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 24-JUL-2024, entry version 231. 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 BTHLM1A 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 BTHLM1A 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 UCMD1A 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 BTHLM1A LEU-274; ARG-290; VAL-341 AND THR-571, VARIANTS UCMD1A 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 BTHLM1A 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 UCMD1A 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 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 1A (BTHLM1A) [MIM:158810]: A form of Bethlem CC myopathy, a slowly progressive muscular dystrophy characterized by CC joint contractures, most frequently affecting the elbows and ankles, CC and muscle weakness and wasting involving the proximal and extensor CC muscles more than the distal and flexor ones. The clinical onset more CC often occurs in childhood or adulthood, but it can be prenatal with CC decreased fetal movements or neonatal with hypotonia. The hallmark of CC Bethlem myopathy is long finger flexion contractures. Inheritance can CC be autosomal dominant or autosomal recessive. 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 1A (UCMD1A) CC [MIM:254090]: A form of Ullrich congenital muscular dystrophy, a CC disease characterized by generalized muscle weakness and striking CC hypermobility of distal joints in conjunction with variable CC contractures of more proximal joints and normal intelligence. CC Additional findings may include kyphoscoliosis, protruded calcanei, and CC follicular hyperkeratosis (rough skin). More severely affected patients CC manifest at birth and never achieve independent ambulation, while CC patients with milder phenotypes might maintain ambulation into CC adulthood. Inheritance can be autosomal dominant or autosomal CC recessive. {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 -!- SIMILARITY: Belongs to the type VI collagen family. {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; 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; 140. DR ComplexPortal; CPX-1736; Collagen type VI trimer. DR IntAct; P12109; 37. DR STRING; 9606.ENSP00000355180; -. DR ChEMBL; CHEMBL2364188; -. DR GlyConnect; 1129; 30 N-Linked glycans (3 sites). DR GlyCosmos; P12109; 7 sites, 30 glycans. 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 SwissPalm; P12109; -. DR BioMuta; COL6A1; -. DR DMDM; 125987811; -. DR REPRODUCTION-2DPAGE; IPI00291136; -. DR REPRODUCTION-2DPAGE; P12109; -. DR jPOST; P12109; -. DR MassIVE; P12109; -. DR PaxDb; 9606-ENSP00000355180; -. DR PeptideAtlas; P12109; -. DR ProteomicsDB; 52829; -. DR Pumba; P12109; -. DR Antibodypedia; 10507; 411 antibodies from 40 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 AGR; HGNC:2211; -. DR CTD; 1291; -. DR DisGeNET; 1291; -. DR GeneCards; COL6A1; -. DR GeneReviews; COL6A1; -. DR HGNC; HGNC:2211; COL6A1. DR HPA; ENSG00000142156; Tissue enhanced (intestine). 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 muscular dystrophy. DR Orphanet; 646098; Collagen VI-related congenital muscular dystrophy. DR Orphanet; 646113; Intermediate collagen VI-related muscular dystrophy. DR Orphanet; 75840; Ullrich congenital muscular dystrophy. 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; QEKKCPD; -. DR OrthoDB; 2906665at2759; -. 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 1161 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 205 other cell types or tissues. DR ExpressionAtlas; P12109; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. 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:0097708; C:intracellular vesicle; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0030016; C:myofibril; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IPI:MGI. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0016529; C:sarcoplasmic reticulum; 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:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl. DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl. DR GO; GO:0030262; P:apoptotic nuclear changes; IEA:Ensembl. DR GO; GO:0006914; P:autophagy; IEA:Ensembl. DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl. DR GO; GO:0060348; P:bone development; IEA:Ensembl. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0070836; P:caveola assembly; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl. DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl. DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0006112; P:energy reserve metabolic process; IEA:Ensembl. DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl. DR GO; GO:0070341; P:fat cell proliferation; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0006096; P:glycolytic process; IEA:Ensembl. DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0036022; P:limb joint morphogenesis; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl. DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl. DR GO; GO:0051882; P:mitochondrial depolarization; IEA:Ensembl. DR GO; GO:1990542; P:mitochondrial transmembrane transport; IEA:Ensembl. DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl. DR GO; GO:0071965; P:multicellular organismal locomotion; IEA:Ensembl. DR GO; GO:0010657; P:muscle cell apoptotic process; IEA:Ensembl. DR GO; GO:0003012; P:muscle system process; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0051262; P:protein tetramerization; IEA:Ensembl. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; IEA:Ensembl. DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl. DR GO; GO:1904026; P:regulation of collagen fibril organization; IEA:Ensembl. DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl. DR GO; GO:1904975; P:response to bleomycin; IEA:Ensembl. DR GO; GO:0036293; P:response to decreased oxygen levels; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl. DR GO; GO:0048265; P:response to pain; IEA:Ensembl. DR GO; GO:1901652; P:response to peptide; IEA:Ensembl. DR GO; GO:1904583; P:response to polyamine macromolecule; IEA:Ensembl. DR GO; GO:0000302; P:response to reactive oxygen species; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0009411; P:response to UV; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0050954; P:sensory perception of mechanical stimulus; IEA:Ensembl. DR GO; GO:0007338; P:single fertilization; IEA:Ensembl. DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl. DR GO; GO:0098528; P:skeletal muscle fiber differentiation; IEA:Ensembl. DR GO; GO:0048630; P:skeletal muscle tissue growth; IEA:Ensembl. DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl. DR GO; GO:0048771; P:tissue remodeling; IEA:Ensembl. DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:Ensembl. DR GO; GO:0060065; P:uterus development; IEA:Ensembl. DR CDD; cd01480; vWA_collagen_alpha_1-VI-type; 3. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 3. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050525; ECM_Assembly_Org. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24020:SF84; COLLAGEN ALPHA-1(XXI) CHAIN-LIKE ISOFORM X1; 1. DR Pfam; PF01391; Collagen; 5. DR Pfam; PF00092; VWA; 3. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00327; VWA; 3. DR SUPFAM; SSF53300; vWA-like; 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; 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 (found in a patient with limb-girdle muscular FT dystrophy; uncertain significance; 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 BTHLM1A; dbSNP:rs121912936)" FT /evidence="ECO:0000269|PubMed:11865138" FT /id="VAR_013580" FT VARIANT 272 FT /note="G -> D (in BTHLM1A; dbSNP:rs1064793840)" FT /evidence="ECO:0000269|PubMed:15955946" FT /id="VAR_058214" FT VARIANT 274 FT /note="P -> L (in BTHLM1A; dbSNP:rs201093313)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058215" FT VARIANT 275 FT /note="G -> R (in BTHLM1A; dbSNP:rs1556425467)" FT /evidence="ECO:0000269|PubMed:15955946" FT /id="VAR_058216" FT VARIANT 281 FT /note="G -> R (in UCMD1A; dbSNP:rs267606746)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058217" FT VARIANT 284 FT /note="G -> R (in UCMD1A; 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 BTHLM1A and UCMD1A; 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 BTHLM1A)" 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 BTHLM1A; dbSNP:rs121912935)" FT /evidence="ECO:0000269|PubMed:11865138" FT /id="VAR_013582" FT VARIANT 341 FT /note="G -> V (in BTHLM1A; 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 BTHLM1A; 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 //