SGTA

Small glutamine-rich tetratricopeptide repeat-containing protein alpha is a protein that in humans is encoded by the SGTA gene. ^{[1] [2] [3]} SGTA orthologs ^[4] have also been identified in several mammals for which complete genome data are available. STGA belongs to a family of co-chaperone proteins that obtain a TPR motif. ^[5] STGA was discovered just 15 years ago.

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SGTA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VYI, 4CPG, 4GOD, 4GOE, 4GOF
Identifiers
Aliases	SGTA , SGT, alphaSGT, hSGT, small glutamine rich tetratricopeptide repeat containing alpha, small glutamine rich tetratricopeptide repeat co-chaperone alpha, SGT1, Vpu
External IDs	OMIM: 603419; MGI: 1098703; HomoloGene: 31122; GeneCards: SGTA; OMA:SGTA - orthologs
Gene location (Human) Chr. Chromosome 19 (human) [6] Band 19p13.3 Start 2,754,715 bp [6] End 2,783,362 bp [6]
Gene location (Mouse) Chr. Chromosome 10 (mouse) [7] Band 10 C1|10 39.72 cM Start 80,879,909 bp [7] End 80,896,015 bp [7]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart C1 segment muscle of thigh gastrocnemius muscle right frontal lobe middle frontal gyrus right auricle of heart paraflocculus of cerebellum cingulate gyrus anterior pituitary Top expressed in perirhinal cortex entorhinal cortex ventricular zone primary visual cortex yolk sac muscle of thigh lip superior frontal gyrus lactiferous gland neural tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding BAT3 complex binding protein self-association identical protein binding molecular adaptor activity Cellular component cytosol membrane nucleus cytoplasm presynapse extrinsic component of synaptic vesicle membrane TRC complex Biological process positive regulation of ER-associated ubiquitin-dependent protein catabolic process viral process ubiquitin-dependent ERAD pathway negative regulation of ER-associated ubiquitin-dependent protein catabolic process negative regulation of ubiquitin-dependent protein catabolic process tail-anchored membrane protein insertion into ER membrane chaperone-mediated protein folding posttranslational protein targeting to endoplasmic reticulum membrane positive regulation of chaperone-mediated protein folding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6449 52551 Ensembl ENSG00000104969 ENSMUSG00000004937 UniProt O43765 Q8BJU0 RefSeq (mRNA) NM_003021 NM_024499 NM_001358549 NM_001358550 RefSeq (protein) NP_003012 NP_078775 NP_001345478 NP_001345479 Location (UCSC) Chr 19: 2.75 – 2.78 Mb Chr 10: 80.88 – 80.9 Mb PubMed search [8] [9]
Wikidata
View/Edit Human View/Edit Mouse

Function

The molecular function of the protein states that SGTA is a small glutamine-rich tetratricopeptide repeat (TRP)-containing protein, ubiquitously expressed, interacting with the NS1 protein of parvovirus H-1. ^[10]

The SGTA gene encodes a protein that is capable of interacting with the major nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate protein; however, its function is not known. Since this transcript is expressed ubiquitously in various tissues, this protein may serve a housekeeping function. ^[3]

Overview of main functions: ^[5]

• hormone signaling
• viral assembly and release
• cell cycle and apoptosis
• intracellular compartmentalization
• neuronal synaptic transmission
• post-translational transport and modification of proteins.

Small glutamine-rich tetratricopeptide repeat-containing protein alpha (STGA) acts as a co-chaperone and regulator of androgen and growth hormone receptor signaling. ^[5] The protein also mediates targets to the endoplasmic reticulum

Interactions

SGTA has been shown to interact with Growth hormone receptor. ^[2]

Interacting Proteins for the SGTA Gene: ^[10]

• HSPA4
• BAG6
• UBL4A
• HSPA8
• GET4

Associated Diseases

Source: ^[5]

• Prostate, ovary, liver, and esophagus cancer
• Hormone-related polycystic ovary syndrome
• Amyloid-related Alzheimer's
• Prion Diseases

