AFG3-like protein 2
Details
- Name
- AFG3-like protein 2
- Synonyms
- 3.4.24.-
- Paraplegin-like protein
- Gene Name
- AFG3L2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0009960|AFG3-like protein 2 MAHRCLRLWGRGGCWPRGLQQLLVPGGVGPGEQPCLRTLYRFVTTQARASRNSLLTDIIA AYQRFCSRPPKGFEKYFPNGKNGKKASEPKEVMGEKKESKPAATTRSSGGGGGGGGKRGG KKDDSHWWSRFQKGDIPWDDKDFRMFFLWTALFWGGVMFYLLLKRSGREITWKDFVNNYL SKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENR VPVVYIAESDGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRTGRGMGGLFSVGETTAKVLK DEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKA TAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGN FGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDI KGRASIFKVHLRPLKLDSTLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDSI NQKHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRG KGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQ IVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARLIDDEVRILINDAYKRTVALLTEKK ADVEKVALLLLEKEVLDKNDMVELLGPRPFAEKSTYEEFVEGTGSLDEDTSLPEGLKDWN KEREKEKEEPPGEKVAN
- Number of residues
- 797
- Molecular Weight
- 88583.03
- Theoretical pI
- 9.09
- GO Classification
- FunctionsATP binding / ATP-dependent peptidase activity / metalloendopeptidase activity / metallopeptidase activity / unfolded protein binding / zinc ion bindingProcessesaxonogenesis / cristae formation / mitochondrial fusion / mitochondrial protein processing / muscle fiber development / myelination / nerve development / neuromuscular junction development / protein complex assembly / protein import into mitochondrial intermembrane space / regulation of multicellular organism growth / righting reflexComponentsintegral component of membrane / mitochondrial inner membrane / mitochondrion
- General Function
- Zinc ion binding
- Specific Function
- ATP-dependent protease which is essential for axonal development.
- Pfam Domain Function
- Transmembrane Regions
- 143-163 251-271
- Cellular Location
- Mitochondrion membrane
- Gene sequence
>lcl|BSEQ0009961|AFG3-like protein 2 (AFG3L2) ATGGCGCACCGCTGTTTGCGGCTGTGGGGCCGGGGCGGCTGCTGGCCCCGCGGCCTACAG CAGCTCCTCGTGCCTGGCGGCGTGGGCCCGGGCGAGCAGCCCTGCCTCCGGACGCTTTAC CGATTTGTTACAACTCAAGCAAGGGCCAGCAGAAATTCTCTTTTGACAGATATAATTGCT GCTTATCAAAGATTCTGTTCTCGACCCCCAAAAGGATTTGAAAAATACTTTCCTAATGGA AAAAATGGAAAAAAAGCTAGTGAACCTAAAGAAGTTATGGGAGAGAAAAAAGAATCAAAG CCAGCTGCTACCACACGCTCTTCTGGAGGAGGAGGTGGTGGCGGTGGAAAACGAGGTGGC AAGAAAGATGATTCTCACTGGTGGTCCAGGTTTCAGAAGGGTGACATTCCATGGGACGAC AAGGATTTCAGGATGTTCTTCCTCTGGACTGCTCTGTTCTGGGGTGGAGTCATGTTTTAC TTGCTGCTCAAGAGATCCGGGAGAGAAATCACTTGGAAGGACTTTGTCAATAACTATCTT TCAAAAGGAGTAGTAGACAGATTGGAAGTCGTCAACAAGCGTTTTGTTCGAGTGACCTTT ACACCAGGAAAAACTCCTGTTGATGGGCAATACGTTTGGTTTAATATTGGCAGTGTGGAC ACCTTTGAACGGAATCTGGAAACTTTACAGCAGGAATTGGGCATAGAAGGAGAAAATCGG GTGCCTGTTGTCTACATTGCTGAAAGTGATGGCTCTTTTCTGCTGAGCATGCTGCCTACG GTGCTCATCATCGCCTTCTTGCTCTACACCATCAGAAGAGGGCCTGCTGGCATTGGCCGG ACAGGCCGAGGGATGGGCGGACTCTTCAGTGTCGGAGAAACCACTGCCAAGGTCTTAAAG GATGAAATTGATGTGAAGTTCAAAGATGTGGCTGGCTGTGAGGAGGCCAAGCTAGAGATC ATGGAATTTGTGAATTTCTTGAAAAACCCAAAGCAGTATCAAGACCTAGGAGCAAAAATC CCAAAGGGTGCCATTCTCACTGGTCCTCCAGGCACTGGGAAGACGCTGCTAGCTAAGGCC