Heat shock protein 47

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)
End	75,572,783 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	99,002,446 bp
RNA expression pattern
	Top expressed in
	smooth muscle tissue; ; ovary; ; cervix; ; lung; ; connective tissue;
	More reference expression data
	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
	871
	12406
	ENSG00000149257
	ENSMUSG00000070436
	P50454
	P19324
	NM_001207014; NM_001235
	NM_001111043; NM_001111044; NM_009825; NM_001285776
	NP_001193943; NP_001226
	NP_001104513; NP_001104514; NP_001272705; NP_033955
	Wikidata
View/Edit Human	View/Edit Mouse

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. Autoantibodies to this protein have been found in patients with rheumatoid arthritis.^[5]

Interactions[]

Heat shock protein 47 has been shown to interact with collagens I, II, III, IV and V.^[8]

References[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000149257 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000070436 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)".
^ Dafforn TR, Della M, Miller AD (December 2001). "The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis". The Journal of Biological Chemistry. 276 (52): 49310–9. doi:10.1074/jbc.M108896200. PMID 11592970.
^ Williams, R. Sanders (21 March 2000). "Heat Shock Protein 47: A Chaperone for the Fibrous Cap?". Circulation. 101 (11): 1227–1228. doi:10.1161/01.CIR.101.11.1227. PMID 10725278. Retrieved 11 December 2017.
^ Mala JG, Rose C (November 2010). "Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?". Life Sciences. 87 (19–22): 579–86. doi:10.1016/j.lfs.2010.09.024. PMID 20888348.

Further reading[]

Razzaque MS, Taguchi T (October 1999). "The possible role of colligin/HSP47, a collagen-binding protein, in the pathogenesis of human and experimental fibrotic diseases". Histology and Histopathology. 14 (4): 1199–212. PMID 10506936.
Gettins PG (December 2002). "Serpin structure, mechanism, and function". Chemical Reviews. 102 (12): 4751–804. doi:10.1021/cr010170. PMID 12475206.
Clarke EP, Sanwal BD (January 1992). "Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1129 (2): 246–8. doi:10.1016/0167-4781(92)90498-o. PMID 1309665.
Ikegawa S, Sudo K, Okui K, Nakamura Y (1995). "Isolation, characterization and chromosomal assignment of human colligin-2 gene (CBP2)". Cytogenetics and Cell Genetics. 71 (2): 182–6. doi:10.1159/000134103. PMID 7656593.
Ikegawa S, Nakamura Y (July 1997). "Structure of the gene encoding human colligin-2 (CBP2)". Gene. 194 (2): 301–3. doi:10.1016/S0378-1119(97)00209-6. PMID 9272875.
Bekri S, Adélaïde J, Merscher S, Grosgeorge J, Caroli-Bosc F, Perucca-Lostanlen D, Kelley PM, Pébusque MJ, Theillet C, Birnbaum D, Gaudray P (1998). "Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma". Cytogenetics and Cell Genetics. 79 (1–2): 125–31. doi:10.1159/000134699. PMID 9533029.
Hattori T, Fujisawa T, Sasaki K, Yutani Y, Nakanishi T, Takahashi K, Takigawa M (April 1998). "Isolation and characterization of a rheumatoid arthritis-specific antigen (RA-A47) from a human chondrocytic cell line (HCS-2/8)". Biochemical and Biophysical Research Communications. 245 (3): 679–83. doi:10.1006/bbrc.1998.8505. PMID 9588174.
Nagai N, Yorihuzi T, Hosokawa N, Nagata K (February 1999). "The human genome has only one functional hsp47 gene (CBP2) and a pseudogene (pshsp47)". Gene. 227 (2): 241–8. doi:10.1016/S0378-1119(98)00592-7. PMID 10023073.
Hebert C, Norris K, Della Coletta R, Reynolds M, Ordóñez J, Sauk JJ (May 1999). "Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines". Journal of Cellular Biochemistry. 73 (2): 248–58. doi:10.1002/(SICI)1097-4644(19990501)73:2<248::AID-JCB11>3.0.CO;2-A. PMID 10227388.
Koide T, Aso A, Yorihuzi T, Nagata K (September 2000). "Conformational requirements of collagenous peptides for recognition by the chaperone protein HSP47". The Journal of Biological Chemistry. 275 (36): 27957–63. doi:10.1074/jbc.M003026200. PMID 10862616.
Hattori T, Takahash K, Yutani Y, Fujisawa T, Nakanishi T, Takigawa M (2001). "Rheumatoid arthritis-related antigen 47kDa (RA-A47) is a product of colligin-2 and acts as a human HSP47". Journal of Bone and Mineral Metabolism. 18 (6): 328–34. doi:10.1007/s007740070004. PMID 11052465. S2CID 35696096.
Pelletier G, Stefanovsky VY, Faubladier M, Hirschler-Laszkiewicz I, Savard J, Rothblum LI, Côté J, Moss T (November 2000). "Competitive recruitment of CBP and Rb-HDAC regulates UBF acetylation and ribosomal transcription". Molecular Cell. 6 (5): 1059–66. doi:10.1016/S1097-2765(00)00104-0. PMID 11106745.
Matsuda M, Koide T, Yorihuzi T, Hosokawa N, Nagata K (January 2001). "Molecular cloning of a novel ubiquitin-like protein, UBIN, that binds to ER targeting signal sequences". Biochemical and Biophysical Research Communications. 280 (2): 535–40. doi:10.1006/bbrc.2000.4149. PMID 11162551.
Zhou M, Nekhai S, Bharucha DC, Kumar A, Ge H, Price DH, Egly JM, Brady JN (November 2001). "TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcription". The Journal of Biological Chemistry. 276 (48): 44633–40. doi:10.1074/jbc.M107466200. PMID 11572868.
Song CZ, Keller K, Murata K, Asano H, Stamatoyannopoulos G (March 2002). "Functional interaction between coactivators CBP/p300, PCAF, and transcription factor FKLF2". The Journal of Biological Chemistry. 277 (9): 7029–36. doi:10.1074/jbc.M108826200. PMC 2808425. PMID 11748222.
Sasaki H, Sato T, Yamauchi N, Okamoto T, Kobayashi D, Iyama S, Kato J, Matsunaga T, Takimoto R, Takayama T, Kogawa K, Watanabe N, Niitsu Y (May 2002). "Induction of heat shock protein 47 synthesis by TGF-beta and IL-1 beta via enhancement of the heat shock element binding activity of heat shock transcription factor 1". Journal of Immunology. 168 (10): 5178–83. doi:10.4049/jimmunol.168.10.5178. PMID 11994473.
Razzaque MS, Ahmed AR (March 2002). "Collagens, collagen-binding heat shock protein 47 and transforming growth factor-beta 1 are induced in cicatricial pemphigoid: possible role(s) in dermal fibrosis". Cytokine. 17 (6): 311–6. doi:10.1006/cyto.2002.1020. PMID 12061838.
Sato K, Yomogida K, Wada T, Yorihuzi T, Nishimune Y, Hosokawa N, Nagata K (October 2002). "Type XXVI collagen, a new member of the collagen family, is specifically expressed in the testis and ovary". The Journal of Biological Chemistry. 277 (40): 37678–84. doi:10.1074/jbc.M205347200. PMID 12145293.
Rocnik EF, van der Veer E, Cao H, Hegele RA, Pickering JG (October 2002). "Functional linkage between the endoplasmic reticulum protein Hsp47 and procollagen expression in human vascular smooth muscle cells". The Journal of Biological Chemistry. 277 (41): 38571–8. doi:10.1074/jbc.M206689200. PMID 12163502.