References

1. Kordes E, Savelyeva L, Schwab M, Rommelaere J, Jauniaux JC, Cziepluch C (August 1998). "Isolation and characterization of human SGT and identification of homologues in Saccharomyces cerevisiae and Caenorhabditis elegans". Genomics. 52 (1): 90–94. doi:10.1006/geno.1998.5385. PMID   9740675.
2. Schantl JA, Roza M, De Jong AP, Strous GJ (August 2003). "Small glutamine-rich tetratricopeptide repeat-containing protein (SGT) interacts with the ubiquitin-dependent endocytosis (UbE) motif of the growth hormone receptor". The Biochemical Journal. 373 (Pt 3): 855–863. doi:10.1042/BJ20021591. PMC   1223544 . PMID   12735788.
3. "Entrez Gene: SGTA small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha".
4. "OrthoMaM phylogenetic marker: SGTA coding sequence". Archived from the original on 2016-03-03. Retrieved 2010-02-17.
5. Philp LK, Day TK, Butler MS, Laven-Law G, Jindal S, Hickey TE, et al. (June 2016). "Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha (SGTA) Ablation Limits Offspring Viability and Growth in Mice". Scientific Reports. 6 (1): 28950. doi: 10.1038/srep28950 . PMC   4928056 . PMID   27358191.
6. GRCh38: Ensembl release 89: ENSG00000104969 – Ensembl, May 2017
7. GRCm38: Ensembl release 89: ENSMUSG00000004937 – Ensembl, May 2017
8. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
9. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
10. "STGA". GeneCards The Human Gene Database. Retrieved 2023-11-28.

Further reading

• Roberts JD, Thapaliya A, Martínez-Lumbreras S, Krysztofinska EM, Isaacson RL (Dec 2015). "Structural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein Alpha". Frontiers in Molecular Biosciences. 2: 71. doi: 10.3389/fmolb.2015.00071 . PMC   4683186 . PMID   26734616.
• Heavner GA, Audhya T, Goldstein G (February 1990). "Peptide analogs of thymopentin distinguish distinct thymopoietin receptor specificities on two human T cell lines". Regulatory Peptides. 27 (2): 257–262. doi:10.1016/0167-0115(90)90044-W. PMID   2158125. S2CID   12562672.Geraghty RJ, Talbot KJ, Callahan M, Harper W, Panganiban AT (1994). "Cell type-dependence for Vpu function". Journal of Medical Primatology. 23 (2–3): 146–150. doi:10.1111/j.1600-0684.1994.tb00115.x. PMID   7966229. S2CID   20674152.
• Cziepluch C, Kordes E, Poirey R, Grewenig A, Rommelaere J, Jauniaux JC (May 1998). "Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1". Journal of Virology. 72 (5): 4149–4156. doi:10.1128/JVI.72.5.4149-4156.1998. PMC   109644 . PMID   9557704.
• Callahan MA, Handley MA, Lee YH, Talbot KJ, Harper JW, Panganiban AT (June 1998). "Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family". Journal of Virology. 72 (6): 5189–5197. doi:10.1128/JVI.72.6.5189-5197.1998. PMC   110095 . PMID   9573291.
• Callahan MA, Handley MA, Lee YH, Talbot KJ, Harper JW, Panganiban AT (October 1998). "Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family". Journal of Virology. 72 (10): 8461. doi:10.1128/JVI.72.10.8460c-8460c.1998. PMC   110251 . PMID   9766974.
• Liu FH, Wu SJ, Hu SM, Hsiao CD, Wang C (November 1999). "Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats". The Journal of Biological Chemistry. 274 (48): 34425–34432. doi: 10.1074/jbc.274.48.34425 . PMID   10567422.
• Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–1795. doi:10.1101/gr.143000. PMC   310948 . PMID   11076863.
• Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, et al. (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–435. doi:10.1101/gr.GR1547R. PMC   311072 . PMID   11230166.
• Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (September 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports. 1 (3): 287–292. doi:10.1093/embo-reports/kvd058. PMC   1083732 . PMID   11256614.
• Handley MA, Paddock S, Dall A, Panganiban AT (December 2001). "Association of Vpu-binding protein with microtubules and Vpu-dependent redistribution of HIV-1 Gag protein". Virology. 291 (2): 198–207. doi: 10.1006/viro.2001.1166 . PMID   11878889.
• Angeletti PC, Walker D, Panganiban AT (July 2002). "Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity". Cell Stress & Chaperones. 7 (3): 258–268. PMC   514826 . PMID   12482202.
• Pai MT, Yang CS, Tzeng SR, Wang C, Cheng JW (August 2003). "1H, 15N and 13C resonance assignments of the tetratricopeptide repeat (TPR) domain of hSGT". Journal of Biomolecular NMR. 26 (4): 381–382. doi:10.1023/A:1024029117511. PMID   12815268. S2CID   19544209.
• Wang H, Zhang Q, Zhu D (November 2003). "hSGT interacts with the N-terminal region of myostatin". Biochemical and Biophysical Research Communications. 311 (4): 877–883. doi:10.1016/j.bbrc.2003.10.080. PMID   14623262.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–167. doi:10.1016/S0888-7543(03)00235-0. PMID   14667819.
• Winnefeld M, Rommelaere J, Cziepluch C (February 2004). "The human small glutamine-rich TPR-containing protein is required for progress through cell division". Experimental Cell Research. 293 (1): 43–57. doi:10.1016/j.yexcr.2003.09.028. PMID   14729056.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi: 10.1073/pnas.0404720101 . PMC   514446 . PMID   15302935.