Detail Information for IndEnz0002009800
IED ID IndEnz0002009800
Enzyme Type ID protease009800
Protein Name Serpin H1
47 kDa heat shock protein
Collagen-binding protein
Colligin
Serine protease inhibitor J6
Gene Name Serpinh1 Cbp1 Hsp47
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 MRSLLLGTLCLLAVALAAEVKKPLEAAAPGTAEKLSSKATTLAERSTGLAFSLYQAMAKDQAVENILLSPLVVASSLGLVSLGGKATTASQAKAVLSAEKLRDEEVHTGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWASQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVTMMHRTGLYNYYDDEKEKLQMVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKAWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWDTEGNPFDQDIYGREELRSPKLFYADHPFIFLVRDNQSGSLLFIGRLVRPKGDKMRDEL
Enzyme Length 417
Uniprot Accession Number P19324
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Glycosylation (3); Modified residue (5); Motif (1); Sequence conflict (7); Signal peptide (1); Site (1)
Keywords Acetylation;Chaperone;Direct protein sequencing;Endoplasmic reticulum;Glycoprotein;Phosphoprotein;Reference proteome;Signal;Stress response
Interact With
Induction INDUCTION: By heat shock and retinoic acid.
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
Modified Residue MOD_RES 93; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 140; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P50454; MOD_RES 206; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 295; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 318; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23806337
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000269|PubMed:1317794
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10862616; 10995453; 12466851; 12748967; 12842808; 1309665; 14610273; 15121863; 15282337; 15522896; 15582152; 16326708; 16484215; 16525016; 16602821; 18093850; 18799693; 19411759; 19521500; 20094730; 21144841; 21335239; 21606205; 21862448; 22159717; 22295344; 22492985; 22925884; 23212911; 23269685; 23587755; 23624931; 24292013; 24295791; 24454956; 24586547; 24650661; 25525267; 26091621; 26196532; 26921296; 27076780; 27477081; 28071719; 28802097; 29351844; 29363541; 29512284; 30786278; 31393098; 32562852; 32714072; 32716577; 34244516; 7656593; 7905876; 8018053; 8187816; 8269704; 8299716; 8848834; 8944545; 9294190; 9853961; 9880236; 9880238;
Motif MOTIF 414..417; /note=Prevents secretion from ER; /evidence=ECO:0000305
Gene Encoded By
Mass 46,534
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda