ID CO6A3_HUMAN Reviewed; 3177 AA. AC P12111; A8MT30; B4E3U5; B7ZMJ7; E9PFQ6; E9PGQ9; Q16501; Q53QF4; Q53QF6; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 5. DT 27-MAR-2024, entry version 248. DE RecName: Full=Collagen alpha-3(VI) chain; DE Flags: Precursor; GN Name=COL6A3; 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], PARTIAL PROTEIN SEQUENCE, HYDROXYLATION AT RP PRO-2100; LYS-2103; PRO-2206; LYS-2209; LYS-2212; PRO-2239; PRO-2316; RP PRO-2319; LYS-2322 AND LYS-2337, AND VARIANTS VAL-2431; THR-2927; VAL-2988 RP AND PRO-3012. RC TISSUE=Fibroblast; RX PubMed=1689238; DOI=10.1002/j.1460-2075.1990.tb08122.x; RA Chu M.-L., Zhang R.-Z., Pan T.-C., Stokes D., Conway D., Kuo H.-J., RA Glanville R., Mayer U., Mann K., Deutzmann R., Timpl R.; RT "Mosaic structure of globular domains in the human type VI collagen alpha 3 RT chain: similarity to von Willebrand factor, fibronectin, actin, salivary RT proteins and aprotinin type protease inhibitors."; RL EMBO J. 9:385-393(1990). RN [2] RP SEQUENCE REVISION. RA Chu M.-L.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-236, AND ALTERNATIVE SPLICING. RX PubMed=1339440; DOI=10.1016/s0021-9258(18)35949-0; RA Zanussi S., Doliana R., Segat D., Bonaldo P., Colombatti A.; RT "The human type VI collagen gene. mRNA and protein variants of the alpha 3 RT chain generated by alternative splicing of an additional 5-end exon."; RL J. Biol. Chem. 267:24082-24089(1992). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2038-2373. 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2092-2157. 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 2092-2151. 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2677. 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 [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2079 AND ASN-2677. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1225, AND IDENTIFICATION BY RP 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 [14] RP INVOLVEMENT IN DYT27, AND VARIANTS DYT27 HIS-2501; THR-2554; HIS-3043 AND RP ARG-3082. RX PubMed=26004199; DOI=10.1016/j.ajhg.2015.04.010; RA Zech M., Lam D.D., Francescatto L., Schormair B., Salminen A.V., Jochim A., RA Wieland T., Lichtner P., Peters A., Gieger C., Lochmueller H., Strom T.M., RA Haslinger B., Katsanis N., Winkelmann J.; RT "Recessive mutations in the alpha3 (VI) collagen gene COL6A3 cause early- RT onset isolated dystonia."; RL Am. J. Hum. Genet. 96:883-893(2015). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3108-3165. RX PubMed=7533217; DOI=10.1016/s0022-2836(05)80110-x; RA Arnoux B., Merigeau K., Saludjian P., Norris F., Norris K., Bjoern S., RA Olsen O., Petersen L., Ducruix A.; RT "The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human RT type VI collagen."; RL J. Mol. Biol. 246:609-617(1995). RN [16] RP STRUCTURE BY NMR OF 3103-3165. RX PubMed=8805527; DOI=10.1016/s0969-2126(96)00022-6; RA Zweckstetter M., Czisch M., Mayer U., Chu M.-L., Zinth W., Timpl R., RA Holak T.A.; RT "Structure and multiple conformations of the Kunitz-type domain from human RT type VI collagen alpha3(VI) chain in solution."; RL Structure 4:195-209(1996). RN [17] RP STRUCTURE BY NMR OF 3108-3165. RX PubMed=9265624; DOI=10.1021/bi9705570; RA Soerensen M.D., Bjoern S., Norris K., Olsen O., Petersen L., James T.L., RA Led J.J.; RT "Solution structure and backbone dynamics of the human alpha3-chain type VI RT collagen C-terminal Kunitz domain."; RL Biochemistry 36:10439-10450(1997). RN [18] RP DISEASE. RX PubMed=11992252; DOI=10.1086/340608; RA Demir E., Sabatelli P., Allamand V., Ferreiro A., Moghadaszadeh B., RA Makrelouf M., Topaloglu H., Echenne B., Merlini L., Guicheney P.; RT "Mutations in COL6A3 cause severe and mild phenotypes of Ullrich congenital RT muscular dystrophy."; RL Am. J. Hum. Genet. 