External links[]

The MEROPS online database for peptidases and their inhibitors: I04.035
HSP47+Heat-Shock+Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by .

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000149257 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000070436 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)".

[pmid11592970-6] Dafforn TR, Della M, Miller AD (December 2001). "The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis". The Journal of Biological Chemistry. 276 (52): 49310–9. doi:10.1074/jbc.M108896200. PMID 11592970.

[7] Williams, R. Sanders (21 March 2000). "Heat Shock Protein 47: A Chaperone for the Fibrous Cap?". Circulation. 101 (11): 1227–1228. doi:10.1161/01.CIR.101.11.1227. PMID 10725278. Retrieved 11 December 2017.

[8] Mala JG, Rose C (November 2010). "Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?". Life Sciences. 87 (19–22): 579–86. doi:10.1016/j.lfs.2010.09.024. PMID 20888348.

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v t Serpins
inhibitory	Alpha 1-antichymotrypsin Alpha 1-antitrypsin Alpha 2-antiplasmin Antithrombin C1-inhibitor Heparin cofactor II Protein C inhibitor Plasminogen activator inhibitor-1 Plasminogen activator inhibitor-2 Protein Z-related protease inhibitor SERPINA1 SERPINA2 SERPINA3 SERPINA4 SERPINA5 SERPINA9 SERPINA14 SERPINB1 SERPINB2 SERPINB3 SERPINB4 SERPINB5 SERPINB6 SERPINB7 SERPINB8 SERPINB9 SERPINB10 SERPINB13 SERPINC1 SERPIND1 SERPINE1 SERPINE2 SERPINE2 SERPINF1 SERPING1 SERPINH1 SERPINI1 SERPINI2
Cross class inhibitory	MENT SCCA-1 CrmA
noninhibitory	Heat shock protein 47 Maspin Ovalbumin Transcortin Thyroxine-binding globulin Angiotensinogen PEDF
see also disorders of globin and globulin proteins