444
FT /note="Cell attachment site"
FT MOTIF 478..480
FT /note="Cell attachment site"
FT COMPBIAS 303..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VARIANT 43
FT /note="D -> A (probable disease-associated variant found in
FT a patient with limb-girdle muscular dystrophy;
FT dbSNP:rs786205555)"
FT /evidence="ECO:0000269|PubMed:30345904"
FT /id="VAR_081097"
FT VARIANT 116
FT /note="S -> N (in dbSNP:rs11553519)"
FT /evidence="ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:16130093"
FT /id="VAR_058213"
FT VARIANT 121
FT /note="K -> R (in BTHLM1; dbSNP:rs121912936)"
FT /evidence="ECO:0000269|PubMed:11865138"
FT /id="VAR_013580"
FT VARIANT 272
FT /note="G -> D (in BTHLM1; dbSNP:rs1064793840)"
FT /evidence="ECO:0000269|PubMed:15955946"
FT /id="VAR_058214"
FT VARIANT 274
FT /note="P -> L (in BTHLM1; dbSNP:rs201093313)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058215"
FT VARIANT 275
FT /note="G -> R (in BTHLM1; dbSNP:rs1556425467)"
FT /evidence="ECO:0000269|PubMed:15955946"
FT /id="VAR_058216"
FT VARIANT 281
FT /note="G -> R (in UCMD1; dbSNP:rs267606746)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058217"
FT VARIANT 284
FT /note="G -> R (in UCMD1; fibroblasts with the mutation
FT assembled and secreted normal collagen VI microfibrils;
FT cell adhesion of heterozygous Arg-284 fibroblasts is
FT markedly decreased but can be rescued by the addition of
FT normal collagen VI; dbSNP:rs121912938)"
FT /evidence="ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:16130093, ECO:0000269|PubMed:17785674"
FT /id="VAR_058218"
FT VARIANT 290
FT /note="G -> R (in BTHLM1 and UCMD1; dbSNP:rs121912939)"
FT /evidence="ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:15955946, ECO:0000269|PubMed:16130093"
FT /id="VAR_058219"
FT VARIANT 305
FT /note="G -> V (in BTHLM1)"
FT /evidence="ECO:0000269|PubMed:8782832"
FT /id="VAR_013581"
FT VARIANT 332
FT /note="G -> S (in dbSNP:rs11701912)"
FT /id="VAR_058220"
FT VARIANT 341
FT /note="G -> D (in BTHLM1; dbSNP:rs121912935)"
FT /evidence="ECO:0000269|PubMed:11865138"
FT /id="VAR_013582"
FT VARIANT 341
FT /note="G -> V (in BTHLM1; dbSNP:rs121912935)"
FT /evidence="ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:15955946"
FT /id="VAR_058221"
FT VARIANT 439
FT /note="R -> Q (in dbSNP:rs35059000)"
FT /id="VAR_048763"
FT VARIANT 571
FT /note="K -> T (in BTHLM1; dbSNP:rs751040647)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058222"
FT VARIANT 850
FT /note="R -> H (in dbSNP:rs1053312)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_048764"
FT VARIANT 881
FT /note="T -> M (in dbSNP:rs150432347)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058223"
FT VARIANT 890
FT /note="S -> L (in dbSNP:rs13051496)"
FT /evidence="ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:16130093"
FT /id="VAR_058224"
FT CONFLICT 387..388
FT /note="SS -> AR (in Ref. 6; M20776 and 7; AAB20835)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..397
FT /note="QP -> PA (in Ref. 6; M20776 and 7; AAB20835)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="T -> P (in Ref. 6; M20776)"
FT /evidence="ECO:0000305"
FT CONFLICT 835..839
FT /note="DGSAS -> EPPPD (in Ref. 1; CAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="A -> P (in Ref. 4; CAA67576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1028 AA; 108529 MW; 04AFF538002A01CD CRC64;
MRAARALLPL LLQACWTAAQ DEPETPRAVA FQDCPVDLFF VLDTSESVAL RLKPYGALVD
KVKSFTKRFI DNLRDRYYRC DRNLVWNAGA LHYSDEVEII QGLTRMPGGR DALKSSVDAV
KYFGKGTYTD CAIKKGLEQL LVGGSHLKEN KYLIVVTDGH PLEGYKEPCG GLEDAVNEAK
HLGVKVFSVA ITPDHLEPRL SIIATDHTYR RNFTAADWGQ SRDAEEAISQ TIDTIVDMIK
NNVEQVCCSF ECQPARGPPG LRGDPGFEGE RGKPGLPGEK GEAGDPGRPG DLGPVGYQGM
KGEKGSRGEK GSRGPKGYKG EKGKRGIDGV DGVKGEMGYP GLPGCKGSPG FDGIQGPPGP
KGDPGAFGLK GEKGEPGADG EAGRPGSSGP SGDEGQPGEP GPPGEKGEAG DEGNPGPDGA
PGERGGPGER GPRGTPGTRG PRGDPGEAGP QGDQGREGPV GVPGDPGEAG PIGPKGYRGD
EGPPGSEGAR GAPGPAGPPG DPGLMGERGE DGPAGNGTEG FPGFPGYPGN RGAPGINGTK
GYPGLKGDEG EAGDPGDDNN DIAPRGVKGA KGYRGPEGPQ GPPGHQGPPG PDECEILDII
MKMCSCCECK CGPIDLLFVL DSSESIGLQN FEIAKDFVVK VIDRLSRDEL VKFEPGQSYA
GVVQYSHSQM QEHVSLRSPS IRNVQELKEA IKSLQWMAGG TFTGEALQYT RDQLLPPSPN
NRIALVITDG RSDTQRDTTP LNVLCSPGIQ VVSVGIKDVF DFIPGSDQLN VISCQGLAPS
QGRPGLSLVK ENYAELLEDA FLKNVTAQIC IDKKCPDYTC PITFSSPADI TILLDGSASV
GSHNFDTTKR FAKRLAERFL TAGRTDPAHD VRVAVVQYSG TGQQRPERAS LQFLQNYTAL
ASAVDAMDFI NDATDVNDAL GYVTRFYREA SSGAAKKRLL LFSDGNSQGA TPAAIEKAVQ
EAQRAGIEIF VVVVGRQVNE PHIRVLVTGK TAEYDVAYGE SHLFRVPSYQ ALLRGVFHQT
VSRKVALG