70:1446-1458(2002). RN [19] RP VARIANT BTHLM1 GLU-1679, AND VARIANT HIS-2831. RX PubMed=9536084; DOI=10.1093/hmg/7.5.807; RA Pan T.-C., Zhang R.-Z., Pericak-Vance M.A., Tandan R., Fries T., RA Stajich J.M., Viles K., Vance J.M., Chu M.-L., Speer M.C.; RT "Missense mutation in a von Willebrand factor type A domain of the alpha RT 3(VI) collagen gene (COL6A3) in a family with Bethlem myopathy."; RL Hum. Mol. Genet. 7:807-812(1998). RN [20] RP VARIANT BTHLM1 ARG-2056. RX PubMed=10399756; DOI=10.1016/s0960-8966(99)00014-0; RA Pepe G., Bertini E., Giusti B., Brunelli T., Comeglio P., Saitta B., RA Merlini L., Chu M.L., Federici G., Abbate R.; RT "A novel de novo mutation in the triple helix of the COL6A3 gene in a two- RT generation Italian family affected by Bethlem myopathy. A diagnostic RT approach in the mutations' screening of type VI collagen."; RL Neuromuscul. Disord. 9:264-271(1999). RN [21] RP VARIANTS BTHLM1 GLU-1014; LYS-1386; ASP-1467; GLU-1679; MET-1985; ASP-2047 RP AND ASP-2080, VARIANT UCMD1 ASN-1674, AND VARIANTS VAL-411; HIS-491; RP SER-492; HIS-677; THR-807; SER-830; GLN-1064; GLN-1088; GLN-1395; GLN-1576; RP GLN-1632; SER-1687; LEU-2218; HIS-2831 AND VAL-2941. 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 [22] RP VARIANT BTHLM1 ARG-1726, AND VARIANTS HIS-677; GLN-1576; VAL-2431; RP LYS-2453; HIS-2831; VAL-2988 AND ILE-3069. RX PubMed=17886299; DOI=10.1002/ana.21213; RA Baker N.L., Moergelin M., Pace R.A., Peat R.A., Adams N.E., Gardner R.J., RA Rowland L.P., Miller G., De Jonghe P., Ceulemans B., Hannibal M.C., RA Edwards M., Thompson E.M., Jacobson R., Quinlivan R.C.M., Aftimos S., RA Kornberg A.J., North K.N., Bateman J.F., Lamande S.R.; RT "Molecular consequences of dominant Bethlem myopathy collagen VI RT mutations."; RL Ann. Neurol. 62:390-405(2007). 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P12111-1; Sequence=Displayed; CC Name=2; CC IsoId=P12111-2; Sequence=VSP_001172; CC Name=3; CC IsoId=P12111-3; Sequence=VSP_001172, VSP_043434, VSP_043435, CC VSP_043436; CC Name=4; CC IsoId=P12111-4; Sequence=VSP_045718, VSP_045719; CC Name=5; CC IsoId=P12111-5; Sequence=VSP_001172, VSP_043435, VSP_043436; 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 {ECO:0000269|PubMed:1689238}. CC -!- PTM: The N-terminus is blocked. 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:10399756, ECO:0000269|PubMed:15689448, CC ECO:0000269|PubMed:17886299, ECO:0000269|PubMed:9536084}. 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}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Dystonia 27 (DYT27) [MIM:616411]: A form of dystonia, a CC disorder defined by the presence of sustained involuntary muscle CC contraction, often leading to abnormal postures. DYT27 is an autosomal CC recessive form characterized by segmental isolated dystonia involving CC the face, neck, bulbar muscles, and upper limbs. CC {ECO:0000269|PubMed:26004199}. 