AFG3L2

Protein-coding gene in the species Homo sapiens

AFG3L2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2LNA

Identifiers
AliasesAFG3L2, SCA28, SPAX5, AFG3 like matrix AAA peptidase subunit 2, OPA12
External IDsOMIM: 604581; MGI: 1916847; HomoloGene: 4947; GeneCards: AFG3L2; OMA:AFG3L2 - orthologs
Gene location (Human)
Chromosome 18 (human)
Chr.Chromosome 18 (human)[1]
Chromosome 18 (human)
Genomic location for AFG3L2
Genomic location for AFG3L2
Band18p11.21Start12,328,944 bp[1]
End12,377,227 bp[1]
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)[2]
Chromosome 18 (mouse)
Genomic location for AFG3L2
Genomic location for AFG3L2
Band18|18 E1Start67,537,834 bp[2]
End67,582,242 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Brodmann area 23

  • endothelial cell

  • jejunal mucosa

  • parietal pleura

  • Skeletal muscle tissue of biceps brachii

  • renal medulla

  • gingival epithelium

  • right ventricle

  • germinal epithelium

  • tibia
Top expressed in
  • interventricular septum

  • muscle of thigh

  • right kidney

  • zygote

  • proximal tubule

  • myocardium of ventricle

  • secondary oocyte

  • gastrula

  • otic vesicle

  • skeletal muscle tissue
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • nucleotide binding
  • unfolded protein binding
  • zinc ion binding
  • metal ion binding
  • peptidase activity
  • protein binding
  • metalloendopeptidase activity
  • hydrolase activity
  • ATP binding
  • metallopeptidase activity
Cellular component
  • integral component of membrane
  • membrane
  • mitochondrion
  • m-AAA complex
  • mitochondrial inner membrane
Biological process
  • regulation of multicellular organism growth
  • mitochondrion organization
  • neuromuscular junction development
  • myelination
  • righting reflex
  • proteolysis
  • axonogenesis
  • calcium import into the mitochondrion
  • mitochondrial calcium ion homeostasis
  • mitochondrial fusion
  • nerve development
  • mitochondrial protein processing
  • cristae formation
  • mitochondrial calcium ion transmembrane transport
  • protein processing
  • protein autoprocessing
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10939

69597

Ensembl

ENSG00000141385

ENSMUSG00000024527

UniProt

Q9Y4W6

Q8JZQ2

RefSeq (mRNA)

NM_006796

NM_027130

RefSeq (protein)

NP_006787

NP_081406

Location (UCSC)Chr 18: 12.33 – 12.38 MbChr 18: 67.54 – 67.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

AFG3 ATPase family gene 3-like 2 (S. cerevisiae) is a protein that in humans is encoded by the AFG3L2 gene.[5]

This gene encodes a protein localized in mitochondria and closely related to paraplegin. The paraplegin gene is responsible for an autosomal recessive form of hereditary spastic paraplegia. This gene is a candidate gene for other hereditary spastic paraplegias or neurodegenerative disorders [5] as well as spastic ataxia-neuropathy syndrome.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141385 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024527 – 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. ^ a b "Entrez Gene: AFG3 ATPase family gene 3-like 2 (S. cerevisiae)". Retrieved 2011-12-30.
  6. ^ Pierson TM, Adams D, Bonn F, Martinelli P, Cherukuri PF, Teer JK, Hansen NF, Cruz P, Mullikin For The Nisc Comparative Sequencing Program JC, Blakesley RW, Golas G, Kwan J, Sandler A, Fuentes Fajardo K, Markello T, Tifft C, Blackstone C, Rugarli EI, Langer T, Gahl WA, Toro C (October 2011). "Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases". PLoS Genet. 7 (10): e1002325. doi:10.1371/journal.pgen.1002325. PMC 3192828. PMID 22022284.

Further reading

  • Banfi S, Bassi MT, Andolfi G, Marchitiello A, Zanotta S, Ballabio A, Casari G, Franco B (1999). "Identification and Characterization of AFG3L2, a Novel Paraplegin-Related Gene". Genomics. 59 (1): 51–58. doi:10.1006/geno.1999.5818. PMID 10395799.
  • Cagnoli C, Mariotti C, Taroni F, Seri M, Brussino A, Michielotto C, Grisoli M, Di Bella D, Migone N, Gellera C, Di Donato S, Brusco A (2005). "SCA28, a novel form of autosomal dominant cerebellar ataxia on chromosome 18p11.22-q11.2". Brain. 129 (Pt 1): 235–242. doi:10.1093/brain/awh651. PMID 16251216.
  • Mariotti C, Brusco A, Bella D, Cagnoli C, Seri M, Gellera C, Donato S, Taroni F (2008). "Spinocerebellar ataxia type 28: A novel autosomal dominant cerebellar ataxia characterized by slow progression and ophthalmoparesis". The Cerebellum. 7 (2): 184–188. doi:10.1007/s12311-008-0053-9. PMID 18769991. S2CID 8173189.
  • Augustin S, Gerdes F, Lee S, Tsai FT, Langer T, Tatsuta T (2009). "An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases". Molecular Cell. 35 (5): 574–585. doi:10.1016/j.molcel.2009.07.018. PMC 2744646. PMID 19748354.
  • Di Bella D, Lazzaro F, Brusco A, Plumari M, Battaglia G, Pastore A, Finardi A, Cagnoli C, Tempia F, Frontali M, Veneziano L, Sacco T, Boda E, Brussino A, Bonn F, Castellotti B, Baratta S, Mariotti C, Gellera C, Fracasso V, Magri S, Langer T, Plevani P, Di Donato S, Muzi-Falconi M, Taroni F (2010). "Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28". Nature Genetics. 42 (4): 313–321. doi:10.1038/ng.544. PMID 20208537. S2CID 1703983.
  • Edener U, Wöllner J, Hehr U, Kohl Z, Schilling S, Kreuz F, Bauer P, Bernard V, Gillessen-Kaesbach G, Zühlke C (2010). "Early onset and slow progression of SCA28, a rare dominant ataxia in a large four-generation family with a novel AFG3L2 mutation". European Journal of Human Genetics. 18 (8): 965–968. doi:10.1038/ejhg.2010.40. PMC 2987378. PMID 20354562.
  • Cagnoli C, Stevanin G, Brussino A, Barberis M, Mancini C, Margolis RL, Holmes SE, Nobili M, Forlani S, Padovan S, Pappi P, Zaros CC, Leber I, Ribai P, Pugliese L, Assalto C, Brice A, Migone N, Dürr A, Brusco A (2010). "Missense mutations in the AFG3L2 proteolytic domain account for ~1.5% of European autosomal dominant cerebellar ataxias". Human Mutation. 31 (10): 1117–1124. doi:10.1002/humu.21342. PMID 20725928. S2CID 38251230.


  • v
  • t
  • e