Q8JZQ2 (AFG32_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AFG3-like protein 2
EC=3.4.24.-

Gene names

Name:

Afg3l2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP-dependent protease which is essential for axonal development. Ref.4
Cofactor	Binds 1 zinc ion per subunit Potential.
Subunit structure	Homooligomer. Interacts with SPG7; the interaction is required for the efficient assembly of mitochondrial complex I By similarity.
Subcellular location	Mitochondrion membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Highly expressed in the cerebellar Purkinje cells. Ref.5
Involvement in disease	Defects in Afg3l2 are the cause of the paralyze (par) phenotype, a spontaneous mutant strain. Par mice have a normal appearance and fertility but are significantly smaller than their littermates at 1 week of age and display a rapidly progressive loss of motor function in all limbs by 12-14 days. As the disease progresses, they lose the ability to support their own weight or turn themselves over when placed on their back and exhibit a typical posture with over extension of all limbs and uncoordinated movements. They rarely survive beyond 16 days of age, when they are completely paralyzed.
Sequence similarities	In the N-terminal section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis Inferred from mutant phenotype PubMed 2917690. Source: MGI cristae formation Inferred from genetic interaction PubMed 20038678. Source: MGI death Inferred from mutant phenotype PubMed 2917690. Source: MGI mitochondrial fusion Inferred from genetic interaction PubMed 20038678. Source: MGI mitochondrial protein processing Inferred from genetic interaction PubMed 20038678. Source: MGI myelination Inferred from mutant phenotype PubMed 2917690. Source: MGI nerve development Inferred from mutant phenotype PubMed 2917690. Source: MGI neuromuscular junction development Inferred from mutant phenotype PubMed 2917690. Source: MGI protein catabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of multicellular organism growth Inferred from mutant phenotype PubMed 2917690. Source: MGI righting reflex Inferred from mutant phenotype PubMed 2917690. Source: MGI
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 802	802	AFG3-like protein 2		PRO_0000084674
Regions
	Transmembrane	142 – 162	21	Helical; Potential
	Transmembrane	250 – 270	21	Helical; Potential
	Nucleotide binding	347 – 354	8	ATP Potential
Sites
	Active site	574	1	By similarity
	Metal binding	573	1	Zinc; catalytic By similarity
	Metal binding	577	1	Zinc; catalytic By similarity
	Metal binding	648	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	307	1	N6-acetyllysine Ref.3
	Modified residue	542	1	N6-acetyllysine Ref.3
Natural variations
	Natural variant	389	1	R → G in par. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8JZQ2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E7300BD686532D2D	FASTA	802	89,519
	10 20 30 40 50 60 MAHRCLLLWS RGGCRRGLPP LLVPRGCLGP DRRPCLRTLY QYATVQTASS RRSLLRDVIA 70 80 90 100 110 120 AYQRFCSRPP KGFEKYFPNG KNGKKASEPK EAVGEKKEPQ PSGPQPSGGA GGGGGKRRGK 130 140 150 160 170 180 KEDSHWWSRF QKGDFPWDDK DFRMYFLWTA LFWGGVMIYF VFKSSGREIT WKDFVNNYLS 190 200 210 220 230 240 KGVVDRLEVV NKRFVRVTFT PGKTPVDGQY VWFNIGSVDT FERNLETLQQ ELGIEGENRV 250 260 270 280 290 300 PVVYIAESDG SFLLSMLPTV LIIAFLLYTI RRGPAGIGRT GRGMGGLFSV GETTAKVLKD 310 320 330 340 350 360 EIDVKFKDVA GCEEAKLEIM EFVNFLKNPK QYQDLGAKIP KGAILTGPPG TGKTLLAKAT 370 380 390 400 410 420 AGEANVPFIT VSGSEFLEMF VGVGPARVRD LFALARKNAP CILFIDEIDA VGRKRGRGNF 430 440 450 460 470 480 GGQSEQENTL NQLLVEMDGF NTTTNVVILA GTNRPDILDP ALLRPGRFDR QIFIGPPDIK 490 500 510 520 530 540 GRASIFKVHL RPLKLDSALE KDKLARKLAS LTPGFSGADV ANVCNEAALI AARHLSDAIN 550 560 570 580 590 600 EKHFEQAIER VIGGLEKKTQ VLQPEEKKTV AYHEAGHAVA GWYLEHADPL LKVSIIPRGK 610 620 630 640 650 660 GLGYAQYLPK EQYLYTKEQL LDRMCMTLGG RVSEEIFFGR ITTGAQDDLR KVTQSAYAQI 670 680 690 700 710 720 VQFGMNEKVG QISFDLPRQG DMVLEKPYSE ATARMIDDEV RILISDAYRR TVALLTEKKA 730 740 750 760 770 780 DVEKVALLLL EKEVLDKNDM VQLLGPRPFT EKSTYEEFVE GTGSLDEDTS LPEGLQDWNK 790 800 EREKEEKKEK EKEEPLNEKV VS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Kidney.
[2]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 173-181; 283-296 AND 632-650, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[3]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-307 AND LYS-542, MASS SPECTROMETRY. Tissue: Liver.
[4]	"The mitochondrial protease AFG3L2 is essential for axonal development." Maltecca F., Aghaie A., Schroeder D.G., Cassina L., Taylor B.A., Phillips S.J., Malaguti M., Previtali S., Guenet J.L., Quattrini A., Cox G.A., Casari G. J. Neurosci. 28:2827-2836(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANT PAR GLY-389.
[5]	"Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28." 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. Nat. Genet. 42:313-321(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC036999 mRNA. Translation: AAH36999.1. BC043056 mRNA. Translation: AAH43056.1.
IPI	IPI00170357.
RefSeq	NP_081406.1. NM_027130.1.
UniGene	Mm.426052.
3D structure databases
ProteinModelPortal	Q8JZQ2.
SMR	Q8JZQ2. Positions 163-250, 295-749.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8JZQ2. 1 interaction.
MINT	MINT-4116623.
STRING	10090.ENSMUSP00000025408.
Protein family/group databases
MEROPS	M41.007.
PTM databases
PhosphoSite	Q8JZQ2.
Proteomic databases
PaxDb	Q8JZQ2.
PRIDE	Q8JZQ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025408; ENSMUSP00000025408; ENSMUSG00000024527.
GeneID	69597.
KEGG	mmu:69597.
UCSC	uc008fmf.1. mouse.
Organism-specific databases
CTD	10939.
MGI	MGI:1916847. Afg3l2.
Phylogenomic databases
eggNOG	COG0465.
GeneTree	ENSGT00530000063070.
HOGENOM	HOG000217277.
HOVERGEN	HBG050184.
InParanoid	Q8JZQ2.
KO	K08956.
OMA	LYRFVTT.
OrthoDB	EOG4SBDXC.
Gene expression databases
ArrayExpress	Q8JZQ2.
Bgee	Q8JZQ2.
CleanEx	MM_AFG3L2.
Genevestigator	Q8JZQ2.
GermOnline	ENSMUSG00000024527. Mus musculus.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR005936. FtsH. IPR027417. P-loop_NTPase. IPR011546. Pept_M41_FtsH_extracell. IPR000642. Peptidase_M41. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF06480. FtsH_ext. 1 hit. PF01434. Peptidase_M41. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR01241. FtsH_fam. 1 hit.
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	329880.
SOURCE	Search...

Entry information

Entry name

AFG32_MOUSE

Accession

Primary (citable) accession number: Q8JZQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program