CO6A3_HUMAN
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 03-AUG-2022, entry version 239.
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}.
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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; 6.
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 GlyGen; P12111; 23 sites, 36 N-linked glycans (6 sites), 5 O-linked glycans (6 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; P12111; -.
DR PeptideAtlas; P12111; -.
DR PRIDE; 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; 94 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 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 myopathy.
DR Orphanet; 75840; Congenital muscular dystrophy, Ullrich type.
DR Orphanet; 464440; Primary dystonia, DYT27 type.
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; TTAMRSE; -.
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 1074 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 181 other tissues.
DR ExpressionAtlas; P12111; baseline and differential.
DR Genevisible; P12111; HS.
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 CDD; cd00063; FN3; 1.
DR CDD; cd00109; KU; 1.
DR CDD; cd01481; vWA_collagen_alpha3-VI-like; 4.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.410; -; 12.
DR Gene3D; 4.10.410.10; -; 1.
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 Pfam; PF01391; Collagen; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 11.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 12.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF53300; SSF53300; 12.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50234; VWFA; 12.
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