ACAGCCGGAGAAGCCAATGTCCCCTTCATCACCGTTAGTGGATCTGAGTTTTTGGAGATG TTCGTTGGTGTGGGCCCTGCTAGAGTCCGAGACTTATTTGCCCTTGCTCGGAAGAATGCC CCTTGCATCCTCTTCATCGATGAAATCGATGCGGTGGGAAGGAAGAGAGGAAGAGGCAAC TTTGGAGGGCAGAGTGAGCAGGAGAACACACTCAACCAGCTGCTGGTGGAGATGGATGGT TTTAATACAACAACAAATGTCGTCATTTTGGCCGGCACCAATCGACCAGATATCCTGGAC CCCGCGCTGCTTAGGCCGGGGCGTTTCGACAGGCAGATCTTTATTGGACCACCAGACATA AAAGGAAGAGCTTCTATTTTCAAAGTTCATCTCCGACCGCTAAAACTGGACAGTACCCTG GAGAAGGATAAATTGGCAAGAAAACTGGCATCTTTAACTCCAGGGTTTTCAGGTGCTGAT GTTGCTAATGTCTGTAATGAAGCTGCGTTGATTGCTGCAAGGCATCTGTCAGATTCCATA AATCAGAAACACTTTGAACAGGCAATTGAACGAGTGATTGGTGGCTTAGAGAAGAAAACG CAGGTTCTGCAGCCTGAGGAGAAGAAGACTGTGGCATACCACGAAGCAGGCCATGCGGTT GCCGGCTGGTATCTGGAGCACGCAGACCCGCTTTTAAAGGTATCCATCATCCCACGTGGC AAAGGACTAGGTTATGCTCAGTATTTACCAAAAGAACAATACCTCTATACCAAAGAGCAG CTCTTGGATAGGATGTGTATGACTTTAGGTGGTCGAGTCTCTGAAGAAATCTTCTTTGGA AGAATTACAACTGGTGCTCAAGATGACTTGAGAAAAGTAACTCAGAGTGCATATGCCCAA ATTGTTCAGTTTGGCATGAATGAAAAGGTTGGGCAAATCTCCTTTGACCTCCCACGTCAG GGGGACATGGTATTGGAGAAACCTTACAGTGAAGCCACTGCAAGATTGATAGATGATGAA GTACGAATACTTATTAATGATGCTTATAAAAGAACAGTAGCTCTTCTCACAGAAAAGAAA GCTGACGTGGAGAAGGTTGCTCTTCTGTTGTTAGAAAAAGAAGTATTAGATAAGAATGAT ATGGTTGAACTTTTGGGCCCCAGACCATTTGCGGAAAAATCTACCTATGAAGAATTTGTG GAAGGCACTGGCAGCTTGGATGAGGACACCTCACTTCCAGAAGGCCTTAAGGACTGGAAC AAGGAGCGGGAAAAGGAGAAAGAGGAGCCCCCGGGTGAGAAAGTTGCCAACTAG
- Chromosome Location
- 18
- Locus
- 18p11
- External Identifiers
Resource Link UniProtKB ID Q9Y4W6 UniProtKB Entry Name AFG32_HUMAN GenBank Protein ID 5457357 GenBank Gene ID Y18314 GenAtlas ID AFG3L2 HGNC ID HGNC:315 - General References
- Banfi S, Bassi MT, Andolfi G, Marchitiello A, Zanotta S, Ballabio A, Casari G, Franco B: Identification and characterization of AFG3L2, a novel paraplegin-related gene. Genomics. 1999 Jul 1;59(1):51-8. [Article]
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- Atorino L, Silvestri L, Koppen M, Cassina L, Ballabio A, Marconi R, Langer T, Casari G: Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J Cell Biol. 2003 Nov 24;163(4):777-87. Epub 2003 Nov 17. [Article]
- Koppen M, Metodiev MD, Casari G, Rugarli EI, Langer T: Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia. Mol Cell Biol. 2007 Jan;27(2):758-67. Epub 2006 Nov 13. [Article]
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- Cagnoli C, Stevanin G, Brussino A, Barberis M, Mancini C, Margolis RL, Holmes SE, Nobili M, Forlani S, Padovan S, Pappi P, Zaros C, Leber I, Ribai P, Pugliese L, Assalto C, Brice A, Migone N, Durr A, Brusco A: Missense mutations in the AFG3L2 proteolytic domain account for approximately 1.5% of European autosomal dominant cerebellar ataxias. Hum Mutat. 2010 Oct;31(10):1117-24. doi: 10.1002/humu.21342. [Article]
- 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: Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28. Nat Genet. 2010 Apr;42(4):313-21. doi: 10.1038/ng.544. Epub 2010 Mar 7. [Article]
- 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: Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases. PLoS Genet. 2011 Oct;7(10):e1002325. doi: 10.1371/journal.pgen.1002325. Epub 2011 Oct 13. [Article]