| IED ID | IndEnz0002018152 |
| Enzyme Type ID | protease018152 |
| Protein Name |
Collagen alpha-3 VI chain |
| Gene Name | COL6A3 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MRKHRHLPLVAVFCLFLSGFPTTHAQQQQADVKNGAAADIIFLVDSSWTIGEEHFQLVREFLYDVVKSLAVGENDFHFALVQFNGNPHTEFLLNTYRTKQEVLSHISNMSYIGGTNQTGKGLEYIMQSHLTKAAGSRAGDGVPQVIVVLTDGHSKDGLALPSAELKSADVNVFAIGVEDADEGALKEIASEPLNMHMFNLENFTSLHDIVGNLVSCVHSSVSPERAGDTETLKDITAQDSADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELANIGLALDFVVENHFTRAGGSRVEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDNLVFTVPEFRSFGDLQEKLLPYIVGVAQRHIVLKPPTIVTQVIEVNKRDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALYTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVFIPAEFRAAPLQGMLPGLLAPLRTLSGTPEVHSNKRDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLNTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVYLMDDFSSLPALPQQLIQPLTTYVSGGVEEVPLAQPESKRDILFLFDGSANLVGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALNLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFILAAESLPKIGDLHPQIVNLLKSVHNGAPAPVSGEKDVVFLLDGSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPNTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAVAIPTFRQLGTVQQVISERVTQLTREELSRLQPVLQPLPSPGVGGKRDVVFLIDGSQSAGPEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQINVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIARNADQEELVKISLSPEYVFSVSTFRELPSLEQKLLTPITTLTSEQIQKLLASTRYPPPAVESDAADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLNTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVFTVREFRELPNIEERIMNSFGPSAATPAPPGVDTPPPSRPEKKKADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHANTKVGLEHLRVNHFVPEAGSRLDQRVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSATAFRVGNVQELSELSEQVLETLHDAMHETLCPGVTDAAKACNLDVILGFDGSRDQNVFVAQKGFESKVDAILNRISQMHRVSCSGGRSPTVRVSVVANTPSGPVEAFDFDEYQPEMLEKFRNMRSQHPYVLTEDTLKVYLNKFRQSSPDSVKVVIHFTDGADGDLADLHRASENLRQEGVRALILVGLERVVNLERLMHLEFGRGFMYDRPLRLNLLDLDYELAEQLDNIAEKACCGVPCKCSGQRGDRGPIGSIGPKGIPGEDGYRGYPGDEGGPGERGPPGVNGTQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQDSQERGPKGETGDLGPMGVPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRGAQGPAGPAGPPGLIGEQGISGPRGSGGAAGAPGERGRTGPLGRKGEPGEPGPKGGIGNRGPRGETGDDGRDGVGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDSIDQCALIQSIKDKCPCCYGPLECPVFPTELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAESNCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVALTSKQQSLETAMSFVARNTFKRVRNGFLMRKVAVFFSNTPTRASPQLREAVLKLSDAGITPLFLTRQEDRQLINALQINNTAVGHALVLPAGRDLTDFLENVLTCHVCLDICNIDPSCGFGSWRPSFRDRRAAGSDVDIDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPKASQHFARVAVVQHAPSESVDNASMPPVKVEFSLTDYGSKEKLVDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDLKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRKVNIKEVYTFASEPNDVFFKLVDKSTELNEEPLMRFGRLLPSFVSSENAFYLSPDIRKQCDWFQGDQPTKNLVKFGHKQVNVPNNVTSSPTSNPVTTTKPVTTTKPVTTTTKPVTTTTKPVTIINQPSVKPAAAKPAPAKPVAAKPVATKMATVRPPVAVKPATAAKPVAAKPAAVRPPAAAAAKPVATKPEVPRPQAAKPAATKPATTKPMVKMSREVQVFEITENSAKLHWERAEPPGPYFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCYLRSQVRATYHGSFSTKKSQPPPPQPARSASSSTINLMVSTEPLALTETDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAPVLAKPGVISVMGT |
| Enzyme Length | 3177 |
| Uniprot Accession Number | P12111 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Collagen VI acts as a cell-binding protein. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (6); Beta strand (5); Chain (1); Compositional bias (3); Disulfide bond (4); Domain (19); Glycosylation (15); Helix (2); Modified residue (12); Motif (5); Natural variant (39); Region (8); Sequence conflict (20); Signal peptide (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Cell adhesion;Collagen;Congenital muscular dystrophy;Direct protein sequencing;Disease variant;Disulfide bond;Dystonia;Extracellular matrix;Glycoprotein;Hydroxylation;Limb-girdle muscular dystrophy;Phosphoprotein;Protease inhibitor;Reference proteome;Repeat;Secreted;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | MOD_RES 433; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21406692; MOD_RES 1225; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:24275569; MOD_RES 2100; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2103; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2206; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2209; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2212; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2239; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2316; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2319; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2322; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:1689238; MOD_RES 2337; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:1689238 |
| Post Translational Modification | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:1689238}.; PTM: The N-terminus is blocked. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (4) |
| Cross Reference PDB | 1KNT; 1KTH; 1KUN; 2KNT; 6SNK; |
| Mapped Pubmed ID | 10508235; 10934207; 11259413; 11572855; 11785962; 12011280; 12077460; 12473679; 12475640; 1311092; 1323838; 14500733; 15044469; 15383545; 1544908; 15563506; 1577494; 15965965; 16293224; 16591531; 16613849; 16754661; 171650; 17170699; 17918257; 18366090; 18487197; 18622425; 19075007; 19693541; 19834535; 19837927; 19851296; 20198315; 20379614; 20470363; 2059554; 20711500; 21789315; 21878990; 21935455; 21967573; 23414517; 23818951; 2430969; 24443028; 24647224; 24719315; 24801232; 25204870; 25337653; 2543975; 25449070; 25635128; 26338966; 26687111; 26872670; 27729337; 2809592; 28403201; 29066004; 29465610; 29620224; 29894794; 30014607; 30066698; 30695889; 30706156; 30896449; 31122696; 31286980; 31425922; 3173483; 32037012; 32245981; 32389683; 32448721; 32719005; 32934754; 33214660; 33749658; 33964895; 3938630; 6307276; 6439184; 6809411; 710450; 7852349; 8118028; 8344274; 8440685; 8900172; 9054364; 9252349; 9334164; 9545296; 9560306; 9582318; 9761897; |
| Motif | MOTIF 2040..2042; /note=Cell attachment site; MOTIF 2136..2138; /note=Cell attachment site; MOTIF 2148..2150; /note=Cell attachment site; MOTIF 2154..2156; /note=Cell attachment site; MOTIF 2370..2372; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 343,669 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |