Detail Information for IndEnz0002018152
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