AFG31_MOUSE
ID AFG31_MOUSE Reviewed; 789 AA.
AC Q920A7; Q3THK2; Q6PGJ7; Q9CZN2;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=AFG3-like protein 1;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Afg3l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ, C57BL/6J, and DBA/2J;
RC TISSUE=Embryo, Erythroleukemia, and Thymic lymphoma;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-789 (ISOFORM 1).
RX PubMed=11549317; DOI=10.1006/geno.2001.6560;
RA Kremmidiotis G., Gardner A.E., Settasatian C., Savoia A., Sutherland G.R.,
RA Callen D.F.;
RT "Molecular and functional analyses of the human and mouse genes encoding
RT AFG3L1, a mitochondrial metalloprotease homologous to the human spastic
RT paraplegia protein.";
RL Genomics 76:58-65(2001).
RN [4]
RP PROTEIN SEQUENCE OF 71-80, FUNCTION, PROTEOLYTIC PROCESSING, SUBUNIT,
RP INTERACTION WITH SPG7 AND AFG3L2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-567.
RX PubMed=19656850; DOI=10.1091/mbc.e09-03-0218;
RA Koppen M., Bonn F., Ehses S., Langer T.;
RT "Autocatalytic processing of m-AAA protease subunits in mitochondria.";
RL Mol. Biol. Cell 20:4216-4224(2009).
RN [5]
RP SUBUNIT.
RX PubMed=17101804; DOI=10.1128/mcb.01470-06;
RA Koppen M., Metodiev M.D., Casari G., Rugarli E.I., Langer T.;
RT "Variable and tissue-specific subunit composition of mitochondrial m-AAA
RT protease complexes linked to hereditary spastic paraplegia.";
RL Mol. Cell. Biol. 27:758-767(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Putative ATP-dependent protease. Required for the maturation
CC of paraplegin (SPG7) after its cleavage by mitochondrial-processing
CC peptidase (MPP), converting it into a proteolytically active mature
CC form. {ECO:0000269|PubMed:19656850}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Homooligomer (PubMed:17101804). Forms heterooligomers with
CC SPG7 and AFG3L2 (PubMed:17101804, PubMed:19656850). Interacts with SPG7
CC and AFG3L2 (PubMed:19656850). {ECO:0000269|PubMed:17101804,
CC ECO:0000269|PubMed:19656850}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:19656850}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q920A7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q920A7-2; Sequence=VSP_031809, VSP_031810;
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
CC -!- CAUTION: The orthologous human gene is a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK66971.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB28211.3; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK012394; BAB28211.3; ALT_FRAME; mRNA.
DR EMBL; AK159647; BAE35259.1; -; mRNA.
DR EMBL; AK167964; BAE39961.1; -; mRNA.
DR EMBL; AK168244; BAE40194.1; -; mRNA.
DR EMBL; BC056978; AAH56978.1; -; mRNA.
DR EMBL; AF329695; AAK66971.1; ALT_INIT; mRNA.
DR CCDS; CCDS22760.1; -. [Q920A7-1]
DR RefSeq; NP_473411.2; NM_054070.3. [Q920A7-1]
DR RefSeq; XP_011246578.1; XM_011248276.2.
DR AlphaFoldDB; Q920A7; -.
DR SMR; Q920A7; -.
DR BioGRID; 227903; 1.
DR IntAct; Q920A7; 1.
DR STRING; 10090.ENSMUSP00000001520; -.
DR MEROPS; M41.016; -.
DR iPTMnet; Q920A7; -.
DR PhosphoSitePlus; Q920A7; -.
DR EPD; Q920A7; -.
DR jPOST; Q920A7; -.
DR MaxQB; Q920A7; -.
DR PaxDb; Q920A7; -.
DR PeptideAtlas; Q920A7; -.
DR PRIDE; Q920A7; -.
DR ProteomicsDB; 296123; -. [Q920A7-1]
DR ProteomicsDB; 296124; -. [Q920A7-2]
DR DNASU; 114896; -.
DR Ensembl; ENSMUST00000001520; ENSMUSP00000001520; ENSMUSG00000031967. [Q920A7-1]
DR Ensembl; ENSMUST00000098320; ENSMUSP00000095924; ENSMUSG00000031967. [Q920A7-2]
DR GeneID; 114896; -.
