IED ID | IndEnz0002017399 |
Enzyme Type ID | protease017399 |
Protein Name |
Collagen alpha-1 III chain |
Gene Name | Col3a1 |
Organism | Mus musculus (Mouse) |
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MMSFVQSGTWFLLTLLHPTLILAQQSNVDELGCSHLGQSYESRDVWKPEPCQICVCDSGSVLCDDIICDEEPLDCPNPEIPFGECCAICPQPSTPAPVLPDGHGPQGPKGDPGPPGIPGRNGDPGLPGQPGLPGPPGSPGICESCPTGGQNYSPQFDSYDVKSGVGGMGGYPGPAGPPGPPGPPGSSGHPGSPGSPGYQGPPGEPGQAGPAGPPGPPGALGPAGPAGKDGESGRPGRPGERGLPGPPGIKGPAGMPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGDNGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGSPGQRGEPGPQGHAGAQGPPGPPGNNGSPGGKGEMGPAGIPGAPGLIGARGPPGPAGTNGIPGTRGPSGEPGKNGAKGEPGARGERGEAGSPGIPGPKGEDGKDGSPGEPGANGLPGAAGERGPSGFRGPAGPNGIPGEKGPPGERGGPGPAGPRGVAGEPGRDGTPGGPGIRGMPGSPGGPGNDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGLPGPAGKNGETGPQGPPGPTGPAGDKGDSGPPGPQGLQGIPGTGGPPGENGKPGEPGPKGEVGAPGAPGGKGDSGAPGERGPPGTAGIPGARGGAGPPGPEGGKGPAGPPGPPGASGSPGLQGMPGERGGPGSPGPKGEKGEPGGAGADGVPGKDGPRGPAGPIGPPGPAGQPGDKGEGGSPGLPGIAGPRGGPGERGEHGPPGPAGFPGAPGQNGEPGAKGERGAPGEKGEGGPPGPAGPTGSSGPAGPPGPQGVKGERGSPGGPGTAGFPGGRGLPGPPGNNGNPGPPGPSGAPGKDGPPGPAGNSGSPGNPGIAGPKGDAGQPGEKGPPGAQGPPGSPGPLGIAGLTGARGLAGPPGMPGPRGSPGPQGIKGESGKPGASGHNGERGPPGPQGLPGQPGTAGEPGRDGNPGSDGQPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPSGKSGDRGETGPAGPSGAPGPAGARGAPGPQGPRGDKGETGERGSNGIKGHRGFPGNPGPPGSPGAAGHQGAIGSPGPAGPRGPVGPHGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGGAAAIAGVGGEKSGGFSPYYGDDPMDFKINTEEIMSSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKMDAIKVFCNMETGETCINASPMTVPRKHWWTDSGAEKKHVWFGESMNGGFQFSYGPPDLPEDVVDVQLAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKSLKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYQTRKAMRLPIIDIAPYDIGGPDQEFGVDIGPVCFL |
Enzyme Length | 1464 |
Uniprot Accession Number | P08121 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12. {ECO:0000269|PubMed:21768377}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (8); Disulfide bond (7); Domain (2); Glycosylation (1); Metal binding (5); Modified residue (6); Propeptide (2); Region (3); Signal peptide (1) |
Keywords | Calcium;Collagen;Disulfide bond;Extracellular matrix;Glycoprotein;Hydroxylation;Metal-binding;Reference proteome;Repeat;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. |
Modified Residue | MOD_RES 262; /note=5-hydroxylysine; alternate; /evidence=ECO:0000250; MOD_RES 283; /note=5-hydroxylysine; /evidence=ECO:0000250; MOD_RES 859; /note=5-hydroxylysine; /evidence=ECO:0000250; MOD_RES 976; /note=5-hydroxylysine; /evidence=ECO:0000250; MOD_RES 1093; /note=5-hydroxylysine; /evidence=ECO:0000250; MOD_RES 1105; /note=5-hydroxylysine; /evidence=ECO:0000250 |
Post Translational Modification | PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. {ECO:0000250}. |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000250 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10022501; 10088787; 10458099; 10995453; 11044607; 11210178; 11217851; 11283268; 12466851; 12571105; 12592609; 12659831; 12874293; 1347472; 1358796; 14559231; 14758483; 15371327; 15582152; 15733672; 16081813; 16107646; 16236725; 16314533; 16452166; 16556917; 16602821; 16818445; 17029294; 17135260; 17453912; 17662583; 17881772; 17950069; 17960558; 18554416; 1879336; 18816857; 19217425; 19334288; 19411759; 19560165; 1981051; 20498044; 20548288; 20587693; 20858856; 20864640; 20944625; 21041952; 21071432; 21173153; 21252470; 21266775; 21267068; 21268075; 21308778; 21352494; 21386911; 21511879; 21512159; 21606205; 21677750; 21979435; 2209468; 22151329; 22158707; 22159717; 22171010; 22206015; 22235340; 22238662; 22351047; 22560297; 22573622; 22682244; 23273220; 23377784; 23630948; 23658023; 23907538; 23921644; 24006456; 24192074; 24626604; 24820199; 24952961; 24994653; 25330296; 25344368; 25516967; 25572963; 25715398; 25715693; 25795282; 26362633; 26446156; 26494538; 26821812; 27249171; 27249321; 27265328; 27527664; 27648120; 27665369; 27746183; 27770432; 27856617; 27870967; 27939132; 28049691; 28052872; 28071719; 28218627; 28237967; 28527294; 28535371; 28684544; 28809397; 29191093; 29551664; 29593327; 29618652; 2981217; 30566624; 30635555; 30670377; 30738849; 30936179; 31056650; 31319059; 31624071; 31634485; 31639107; 31655293; 31844321; 32546759; 32580935; 32882513; 32979396; 33504048; 33763067; 34003106; 34189436; 34205850; 34248495; 34830270; 7752808; 7777502; 7825727; 7919967; 8069308; 8088797; 8188220; 8244386; 8661741; 8678985; 8686743; 8785585; 8849351; 8900172; 8948440; 8984825; 9021163; 9050868; 9164858; 9382709; 9614124; 9832566; 9870870; |
Motif | |
Gene Encoded By | |
Mass | 138,943 |
Kinetics | |
Metal Binding | METAL 1278; /note=Calcium; /evidence=ECO:0000250; METAL 1280; /note=Calcium; /evidence=ECO:0000250; METAL 1281; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 1283; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 1286; /note=Calcium; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |