SERPINH1
Identifiers
Aliases	SERPINH1, AsTP3, CBP1, CBP2, HSP47, OI10, PIG14, PPROM, RA-A47, SERPINH2, gp46, serpin family H member 1
External IDs	OMIM: 600943 MGI: 88283 HomoloGene: 20331 GeneCards: SERPINH1
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.5 Start 75,562,056 bp[1] End 75,572,783 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 E1 Start 98,994,583 bp[2] End 99,002,446 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium smooth muscle tissue pericardium right coronary artery ascending aorta left uterine tube upper lobe of left lung myometrium left coronary artery canal of the cervix Top expressed in dermis molar ascending aorta calvaria aortic valve atrium body of femur belly cord hand maxillary prominence More reference expression data BioGPS More reference expression data
Gene ontology Molecular function unfolded protein binding collagen binding RNA binding serine-type endopeptidase inhibitor activity Cellular component cytoplasm membrane raft endoplasmic reticulum lumen extracellular exosome endoplasmic reticulum-Golgi intermediate compartment extracellular space endoplasmic reticulum collagen-containing extracellular matrix Biological process response to unfolded protein protein maturation chondrocyte development involved in endochondral bone morphogenesis collagen biosynthetic process collagen fibril organization negative regulation of endopeptidase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 871 12406 Ensembl ENSG00000149257 ENSMUSG00000070436 UniProt P50454 P19324 RefSeq (mRNA) NM_001207014 NM_001235 NM_001111043 NM_001111044 NM_009825 NM_001285776 RefSeq (protein) NP_001193943 NP_001226 NP_001104513 NP_001104514 NP_001272705 NP_033955 Location (UCSC) Chr 11: 75.56 – 75.57 Mb Chr 7: 98.99 – 99 Mb PubMed search [3] [4]
Wikidata
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Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen.^[5][6]

Function

This protein is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 is expressed in the endoplasmic reticulum. These cells synthesize and secrete type I and type II collagen. ^[7] The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. HSP47 is essential for the correct folding of procollagen. Antibodies directed to this protein have been found in patients with rheumatoid arthritis.^[5]

Structure

HSP47 contains 3 beta sheets and 9 alpha helices. After binding with collagen no conformation change is observed.^[8]

Interactions

Heat shock protein 47 has been shown to interact with collagens I, II, III, IV and V.^[9] It is involved in the secretion of collagen as well as the processing, assembly, and folding of collagen proteins. Hsp 47 binds specifically to procollagen and collagen only. The protein recognizes the triple helix of procollagen, two HSP47 proteins will bind to the leading and trailing strands of procollagen.^[8]

Research on role in preventing deep vein thrombosis

Research published in 2023 indicates a potential role of HSP47 regarding deep vein thrombosis.^{[10] [11]} This initial research will be followed by additional studies.

Role in Fibrosis

Fibrosis is the scarring of connective tissue, one attribute is the excess deposition of collagen in the extracellular matrix of tissue. Research has shown that HSPs have a role in fibrotic diseases.^[12] HSP47 has been shown to be pro-fibrosis in various fibrotic diseases. During the process of fibrosis, HSP47 is expressed and is involved in the production of collagen.^[13] HSP47 could be a potential therapeutic agent for fibrotic disease, a down-regulation of HSP47 leads to decreased fibrotic progression.^[14]