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; X52022; CAA36267.1; -; mRNA. DR EMBL; AK092021; BAG52467.1; -; mRNA. DR EMBL; AK304870; BAG65607.1; -; mRNA. DR EMBL; AC112715; AAY14906.1; -; Genomic_DNA. DR EMBL; AC112721; AAY24135.1; -; Genomic_DNA. DR EMBL; BC144595; AAI44596.1; -; mRNA. DR EMBL; BC150625; AAI50626.1; -; mRNA. DR EMBL; S49432; AAB24261.1; -; mRNA. DR EMBL; M20778; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X06196; CAA29557.1; -; mRNA. DR EMBL; M27449; AAA52057.1; -; mRNA. DR CCDS; CCDS33409.1; -. [P12111-2] DR CCDS; CCDS33410.2; -. [P12111-4] DR CCDS; CCDS33411.2; -. [P12111-5] DR CCDS; CCDS33412.1; -. [P12111-1] DR CCDS; CCDS54439.1; -. [P12111-3] DR PIR; A59140; CGHU3A. DR RefSeq; NP_004360.2; NM_004369.3. [P12111-1] DR RefSeq; NP_476505.3; NM_057164.4. [P12111-3] DR RefSeq; NP_476506.3; NM_057165.4. [P12111-5] DR RefSeq; NP_476507.3; NM_057166.4. [P12111-4] DR RefSeq; NP_476508.2; NM_057167.3. [P12111-2] DR RefSeq; XP_016858792.1; XM_017003303.1. DR PDB; 1KNT; X-ray; 1.60 A; A=3108-3165. DR PDB; 1KTH; X-ray; 0.95 A; A=3108-3165. DR PDB; 1KUN; NMR; -; A=3108-3165. DR PDB; 2KNT; X-ray; 1.20 A; A=3108-3165. DR PDB; 6SNK; X-ray; 2.20 A; A/B=1634-1833. DR PDBsum; 1KNT; -. DR PDBsum; 1KTH; -. DR PDBsum; 1KUN; -. DR PDBsum; 2KNT; -. DR PDBsum; 6SNK; -. DR SASBDB; P12111; -. DR SMR; P12111; -. DR BioGRID; 107690; 8. DR ComplexPortal; CPX-1736; Collagen type VI trimer. DR CORUM; P12111; -. DR IntAct; P12111; 12. DR MINT; P12111; -. DR STRING; 9606.ENSP00000295550; -. DR ChEMBL; CHEMBL2364188; -. DR MEROPS; I02.968; -. DR CarbonylDB; P12111; -. DR GlyConnect; 1139; 37 N-Linked glycans (6 sites). DR GlyCosmos; P12111; 23 sites, 41 glycans. DR GlyGen; P12111; 24 sites, 36 N-linked glycans (6 sites), 5 O-linked glycans (7 sites). DR iPTMnet; P12111; -. DR MetOSite; P12111; -. DR PhosphoSitePlus; P12111; -. DR BioMuta; COL6A3; -. DR DMDM; 311033499; -. DR CPTAC; CPTAC-1485; -. DR EPD; P12111; -. DR jPOST; P12111; -. DR MassIVE; P12111; -. DR MaxQB; P12111; -. DR PaxDb; 9606-ENSP00000295550; -. DR PeptideAtlas; P12111; -. DR ProteomicsDB; 20154; -. DR ProteomicsDB; 20370; -. DR ProteomicsDB; 52833; -. [P12111-1] DR ProteomicsDB; 52834; -. [P12111-2] DR ProteomicsDB; 52835; -. [P12111-3] DR Antibodypedia; 1395; 99 antibodies from 19 providers. DR DNASU; 1293; -. DR Ensembl; ENST00000295550.9; ENSP00000295550.4; ENSG00000163359.17. [P12111-1] DR Ensembl; ENST00000353578.9; ENSP00000315873.4; ENSG00000163359.17. [P12111-2] DR Ensembl; ENST00000392003.6; ENSP00000375860.2; ENSG00000163359.17. [P12111-3] DR Ensembl; ENST00000392004.7; ENSP00000375861.3; ENSG00000163359.17. [P12111-5] DR Ensembl; ENST00000472056.5; ENSP00000418285.1; ENSG00000163359.17. [P12111-4] DR GeneID; 1293; -. DR KEGG; hsa:1293; -. DR MANE-Select; ENST00000295550.9; ENSP00000295550.4; NM_004369.4; NP_004360.2. DR UCSC; uc002vwl.3; human. [P12111-1] DR AGR; HGNC:2213; -. DR CTD; 1293; -. DR DisGeNET; 1293; -. DR GeneCards; COL6A3; -. DR GeneReviews; COL6A3; -. DR HGNC; HGNC:2213; COL6A3. DR HPA; ENSG00000163359; Tissue enhanced (smooth). DR MalaCards; COL6A3; -. DR MIM; 120250; gene. DR MIM; 158810; phenotype. DR MIM; 254090; phenotype. DR MIM; 616411; phenotype. DR neXtProt; NX_P12111; -. DR OpenTargets; ENSG00000163359; -. 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; 464440; Primary dystonia, DYT27 type. DR Orphanet; 75840; Ullrich congenital muscular dystrophy. DR PharmGKB; PA26729; -. DR VEuPathDB; HostDB:ENSG00000163359; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000156462; -. DR HOGENOM; CLU_000182_1_0_1; -. DR InParanoid; P12111; -. DR OMA; KGGRQAN; -. DR OrthoDB; 5359724at2759; -. DR PhylomeDB; P12111; -. DR TreeFam; TF337483; -. DR PathwayCommons; P12111; -. 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; P12111; -. DR SIGNOR; P12111; -. DR BioGRID-ORCS; 1293; 12 hits in 1152 CRISPR screens. DR ChiTaRS; COL6A3; human. DR EvolutionaryTrace; P12111; -. DR GeneWiki; COL6A3; -. DR GenomeRNAi; 1293; -. DR Pharos; P12111; Tbio. DR PRO; PR:P12111; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P12111; Protein. DR Bgee; ENSG00000163359; Expressed in stromal cell of endometrium and 183 other cell types or tissues. DR ExpressionAtlas; P12111; baseline and differential. DR GO; GO:0005589; C:collagen type VI trimer; TAS:ProtInc. 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:0031012; C:extracellular matrix; IDA:MGI. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; ISS:BHF-UCL. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0009411; P:response to UV; IEA:Ensembl. DR CDD; cd00063; FN3; 1. DR CDD; cd22629; Kunitz_collagen_alpha3_VI; 1. DR CDD; cd01481; vWA_collagen_alpha3-VI-like; 4. DR CDD; cd01450; vWFA_subfamily_ECM; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 12. DR InterPro; IPR008160; Collagen. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR002223; Kunitz_BPTI. DR InterPro; IPR036880; Kunitz_BPTI_sf. DR InterPro; IPR020901; Prtase_inh_Kunz-CS. DR InterPro; IPR041900; vWA_collagen_alpha3-VI-like. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24020:SF13; COLLAGEN ALPHA-3(VI) CHAIN; 1. DR Pfam; PF01391; Collagen; 2. DR Pfam; PF00014; Kunitz_BPTI; 1. DR Pfam; PF00092; VWA; 12. DR PRINTS; PR00759; BASICPTASE. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00131; KU; 1. DR SMART; SM00327; VWA; 12. DR SUPFAM; SSF57362; BPTI-like; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF53300; vWA-like; 12. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS50234; VWFA; 12. DR Genevisible; P12111; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Collagen; KW Congenital muscular dystrophy; Direct protein sequencing; Disease variant; KW Disulfide bond; Dystonia; Extracellular matrix; Glycoprotein; KW Hydroxylation; Limb-girdle muscular dystrophy; Phosphoprotein; KW Protease inhibitor; Reference proteome; Repeat; Secreted; KW Serine protease inhibitor; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..3177 FT /note="Collagen alpha-3(VI) chain" FT /id="PRO_0000005847" FT DOMAIN 39..213 FT /note="VWFA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 242..419 FT /note="VWFA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 445..620 FT /note="VWFA 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 639..816 FT /note="VWFA 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 837..1009 FT /note="VWFA 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 1029..1205 FT /note="VWFA 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 1233..1404 FT /note="VWFA 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 1436..1609 FT /note="VWFA 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 1639..1812 FT /note="VWFA 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 1838..2024 FT /note="VWFA 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 2038..2097 FT /note="Collagen-like 1" FT DOMAIN 2104..2163 FT /note="Collagen-like 2" FT DOMAIN 2174..2233 FT /note="Collagen-like 3" FT DOMAIN 2249..2300 FT /note="Collagen-like 4" FT DOMAIN 2314..2373 FT /note="Collagen-like 5" FT DOMAIN 2402..2581 FT /note="VWFA 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 2619..2815 FT /note="VWFA 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 2991..3085 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 3112..3162 FT /note="BPTI/Kunitz inhibitor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT REGION 26..2038 FT /note="Nonhelical region" FT REGION 1612..1634 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2039..2375 FT /note="Triple-helical region" FT REGION 