SCG5

Last updated

SCG5
Identifiers
Aliases SCG5 , 7B2, P7B2, SGNE1, SgV, secretogranin V
External IDs OMIM: 173120; MGI: 98289; HomoloGene: 37722; GeneCards: SCG5; OMA:SCG5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001144757
NM_003020
NM_001394278
NM_001394279

NM_009162

RefSeq (protein)

NP_001138229
NP_003011

NP_033188

Location (UCSC) Chr 15: 32.64 – 32.7 Mb Chr 2: 113.78 – 113.83 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Neuroendocrine protein 7B2 is a protein that in humans is encoded by the SCG5 gene. [5] [6] [7] The protein expressed by this gene is widely distributed in neuroendocrine tissues. It functions as a chaperone protein for the proprotein convertase PC2 by blocking the aggregation of this protein, and is required for the production of an active PC2 enzyme. [8] [9] It is an intrinsically disordered protein that may also function as a chaperone for other aggregating secretory proteins in addition to proPC2 (Helwig et al. 2013). 7B2 has been identified in vertebrates and in invertebrates as low as flatworms (Protein ID: AIZ72728.1) and insects. [10] It is also called Sgne1 and Secretogranin V. In C. elegans, it was originally called e7B2 [11] and then renamed Seven B Two (gene name sbt-1). [12] There is a Pfam entry for this protein: Secretogranin_V (PF05281).

Related Research Articles

<span class="mw-page-title-main">Proopiomelanocortin</span> Mammalian protein found in Homo sapiens

Pro-opiomelanocortin (POMC) is a precursor polypeptide with 241 amino acid residues. POMC is synthesized in corticotrophs of the anterior pituitary from the 267-amino-acid-long polypeptide precursor pre-pro-opiomelanocortin (pre-POMC), by the removal of a 26-amino-acid-long signal peptide sequence during translation. POMC is part of the central melanocortin system.

<span class="mw-page-title-main">Tryptase</span> Class of enzymes

Tryptase is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast cell activation. Club cells contain tryptase, which is believed to be responsible for cleaving the hemagglutinin surface protein of influenza A virus, thereby activating it and causing the symptoms of flu.

<span class="mw-page-title-main">Proprotein convertase 1</span>

Proprotein convertase 1, also known as prohormone convertase, prohormone convertase 3, or neuroendocrine convertase 1 and often abbreviated as PC1/3 is an enzyme that in humans is encoded by the PCSK1 gene. PCSK1 and PCSK2 differentially cleave proopiomelanocortin and they act together to process proinsulin and proglucagon in pancreatic islets.

<span class="mw-page-title-main">Furin</span> Enzyme found in humans

Furin is a protease, a proteolytic enzyme activated by substrate presentation that in humans and other animals is encoded by the FURIN gene. Some proteins are inactive when they are first synthesized, and must have sections removed in order to become active. Furin cleaves these sections and activates the proteins. It was named furin because it was in the upstream region of an oncogene known as FES. The gene was known as FUR and therefore the protein was named furin. Furin is also known as PACE. A member of family S8, furin is a subtilisin-like peptidase.

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<span class="mw-page-title-main">Proprotein convertase 2</span> Protein-coding gene in the species Homo sapiens

Proprotein convertase 2 (PC2) also known as prohormone convertase 2 or neuroendocrine convertase 2 (NEC2) is a serine protease and proprotein convertase PC2, like proprotein convertase 1 (PC1), is an enzyme responsible for the first step in the maturation of many neuroendocrine peptides from their precursors, such as the conversion of proinsulin to insulin intermediates. To generate the bioactive form of insulin, a second step involving the removal of C-terminal basic residues is required; this step is mediated by carboxypeptidases E and/or D. PC2 plays only a minor role in the first step of insulin biosynthesis, but a greater role in the first step of glucagon biosynthesis compared to PC1. PC2 binds to the neuroendocrine protein named 7B2, and if this protein is not present, proPC2 cannot become enzymatically active. 7B2 accomplishes this by preventing the aggregation of proPC2 to inactivatable forms. The C-terminal domain of 7B2 also inhibits PC2 activity until it is cleaved into smaller inactive forms that lack carboxy-terminal basic residues. Thus, 7B2 is both an activator and an inhibitor of PC2. PC2 has been identified in a number of animals, including C. elegans.

<span class="mw-page-title-main">Chromogranin-A</span> Mammalian protein found in Homo sapiens

Chromogranin-A (CgA) or parathyroid secretory protein 1 is encoded in the human by the gene CHGA. Cga is a member of the granin family of neuroendocrine secretory proteins. As such, it is located in secretory vesicles of neurons and endocrine cells such as islet beta cell secretory granules in the pancreas.

<span class="mw-page-title-main">Carboxypeptidase E</span> Enzyme found in humans

Carboxypeptidase E (CPE), also known as carboxypeptidase H (CPH) and enkephalin convertase, is an enzyme that in humans is encoded by the CPE gene. This enzyme catalyzes the release of C-terminal arginine or lysine residues from polypeptides.

<span class="mw-page-title-main">Sterol regulatory element-binding protein 2</span> Protein-coding gene in the species Homo sapiens

Sterol regulatory element-binding protein 2 (SREBP-2) also known as sterol regulatory element binding transcription factor 2 (SREBF2) is a protein that in humans is encoded by the SREBF2 gene.

<span class="mw-page-title-main">SCG2</span>

SCG2, also called secretogranin II (chromogranin C), is a protein which in humans is encoded by the SCG2 gene.

