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NameAFG3-like protein 2
Synonyms
  • 3.4.24.-
  • Paraplegin-like protein
Gene NameAFG3L2
OrganismHuman
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 residues797
Molecular Weight88583.03
Theoretical pI9.09
GO Classification
Functions
  • ATP binding
  • metallopeptidase activity
  • metalloendopeptidase activity
  • unfolded protein binding
  • ATP-dependent peptidase activity
  • zinc ion binding
Processes
  • protein import into mitochondrial intermembrane space
  • regulation of multicellular organism growth
  • righting reflex
  • protein complex assembly
  • axonogenesis
  • cristae formation
  • mitochondrial fusion
  • mitochondrial protein processing
  • muscle fiber development
  • myelination
  • nerve development
  • neuromuscular junction development
Components
  • mitochondrial inner membrane
  • integral component of membrane
  • mitochondrion
General FunctionZinc ion binding
Specific FunctionATP-dependent protease which is essential for axonal development.
Pfam Domain Function
Transmembrane Regions143-163 251-271
GenBank Protein ID5457357
UniProtKB IDQ9Y4W6
UniProtKB Entry NameAFG32_HUMAN
Cellular LocationMitochondrion 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
GenBank Gene IDY18314
GeneCard IDNot Available
GenAtlas IDAFG3L2
HGNC IDHGNC:315
Chromosome Location18
Locus18p11
References
  1. 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. 10395799
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  3. 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. 14623864
  4. 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. 17101804
  5. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  6. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  7. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. 25944712
  8. Edener U, Wollner J, Hehr U, Kohl Z, Schilling S, Kreuz F, Bauer P, Bernard V, Gillessen-Kaesbach G, Zuhlke C: Early onset and slow progression of SCA28, a rare dominant ataxia in a large four-generation family with a novel AFG3L2 mutation. Eur J Hum Genet. 2010 Aug;18(8):965-8. doi: 10.1038/ejhg.2010.40. Epub 2010 Mar 31. 20354562
  9. 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. 20725928
  10. 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. 20208537
  11. 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. 22022284