2041..2369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2376..3177 FT /note="Nonhelical region" FT REGION 2859..2890 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2957..2986 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3073..3093 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 2040..2042 FT /note="Cell attachment site" FT MOTIF 2136..2138 FT /note="Cell attachment site" FT MOTIF 2148..2150 FT /note="Cell attachment site" FT MOTIF 2154..2156 FT /note="Cell attachment site" FT MOTIF 2370..2372 FT /note="Cell attachment site" FT COMPBIAS 2108..2124 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2132..2152 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2291..2313 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 3122..3123 FT /note="Reactive bond" FT MOD_RES 433 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1225 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 2100 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2103 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2206 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2209 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2212 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2239 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2316 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2319 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2322 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:1689238" FT MOD_RES 2337 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:1689238" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 202 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 251 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2079 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2103 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT CARBOHYD 2209 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT CARBOHYD 2212 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT CARBOHYD 2322 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT CARBOHYD 2331 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2337 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT CARBOHYD 2558 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2677 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 2861 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 3037 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 2087 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 3112..3162 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 3121..3145 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT DISULFID 3137..3158 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031" FT VAR_SEQ 31..437 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045718" FT VAR_SEQ 31..236 FT /note="Missing (in isoform 2, isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_001172" FT VAR_SEQ 237..437 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043434" FT VAR_SEQ 633..832 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045719" FT VAR_SEQ 1429..1443 FT /note="AVESDAADIVFLIDS -> GEMGASEVLLGAFSI (in isoform 3 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043435" FT VAR_SEQ 1444..3177 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043436" FT VARIANT 411 FT /note="L -> V (in dbSNP:rs113716915)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058242" FT VARIANT 491 FT /note="D -> H (in dbSNP:rs112010940)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058243" FT VARIANT 492 FT /note="T -> S (in dbSNP:rs113897824)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058244" FT VARIANT 