DR KEGG; mmu:114896; -.
DR UCSC; uc009nwd.2; mouse. [Q920A7-1]
DR CTD; 114896; -.
DR MGI; MGI:1928277; Afg3l1.
DR VEuPathDB; HostDB:ENSMUSG00000031967; -.
DR eggNOG; KOG0731; Eukaryota.
DR GeneTree; ENSGT00940000160625; -.
DR HOGENOM; CLU_000688_23_1_1; -.
DR InParanoid; Q920A7; -.
DR OMA; YDKQGGG; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q920A7; -.
DR TreeFam; TF105004; -.
DR BRENDA; 3.4.24.B18; 3474.
DR BioGRID-ORCS; 114896; 8 hits in 72 CRISPR screens.
DR PRO; PR:Q920A7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q920A7; protein.
DR Bgee; ENSMUSG00000031967; Expressed in yolk sac and 227 other tissues.
DR Genevisible; Q920A7; MM.
DR GO; GO:0005745; C:m-AAA complex; IDA:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042407; P:cristae formation; IGI:MGI.
DR GO; GO:0008053; P:mitochondrial fusion; IGI:MGI.
DR GO; GO:0034982; P:mitochondrial protein processing; IDA:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IGI:MGI.
DR GO; GO:0016485; P:protein processing; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IBA:GO_Central.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Direct protein sequencing; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..70
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19656850"
FT CHAIN 71..789
FT /note="AFG3-like protein 1"
FT /id="PRO_0000084672"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 81..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 567
FT /evidence="ECO:0000250"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 641
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 548..584
FT /note="LEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLL -> VHHTSRQGAWL
FT RPVPSPRAVPLHTRAALRPHVYDAGG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031809"
FT VAR_SEQ 585..789
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031810"
FT MUTAGEN 567
FT /note="E->Q: Absence of proteolytic activity. Loss of its
FT processing into the mature form."
FT /evidence="ECO:0000269|PubMed:19656850"
SQ SEQUENCE 789 AA; 87047 MW; 06B23E0176285346 CRC64;
MLLRLVGAAG SRALAWPFSK LWRCGGCAGS GGTVWSSVRA CGIALQGHLG RCSQQLALQG
KLTSFSPRLY SKPPRGFEKF FKNKKNRKSA SPGNSVPPKK EPKNAGPGGD GGNRGGKGDD
FPWWKRMQKG EFPWDDKDFR SLAVLGAGVA AGFLYFYFRD PGKEITWKHF VQYYLARGLV
DRLEVVNKQF VRVIPVPGTT SERFVWFNIG SVDTFERNLE SAQWELGIEP TNQAAVVYTT
ESDGSFLRSL VPTLVLVSIL LYAMRRGPMG TGRGGRGGGL FSVGETTAKI LKNNIDVRFA
DVAGCEEAKL EIMEFVNFLK NPKQYQDLGA KIPKGAMLTG PPGTGKTLLA KATAGEANVP
FITVNGSEFL EMFVGVGPAR VRDMFAMARK HAPCILFIDE IDAIGRKRGR GHLGGQSEQE
NTLNQMLVEM DGFNSSTNVV VLAGTNRPDI LDPALTRPGR FDRQIYIGPP DIKGRSSIFK
VHLRPLKLDG SLSKDALSRK LAALTPGFTG ADISNVCNEA ALIAARHLSP SVQERHFEQA
IERVIGGLEK KTQVLQPSEK TTVAYHEAGH AVVGWFLEHA DPLLKVSIIP RGKGLGYAQY
LPREQFLYTR EQLFDRMCMM LGGRVAEQLF FGQITTGAQD DLRKVTQSAY AQIVQFGMSE
KLGQVSFDFP RQGETMVEKP YSEATAQLID EEVRCLVRSA YNRTLELLTQ CREQVEKVGR
RLLEKEVLEK ADMIELLGPR PFAEKSTYEE FVEGTGSLEE DTSLPEGLKD WNKGREEGGT
ERGLQESPV
