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PSMF1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VT8, 4OUH
Identifiers
Aliases	PSMF1, PI31, proteasome inhibitor subunit 1
External IDs	OMIM: 617858; MGI: 1346072; HomoloGene: 38231; GeneCards: PSMF1; OMA:PSMF1 - orthologs
Gene location (Human) Chr. Chromosome 20 (human) Band 20p13 Start 1,113,240 bp End 1,189,415 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 G3 Start 151,557,732 bp End 151,586,106 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm left testis right testis muscle of thigh blood gastrocnemius muscle popliteal artery tibial arteries monocyte islet of Langerhans Top expressed in seminiferous tubule spermatid secondary oocyte zygote primary oocyte blood sciatic nerve interventricular septum fetal liver hematopoietic progenitor cell spermatocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function proteasome binding protein binding endopeptidase inhibitor activity protein homodimerization activity protein heterodimerization activity Cellular component cytoplasm cytosol membrane nucleoplasm endoplasmic reticulum proteasome complex proteasome core complex perinuclear region of cytoplasm Biological process regulation of cellular amino acid metabolic process antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent ubiquitin-dependent protein catabolic process regulation of mRNA stability positive regulation of canonical Wnt signaling pathway protein polyubiquitination stimulatory C-type lectin receptor signaling pathway tumor necrosis factor-mediated signaling pathway MAPK cascade Fc-epsilon receptor signaling pathway NIK/NF-kappaB signaling negative regulation of proteasomal protein catabolic process anaphase-promoting complex-dependent catabolic process T cell receptor signaling pathway negative regulation of canonical Wnt signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process Wnt signaling pathway, planar cell polarity pathway negative regulation of endopeptidase activity negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination SCF-dependent proteasomal ubiquitin-dependent protein catabolic process transmembrane transport regulation of transcription from RNA polymerase II promoter in response to hypoxia post-translational protein modification regulation of hematopoietic stem cell differentiation interleukin-1-mediated signaling pathway regulation of mitotic cell cycle phase transition Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9491 228769 Ensembl ENSG00000125818 ENSMUSG00000032869 UniProt Q92530 Q5QPM9 Q8BHL8 RefSeq (mRNA) NM_006814 NM_178578 NM_178579 NM_001323407 NM_001323408 NM_001323409 NM_001323410 NM_144889 NM_212446 NM_001305244 RefSeq (protein) NP_001310336 NP_001310337 NP_001310338 NP_001310339 NP_006805 NP_848693 NP_001292173 NP_997611 Location (UCSC) Chr 20: 1.11 – 1.19 Mb Chr 2: 151.56 – 151.59 Mb PubMed search
Wikidata
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Proteasome inhibitor PI31 subunit is a protein that in humans is encoded by the PSMF1 gene.

Function

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMF1 encodes a protein termed PI31 that binds to both 20S and 26S proteasomes. PI31 was originally identified by its ability to inhibit the hydrolysis of small synthetic peptides in a cell free assay, but it stimulates 26S proteasome activity both in vitro and in vivo. PI31 can promote the assembly of 26S proteasomes from 19S and 20S sub-particles, and it also serves as an adapter to couple proteasomes with motor proteins to mediate fast axonal transport in neurons. Inactivation of PMSF1 in yeast, plants, fruit flies and mice attenuates protein degradation and stimulates accumulation of ubiquitinated protein aggregates. Furthermore, loss of PSMF1 function in mice causes progressive neuronal dysfunction, synaptic degeneration and eventually neuronal cell death. Alternative transcript variants have been identified for this gene.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000125818 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000032869 – 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.
5. Tanahashi N, Kawahara H, Murakami Y, Tanaka K (Apr 1999). "The proteasome-dependent proteolytic system". Molecular Biology Reports. 26 (1–2): 3–9. doi:10.1023/A:1006909522731. PMID 10363639. S2CID 38305744.
6. ^ "Entrez Gene: PSMF1 proteasome (prosome, macropain) inhibitor subunit 1 (PI31)".
7. Chu-Ping, M (1992). "Purification and characterization of a protein inhibitor of the 20S proteasome (macropain)". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1119 (3): 303–11. doi:10.1016/0167-4838(92)90218-3. PMID 1312359.
8. Bader, Maya (2011). "A conserved F box regulatory complex controls proteasome activity in Drosophila". Cell. 145 (3): 371–382. doi:10.1016/j.cell.2011.03.021. PMC 3108249. PMID 21529711.
9. Liu, Kai (2019). "PI31 Is an Adaptor Protein for Proteasome Transport in Axons and Required for Synaptic Development". Dev Cell. 50 (4): 509–524. doi:10.1016/j.devcel.2019.06.009. PMC 6702053. PMID 31327739.
10. Minis, Adi (2019). "The proteasome regulator PI31 is required for protein homeostasis, synapse maintenance, and neuronal survival in mice". Proc Natl Acad Sci U S A. 116 (49): 24639–24650. Bibcode:2019PNAS..11624639M. doi:10.1073/pnas.1911921116. PMC 6900516. PMID 31754024.