538 FT /note="T -> M (in dbSNP:rs34741387)" FT /id="VAR_047279" FT VARIANT 659 FT /note="R -> H (in dbSNP:rs36092870)" FT /id="VAR_047280" FT VARIANT 677 FT /note="R -> H (in dbSNP:rs35227432)" FT /evidence="ECO:0000269|PubMed:15689448, FT ECO:0000269|PubMed:17886299" FT /id="VAR_058245" FT VARIANT 807 FT /note="A -> T (in dbSNP:rs113155945)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058246" FT VARIANT 830 FT /note="A -> S (in dbSNP:rs77181645)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058247" FT VARIANT 886 FT /note="V -> E (in dbSNP:rs9630964)" FT /id="VAR_047281" FT VARIANT 1014 FT /note="K -> E (in BTHLM1; dbSNP:rs114284669)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058248" FT VARIANT 1064 FT /note="R -> Q (in dbSNP:rs112638391)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058249" FT VARIANT 1088 FT /note="K -> Q (in dbSNP:rs11896521)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_047282" FT VARIANT 1386 FT /note="E -> K (in BTHLM1; dbSNP:rs146092501)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058250" FT VARIANT 1395 FT /note="R -> Q (in dbSNP:rs80272723)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058251" FT VARIANT 1467 FT /note="N -> D (in BTHLM1; dbSNP:rs138049094)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058252" FT VARIANT 1576 FT /note="R -> Q (in dbSNP:rs61729839)" FT /evidence="ECO:0000269|PubMed:15689448, FT ECO:0000269|PubMed:17886299" FT /id="VAR_058253" FT VARIANT 1632 FT /note="R -> Q (in dbSNP:rs111231885)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058254" FT VARIANT 1674 FT /note="D -> N (in UCMD1; dbSNP:rs778940391)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058255" FT VARIANT 1679 FT /note="G -> E (in BTHLM1; dbSNP:rs121434553)" FT /evidence="ECO:0000269|PubMed:15689448, FT ECO:0000269|PubMed:9536084" FT /id="VAR_001910" FT VARIANT 1687 FT /note="P -> S (in dbSNP:rs35273032)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058256" FT VARIANT 1726 FT /note="L -> R (in BTHLM1; dbSNP:rs121434555)" FT /evidence="ECO:0000269|PubMed:17886299" FT /id="VAR_058257" FT VARIANT 1985 FT /note="V -> M (in BTHLM1; dbSNP:rs200478135)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058258" FT VARIANT 2047 FT /note="G -> D (in BTHLM1)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058259" FT VARIANT 2056 FT /note="G -> R (in BTHLM1)" FT /evidence="ECO:0000269|PubMed:10399756" FT /id="VAR_058260" FT VARIANT 2080 FT /note="G -> D (in BTHLM1; dbSNP:rs794727188)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058261" FT VARIANT 2218 FT /note="P -> L (in dbSNP:rs36117715)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_047283" FT VARIANT 2431 FT /note="D -> V" FT /evidence="ECO:0000269|PubMed:1689238, FT ECO:0000269|PubMed:17886299" FT /id="VAR_058262" FT VARIANT 2453 FT /note="E -> K (in dbSNP:rs886044364)" FT /evidence="ECO:0000269|PubMed:17886299" FT /id="VAR_058263" FT VARIANT 2501 FT /note="R -> H (in DYT27; dbSNP:rs541928674)" FT /evidence="ECO:0000269|PubMed:26004199" FT /id="VAR_073836" FT VARIANT 2554 FT /note="A -> T (in DYT27; dbSNP:rs786205870)" FT /evidence="ECO:0000269|PubMed:26004199" FT /id="VAR_073837" FT VARIANT 2805 FT /note="N -> T (in dbSNP:rs35848091)" FT /id="VAR_047284" FT VARIANT 2831 FT /note="D -> H (in dbSNP:rs36104025)" FT /evidence="ECO:0000269|PubMed:15689448, FT ECO:0000269|PubMed:17886299, ECO:0000269|PubMed:9536084" FT /id="VAR_001911" FT VARIANT 2927 FT /note="M -> T (in dbSNP:rs6728818)" FT /evidence="ECO:0000269|PubMed:1689238" FT /id="VAR_047285" FT VARIANT 2941 FT /note="A -> V (in dbSNP:rs11903206)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058264" FT VARIANT 2988 FT /note="M -> V (in dbSNP:rs11690358)" FT /evidence="ECO:0000269|PubMed:1689238, FT ECO:0000269|PubMed:17886299" FT /id="VAR_047286" FT VARIANT 3012 FT /note="A -> P (in dbSNP:rs2270669)" FT /evidence="ECO:0000269|PubMed:1689238" FT /id="VAR_047287" FT VARIANT 3043 FT /note="R -> H (in DYT27; dbSNP:rs552651651)" FT /evidence="ECO:0000269|PubMed:26004199" FT /id="VAR_073838" FT VARIANT 3069 FT /note="T -> I (in dbSNP:rs1131296)" FT /evidence="ECO:0000269|PubMed:17886299" FT /id="VAR_047288" FT VARIANT 3082 FT /note="P -> R (in DYT27; dbSNP:rs182976977)" FT /evidence="ECO:0000269|PubMed:26004199" FT /id="VAR_073839" FT CONFLICT 127..128 FT /note="QS -> AK (in Ref. 6; AAB24261)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="R -> L (in Ref. 6; AAB24261)" FT /evidence="ECO:0000305" FT CONFLICT 381 FT /note="A -> V (in Ref. 3; BAG65607)" FT /evidence="ECO:0000305" FT CONFLICT 608 FT /note="F -> S (in Ref. 3; BAG65607)" FT /evidence="ECO:0000305" FT CONFLICT 885 FT /note="K -> E (in Ref. 5; AAI44596/AAI50626)" FT /evidence="ECO:0000305" FT CONFLICT 1282 FT /note="V -> A (in Ref. 1; CAA36267)" FT /evidence="ECO:0000305" FT CONFLICT 1353..1354 FT /note="DD -> VV (in Ref. 1; CAA36267)" FT /evidence="ECO:0000305" FT CONFLICT 2157 FT /note="P -> R (in Ref. 8; CAA29557)" FT /evidence="ECO:0000305" FT CONFLICT 2257 FT /note="A -> R (in Ref. 1; CAA36267 and 7; M20778)" FT /evidence="ECO:0000305" FT CONFLICT 2287 FT /note="R -> P (in Ref. 1; CAA36267 and 7; M20778)" FT /evidence="ECO:0000305" FT CONFLICT 2357 FT /note="D -> R (in Ref. 1; CAA36267 and 7; M20778)" FT /evidence="ECO:0000305" FT CONFLICT 2367 FT /note="K -> R (in Ref. 1; CAA36267 and 7; M20778)" FT /evidence="ECO:0000305" FT CONFLICT 2441 FT /note="R -> T (in Ref. 1; CAA36267)" FT /evidence="ECO:0000305" FT CONFLICT 2956 FT /note="Missing (in Ref. 1; CAA36267)" FT /evidence="ECO:0000305" FT CONFLICT 2992 FT /note="S -> L (in Ref. 1; CAA36267)" FT /evidence="ECO:0000305" FT STRAND 1637..1645 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1652..1669 FT /evidence="ECO:0007829|PDB:6SNK" FT STRAND 1675..1691 FT /evidence="ECO:0007829|PDB:6SNK" FT TURN 1693..1695 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1699..1706 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1719..1729 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1733..1735 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1739..1741 FT /evidence="ECO:0007829|PDB:6SNK" FT STRAND 1745..1753 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1760..1768 FT /evidence="ECO:0007829|PDB:6SNK" FT STRAND 1771..1780 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1783..1789 FT /evidence="ECO:0007829|PDB:6SNK" FT STRAND 1790..1792 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1793..1795 FT /evidence="ECO:0007829|PDB:6SNK" FT STRAND 1796..1801 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1802..1808 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 1809..1820 FT /evidence="ECO:0007829|PDB:6SNK" FT HELIX 3110..3113 FT /evidence="ECO:0007829|PDB:1KTH" FT STRAND 3120..3122 FT /evidence="ECO:0007829|PDB:1KTH" FT STRAND 3125..3131 FT /evidence="ECO:0007829|PDB:1KTH" FT TURN 3132..3135 FT /evidence="ECO:0007829|PDB:1KTH" FT STRAND 3136..3142 FT /evidence="ECO:0007829|PDB:1KTH" FT STRAND 3144..3146 FT /evidence="ECO:0007829|PDB:1KTH" FT STRAND 3152..3154 FT /evidence="ECO:0007829|PDB:1KTH" FT HELIX 3155..3162 FT /evidence="ECO:0007829|PDB:1KTH" SQ SEQUENCE 3177 AA; 