Kexin is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast. It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors. The human homolog is PCSK4. It is a family of subtilisin-like peptidases. Even though there are a few prokaryote kexin-like peptidases, all kexins are eukaryotes. The enzyme is encoded by the yeast gene KEX2, and usually referred to in the scientific community as Kex2p. It shares structural similarities with the bacterial protease subtilisin. The first mammalian homologue of this protein to be identified was furin. In the mammal, kexin-like peptidases function in creating and regulating many differing proproteins.

<span class="mw-page-title-main">MSMB</span> Animal protein produced in the prostate

Beta-microseminoprotein is a protein that in humans is encoded by the MSMB gene. For historical reasons, the scientific literature may also refer to this protein as Prostate secretory protein 94 (PSP94), microseminoprotein (MSP), microseminoprotein-beta (MSMB), beta-inhibitin, prostatic inhibin peptide (PIP), and inhibitin like material (ILM).

<span class="mw-page-title-main">PCSK5</span> Protein-coding gene in the species Homo sapiens

Proprotein convertase subtilisin/kexin type 5 is an enzyme that in humans is encoded by the PCSK5 gene, found in chromosome 9q21.3 Two alternatively spliced transcripts are described for this gene but only one has its full length nature known.

<span class="mw-page-title-main">PCSK7</span> Protein-coding gene in the species Homo sapiens

Proprotein convertase subtilisin/kexin type 7 is an enzyme that in humans is encoded by the PCSK7 gene.

<span class="mw-page-title-main">PCSK6</span> Protein-coding gene in the species Homo sapiens

Proprotein convertase subtilisin/kexin type 6 is an protease that in humans is encoded by the PCSK6 gene which is located in chromosome 15. Pcsk6 is a calcium-dependent serine endoprotease that catalyzes the post-translational modification of precursor proteins from its ‘latent’ form to the cleaved ‘active’ form. Active Pcsk6 has been reported to process substrates such as transforming growth factor β, pro-albumin, von Willebrand factor, and corin. Clinically, Pcsk6 is suggested to play a role in left/right asymmetry, structural asymmetry of the brain, handedness, tumor progression, hemostasis, and cardiovascular diseases.

<span class="mw-page-title-main">NRD1</span> Protein-coding gene in the species Homo sapiens

Nardilysin is a protein that in humans is encoded by the NRD1 gene.

<span class="mw-page-title-main">DNAJC5</span> Protein-coding gene in the species Homo sapiens

DnaJ homolog subfamily C member 5, also known as cysteine string protein or CSP is a protein, that in humans encoded by the DNAJC5 gene. It was first described in 1990.

<span class="mw-page-title-main">SCG3</span> Protein-coding gene in the species Homo sapiens

Secretogranin III, also known as SCG3, is a protein which in humans is encoded by the SCG3 gene.

<span class="mw-page-title-main">PCSK4</span> Protein-coding gene in the species Homo sapiens

Proprotein convertase subtilisin/kexin type 4 is an enzyme that in humans is encoded by the PCSK4 gene.

<span class="mw-page-title-main">Proprotein convertase subtilisin/kexin type 1 inhibitor</span> Mammalian protein found in Homo sapiens

Proprotein convertase subtilisin/kexin type 1 inhibitor is a protein by the name of proSAAS that in humans is encoded by the PCSK1N gene.

References

  1. 1 2 3 ENSG00000166922, ENSG00000281931 GRCh38: Ensembl release 89: ENSG00000277614, ENSG00000166922, ENSG00000281931 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023236 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. Lloyd RV, Jin L (March 1994). "Analysis of chromogranin/secretogranin messenger RNAs in human pituitary adenomas". Diagnostic Molecular Pathology. 3 (1): 38–45. doi:10.1097/00019606-199403010-00007. PMID   8162254.
  6. Taupenot L, Harper KL, O'Connor DT (March 2003). "The chromogranin-secretogranin family". The New England Journal of Medicine. 348 (12): 1134–49. doi:10.1056/NEJMra021405. PMID   12646671.
  7. Martens GJ (July 1988). "Cloning and sequence analysis of human pituitary cDNA encoding the novel polypeptide 7B2". FEBS Letters. 234 (1): 160–4. doi: 10.1016/0014-5793(88)81324-3 . PMID   3134253.
  8. "Entrez Gene: SCG5 secretogranin V (7B2 protein)".
  9. Mbikay M, Seidah NG, Chrétien M (July 2001). "Neuroendocrine secretory protein 7B2: structure, expression and functions". The Biochemical Journal. 357 (Pt 2): 329–42. doi:10.1042/0264-6021:3570329. PMC   1221959 . PMID   11439082.
  10. Hwang JR, Siekhaus DE, Fuller RS, Taghert PH, Lindberg I (June 2000). "Interaction of Drosophila melanogaster prohormone convertase 2 and 7B2. Insect cell-specific processing and secretion". The Journal of Biological Chemistry. 275 (23): 17886–93. doi: 10.1074/jbc.M000032200 . PMID   10749852.
  11. Lindberg I, Tu B, Muller L, Dicksinson I (August 1998). "Cloning and functional analysis of C. elegans 7B2". DNA and Cell Biology. 17 (8): 727–734. doi:10.1089/dna.1998.17.727. PMID   9726255.
  12. Sieburth, et al. (July 2005). "Systematic analysis of genes required for synapse structure and function". Nature. 436 (7050): 510–517. Bibcode:2005Natur.436..510S. doi:10.1038/nature03809. PMID   16049479. S2CID   4427397.

Further reading