Further reading

• Cho-Park PF (Apr 2013). "Proteasome regulation by ADP-ribosylation". Cell. 153 (3): 614–27. doi:10.1016/j.cell.2013.03.040. PMC 3676968. PMID 23622245.
• Yang BJ (Apr 2016). "Arabidopsis PROTEASOME REGULATOR1 is required for auxin-mediated suppression of proteasome activity and regulates auxin signalling". Nat Commun. 7 (3): 11388. Bibcode:2016NatCo...711388Y. doi:10.1038/ncomms11388. PMC 4848511. PMID 27109828.
• Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281–3. doi:10.1016/S0092-8674(03)00602-0. PMID 12914693. S2CID 16340355.
• Minghetti L, Visentin S, Patrizio M, Franchini L, Ajmone-Cat MA, Levi G (May 2004). "Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions". Neurochemical Research. 29 (5): 965–78. doi:10.1023/B:NERE.0000021241.90133.89. PMID 15139295. S2CID 25323034.
• Liou LY, Herrmann CH, Rice AP (Sep 2004). "HIV-1 infection and regulation of Tat function in macrophages". The International Journal of Biochemistry & Cell Biology. 36 (9): 1767–75. doi:10.1016/j.biocel.2004.02.018. PMID 15183343.
• Bannwarth S, Gatignol A (Jan 2005). "HIV-1 TAR RNA: the target of molecular interactions between the virus and its host". Current HIV Research. 3 (1): 61–71. doi:10.2174/1570162052772924. PMID 15638724.
• Gibellini D, Vitone F, Schiavone P, Re MC (Apr 2005). "HIV-1 tat protein and cell proliferation and survival: a brief review". The New Microbiologica. 28 (2): 95–109. PMID 16035254.
• Hetzer C, Dormeyer W, Schnölzer M, Ott M (Oct 2005). "Decoding Tat: the biology of HIV Tat posttranslational modifications". Microbes and Infection / Institut Pasteur. 7 (13): 1364–9. doi:10.1016/j.micinf.2005.06.003. PMID 16046164.
• Peruzzi F (2006). "The multiple functions of HIV-1 Tat: proliferation versus apoptosis". Frontiers in Bioscience. 11: 708–17. doi:10.2741/1829. PMID 16146763.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Seeger M, Ferrell K, Frank R, Dubiel W (Mar 1997). "HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation". The Journal of Biological Chemistry. 272 (13): 8145–8. doi:10.1074/jbc.272.13.8145. PMID 9079628.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Madani N, Kabat D (Dec 1998). "An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein". Journal of Virology. 72 (12): 10251–5. doi:10.1128/JVI.72.12.10251-10255.1998. PMC 110608. PMID 9811770.
• Simon JH, Gaddis NC, Fouchier RA, Malim MH (Dec 1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype". Nature Medicine. 4 (12): 1397–400. doi:10.1038/3987. PMID 9846577. S2CID 25235070.
• McCutchen-Maloney SL, Matsuda K, Shimbara N, Binns DD, Tanaka K, Slaughter CA, DeMartino GN (Jun 2000). "cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome". The Journal of Biological Chemistry. 275 (24): 18557–65. doi:10.1074/jbc.M001697200. PMID 10764772.
• Mulder LC, Muesing MA (Sep 2000). "Degradation of HIV-1 integrase by the N-end rule pathway". The Journal of Biological Chemistry. 275 (38): 29749–53. doi:10.1074/jbc.M004670200. PMID 10893419.
• Sheehy AM, Gaddis NC, Choi JD, Malim MH (Aug 2002). "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein". Nature. 418 (6898): 646–50. Bibcode:2002Natur.418..646S. doi:10.1038/nature00939. PMID 12167863. S2CID 4403228.
• Zaiss DM, Standera S, Kloetzel PM, Sijts AJ (Oct 2002). "PI31 is a modulator of proteasome formation and antigen processing". Proceedings of the National Academy of Sciences of the United States of America. 99 (22): 14344–9. Bibcode:2002PNAS...9914344Z. doi:10.1073/pnas.212257299. PMC 137886. PMID 12374861.
• Huang X, Seifert U, Salzmann U, Henklein P, Preissner R, Henke W, Sijts AJ, Kloetzel PM, Dubiel W (Nov 2002). "The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing". Journal of Molecular Biology. 323 (4): 771–82. doi:10.1016/S0022-2836(02)00998-1. PMID 12419264.

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