343669 MW; 56D54CAC4FBB30AF CRC64; MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA DVKNGAAADI IFLVDSSWTI GEEHFQLVRE FLYDVVKSLA VGENDFHFAL VQFNGNPHTE FLLNTYRTKQ EVLSHISNMS YIGGTNQTGK GLEYIMQSHL TKAAGSRAGD GVPQVIVVLT DGHSKDGLAL PSAELKSADV NVFAIGVEDA DEGALKEIAS EPLNMHMFNL ENFTSLHDIV GNLVSCVHSS VSPERAGDTE TLKDITAQDS ADIIFLIDGS NNTGSVNFAV ILDFLVNLLE KLPIGTQQIR VGVVQFSDEP RTMFSLDTYS TKAQVLGAVK ALGFAGGELA NIGLALDFVV ENHFTRAGGS RVEEGVPQVL VLISAGPSSD EIRYGVVALK QASVFSFGLG AQAASRAELQ HIATDDNLVF TVPEFRSFGD LQEKLLPYIV GVAQRHIVLK PPTIVTQVIE VNKRDIVFLV DGSSALGLAN FNAIRDFIAK VIQRLEIGQD LIQVAVAQYA DTVRPEFYFN THPTKREVIT AVRKMKPLDG SALYTGSALD FVRNNLFTSS AGYRAAEGIP KLLVLITGGK SLDEISQPAQ ELKRSSIMAF AIGNKGADQA ELEEIAFDSS LVFIPAEFRA APLQGMLPGL LAPLRTLSGT PEVHSNKRDI IFLLDGSANV GKTNFPYVRD FVMNLVNSLD IGNDNIRVGL VQFSDTPVTE FSLNTYQTKS DILGHLRQLQ LQGGSGLNTG SALSYVYANH FTEAGGSRIR EHVPQLLLLL TAGQSEDSYL QAANALTRAG ILTFCVGASQ ANKAELEQIA FNPSLVYLMD DFSSLPALPQ QLIQPLTTYV SGGVEEVPLA QPESKRDILF LFDGSANLVG QFPVVRDFLY KIIDELNVKP EGTRIAVAQY SDDVKVESRF DEHQSKPEIL NLVKRMKIKT GKALNLGYAL DYAQRYIFVK SAGSRIEDGV LQFLVLLVAG RSSDRVDGPA SNLKQSGVVP FIFQAKNADP AELEQIVLSP AFILAAESLP KIGDLHPQIV NLLKSVHNGA PAPVSGEKDV VFLLDGSEGV RSGFPLLKEF VQRVVESLDV GQDRVRVAVV QYSDRTRPEF YLNSYMNKQD VVNAVRQLTL LGGPTPNTGA ALEFVLRNIL VSSAGSRITE GVPQLLIVLT ADRSGDDVRN PSVVVKRGGA VPIGIGIGNA DITEMQTISF IPDFAVAIPT FRQLGTVQQV ISERVTQLTR EELSRLQPVL QPLPSPGVGG KRDVVFLIDG SQSAGPEFQY VRTLIERLVD YLDVGFDTTR VAVIQFSDDP KVEFLLNAHS SKDEVQNAVQ RLRPKGGRQI NVGNALEYVS RNIFKRPLGS RIEEGVPQFL VLISSGKSDD EVDDPAVELK QFGVAPFTIA RNADQEELVK ISLSPEYVFS VSTFRELPSL EQKLLTPITT LTSEQIQKLL ASTRYPPPAV ESDAADIVFL IDSSEGVRPD GFAHIRDFVS RIVRRLNIGP SKVRVGVVQF SNDVFPEFYL KTYRSQAPVL DAIRRLRLRG GSPLNTGKAL EFVARNLFVK SAGSRIEDGV PQHLVLVLGG KSQDDVSRFA QVIRSSGIVS LGVGDRNIDR TELQTITNDP RLVFTVREFR ELPNIEERIM NSFGPSAATP APPGVDTPPP SRPEKKKADI VFLLDGSINF RRDSFQEVLR FVSEIVDTVY EDGDSIQVGL VQYNSDPTDE FFLKDFSTKR QIIDAINKVV YKGGRHANTK VGLEHLRVNH FVPEAGSRLD QRVPQIAFVI TGGKSVEDAQ DVSLALTQRG VKVFAVGVRN IDSEEVGKIA SNSATAFRVG NVQELSELSE QVLETLHDAM HETLCPGVTD AAKACNLDVI LGFDGSRDQN VFVAQKGFES KVDAILNRIS QMHRVSCSGG RSPTVRVSVV ANTPSGPVEA FDFDEYQPEM LEKFRNMRSQ HPYVLTEDTL KVYLNKFRQS SPDSVKVVIH FTDGADGDLA DLHRASENLR QEGVRALILV GLERVVNLER LMHLEFGRGF MYDRPLRLNL LDLDYELAEQ LDNIAEKACC GVPCKCSGQR GDRGPIGSIG PKGIPGEDGY RGYPGDEGGP GERGPPGVNG TQGFQGCPGQ RGVKGSRGFP GEKGEVGEIG LDGLDGEDGD KGLPGSSGEK GNPGRRGDKG PRGEKGERGD VGIRGDPGNP GQDSQERGPK GETGDLGPMG VPGRDGVPGG PGETGKNGGF GRRGPPGAKG NKGGPGQPGF EGEQGTRGAQ GPAGPAGPPG LIGEQGISGP RGSGGAAGAP GERGRTGPLG RKGEPGEPGP KGGIGNRGPR GETGDDGRDG VGSEGRRGKK GERGFPGYPG PKGNPGEPGL NGTTGPKGIR GRRGNSGPPG IVGQKGDPGY PGPAGPKGNR GDSIDQCALI QSIKDKCPCC YGPLECPVFP TELAFALDTS EGVNQDTFGR MRDVVLSIVN DLTIAESNCP RGARVAVVTY NNEVTTEIRF ADSKRKSVLL DKIKNLQVAL TSKQQSLETA MSFVARNTFK RVRNGFLMRK VAVFFSNTPT RASPQLREAV LKLSDAGITP LFLTRQEDRQ LINALQINNT AVGHALVLPA GRDLTDFLEN VLTCHVCLDI CNIDPSCGFG SWRPSFRDRR AAGSDVDIDM AFILDSAETT TLFQFNEMKK YIAYLVRQLD MSPDPKASQH FARVAVVQHA PSESVDNASM PPVKVEFSLT DYGSKEKLVD FLSRGMTQLQ GTRALGSAIE YTIENVFESA PNPRDLKIVV LMLTGEVPEQ QLEEAQRVIL QAKCKGYFFV VLGIGRKVNI KEVYTFASEP NDVFFKLVDK STELNEEPLM RFGRLLPSFV SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK FGHKQVNVPN NVTSSPTSNP VTTTKPVTTT KPVTTTTKPV TTTTKPVTII NQPSVKPAAA KPAPAKPVAA KPVATKMATV RPPVAVKPAT AAKPVAAKPA AVRPPAAAAA KPVATKPEVP RPQAAKPAAT KPATTKPMVK MSREVQVFEI TENSAKLHWE RAEPPGPYFY DLTVTSAHDQ SLVLKQNLTV TDRVIGGLLA GQTYHVAVVC YLRSQVRATY HGSFSTKKSQ PPPPQPARSA SSSTINLMVS TEPLALTETD ICKLPKDEGT CRDFILKWYY DPNTKSCARF WYGGCGGNEN KFGSQKECEK VCAPVLAKPG VISVMGT //