AFG32_BOVIN
ID AFG32_BOVIN Reviewed; 805 AA.
AC Q2KJI7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=AFG3-like protein 2;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9Y4W6};
DE Flags: Precursor;
GN Name=AFG3L2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent protease which is essential for axonal and
CC neuron development. In neurons, mediates degradation of SMDT1/EMRE
CC before its assembly with the uniporter complex, limiting the
CC availability of SMDT1/EMRE for MCU assembly and promoting efficient
CC assembly of gatekeeper subunits with MCU. 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. Required for the maturation of PINK1 into its 52kDa mature form
CC after its cleavage by mitochondrial-processing peptidase (MPP) (By
CC similarity). Involved in the regulation of OMA1-dependent processing of
CC OPA1 (By similarity). {ECO:0000250|UniProtKB:Q8JZQ2,
CC ECO:0000250|UniProtKB:Q9Y4W6}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9WZ49};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9WZ49};
CC -!- SUBUNIT: Homooligomer. Forms heterooligomers with SPG7 and AFG3L1.
CC Interacts with SPG7; the interaction is required for the efficient
CC assembly of mitochondrial complex I. Interacts with AFG3L1. Interacts
CC with MAIP1. Interacts with DNAJC19 and PHB2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8JZQ2, ECO:0000250|UniProtKB:Q9Y4W6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9Y4W6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Upon import into the mitochondrion, the N-terminal transit peptide
CC is cleaved to generate an intermediate form which undergoes
CC autocatalytic proteolytic processing to generate the proteolytically
CC active mature form. {ECO:0000250|UniProtKB:Q8JZQ2}.
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}.
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DR EMBL; BC105322; AAI05323.1; -; mRNA.
DR RefSeq; NP_001039676.1; NM_001046211.1.
DR AlphaFoldDB; Q2KJI7; -.
DR BMRB; Q2KJI7; -.
DR SMR; Q2KJI7; -.
DR STRING; 9913.ENSBTAP00000030993; -.
DR MEROPS; M41.016; -.
DR PaxDb; Q2KJI7; -.
DR PRIDE; Q2KJI7; -.
DR Ensembl; ENSBTAT00000031029; ENSBTAP00000030993; ENSBTAG00000011250.
DR GeneID; 515757; -.
DR KEGG; bta:515757; -.
DR CTD; 10939; -.
DR VEuPathDB; HostDB:ENSBTAG00000011250; -.
DR VGNC; VGNC:25714; AFG3L2.
DR eggNOG; KOG0731; Eukaryota.
DR GeneTree; ENSGT00940000159566; -.
DR HOGENOM; CLU_000688_23_1_1; -.
DR InParanoid; Q2KJI7; -.
DR OMA; DEAYKQC; -.
DR OrthoDB; 217929at2759; -.
DR TreeFam; TF105004; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000011250; Expressed in infraspinatus muscle and 102 other tissues.
DR ExpressionAtlas; Q2KJI7; baseline.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0008237; F:metallopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0036444; P:calcium import into the mitochondrion; ISS:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IEA:Ensembl.
DR GO; GO:0033619; P:membrane protein proteolysis; IEA:Ensembl.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IEA:Ensembl.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0021675; P:nerve development; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
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 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ2"
FT PROPEP 40..67
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ2"
FT /id="PRO_0000442309"
FT CHAIN 68..805
FT /note="AFG3-like protein 2"
FT /id="PRO_0000442310"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 74..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 576
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 349..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT MOD_RES 118
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ2"
SQ SEQUENCE 805 AA; 89388 MW; 850FF0D0D111F1BF CRC64;
MAHRCLLLWG RGACRPRGMP PMLLPGGRTG STERLYLRML YRYATTQAKT SRNSLLTDVI
AAYQRLCSRP PKGFEKYFPN GKNGKKTSEP KEVMGEKKEP KPAAAPRPSG GGVGGGGKRG
GKKDDSHWWS RFQKGDIPWD DKEFKMYFLW TALFWGGFLF YFLFKSSGRE ITWKDFANNY
LSKGVVDRLE VVNKRFVRVT FTPGKTPVDG QYVWFNIGSV DTFERNLETL QQELGIEGEN
RVPVVYIAES DGSFLLSMLP TVLIIAFLLY TIRRGPAGIG RTGRGMGGLF SVGETTAKVL
KDEIDVKFKD VAGCEEAKLE IMEFVNFLKN PKQYQDLGAK IPKGAILTGP PGTGKTLLAK
ATAGEANVPF ITVSGSEFLE MFVGVGPARV RDLFALARKN APCILFIDEI DAVGRKRGRG
NFGGQSEQEN TLNQLLVEMD GFNTTTNVVI LAGTNRPDIL DPALMRPGRF DRQIFIGPPD
IKGRASIFKV HLRPLKLDST LEKEKLARKL ASLTPGFSGA DVANVCNEAA LIAARHLSDS
INQKHFEQAI ERVIGGLEKK TQVLQPEEKK TVAYHEAGHA VAGWYLEHAD PLLKVSIIPR
GKGLGYAQYL PREQYLYTRE QLLDRMCMTL GGRVSEEIFF GRITTGAQDD LRKVTQSAYA
QIVQFGMNEK VGQISFDLPR QGDMVLEKPY SEATARLIDD EVRILINDAY KRTVALLTEK
KADVEKVALL LLEKEVLDKN DMVELLGPRP FAEKSTYEEF VEGTGSLDED TSLPEGLKDW
NREREGSEEP SGEKVTSPVQ GAGPA
