YMEL1_RAT
ID YMEL1_RAT Reviewed; 715 AA.
AC Q925S8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATP-dependent zinc metalloprotease YME1L1;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q96TA2};
DE AltName: Full=ATP-dependent metalloprotease FtsH1;
DE AltName: Full=Meg-4 {ECO:0000303|Ref.1};
DE AltName: Full=YME1-like protein 1;
GN Name=Yme1l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miyata T., Inagi R., Yasuda Y., Kurokawa K.;
RT "Partial cDNA sequence of rat meg-4, ATP-dependent metalloprotease (FtsH)
RT homolog.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation
CC of folded and unfolded proteins with a suitable degron sequence in the
CC mitochondrial intermembrane region (By similarity). Plays an important
CC role in regulating mitochondrial morphology and function by cleaving
CC OPA1 at position S2, giving rise to a form of OPA1 that promotes
CC maintenance of normal mitochondrial structure (By similarity). Ensures
CC cell proliferation, maintains normal cristae morphology and complex I
CC respiration activity, promotes antiapoptotic activity and protects
CC mitochondria from the accumulation of oxidatively damaged membrane
CC proteins (By similarity). Required for normal, constitutive degradation
CC of PRELID1 (By similarity). Catalyzes the degradation of OMA1 in
CC response to membrane depolarization. Required to control the
CC accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4
CC and ND1) (By similarity). {ECO:0000250|UniProtKB:O88967,
CC ECO:0000250|UniProtKB:Q96TA2}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q96TA2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q96TA2};
CC -!- SUBUNIT: Homohexamer; may also form heterohexamers. Exists in several
CC complexes of 600-1100 kDa. Interacts with AFG1L.
CC {ECO:0000250|UniProtKB:Q96TA2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q96TA2}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q96TA2}.
CC -!- PTM: Proteolytically processed by mitochondrial processing peptidase
CC (MPP) to generate the mature form. {ECO:0000250|UniProtKB:Q96TA2}.
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; AF151784; AAK57557.1; -; mRNA.
DR AlphaFoldDB; Q925S8; -.
DR SMR; Q925S8; -.
DR IntAct; Q925S8; 1.
DR MINT; Q925S8; -.
DR STRING; 10116.ENSRNOP00000023395; -.
DR MEROPS; M41.026; -.
DR jPOST; Q925S8; -.
DR PaxDb; Q925S8; -.
DR PRIDE; Q925S8; -.
DR UCSC; RGD:620764; rat.
DR RGD; 620764; Yme1l1.
DR eggNOG; KOG0734; Eukaryota.
DR InParanoid; Q925S8; -.
DR PhylomeDB; Q925S8; -.
DR Reactome; R-RNO-8949664; Processing of SMDT1.
DR PRO; PR:Q925S8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; ISO:RGD.
DR GO; GO:0034982; P:mitochondrial protein processing; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0034214; P:protein hexamerization; ISO:RGD.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; 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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..715
FT /note="ATP-dependent zinc metalloprotease YME1L1"
FT /id="PRO_0000084669"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 31..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 542
FT /evidence="ECO:0000250|UniProtKB:P0AAI3"
FT BINDING 321..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AAI3"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AAI3"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 715 AA; 79867 MW; 900A98F4EB95AB92 CRC64;
MFSLSSTVQP QVTVPLSHLI NAFHSPKNIS VSVNTSASPK QHRDTVAEHE APSSEPVLNL
RDLGLSELKI GQIDKLVENL LPGFYKDKRV SSCWHTSHIS AQSFFENKYG HLDMFSTLRS
SSLYRQHPKT LQSICSDLQN FPVFIQSRGF KTLKSRTRRL QSTSERLAEA QNIAPSFVKG
FLLRDRGTDL ESLDKLMKTK NIPEAHQDAF KTGFAEGFLK AQALTQKTND SLRRTRLILF
VLLLFGIYGL LKNPFLSVRF RTTTGLDSAV DPVQMKNVTF EHVKGVEEAK QELQEVVEFL
KNPQKFTVLG GKLPKGILLV GPPGTGKTLL ARAVAGEADV PFYYASGSEF DEMFVGVGAS
RIRNLFREAK ANAPCVIFID ELDSVGGKRI EFPMHPYSRQ TIIQLLAEMD GFKPNEGVII
IGATNFPEAL DNALIRPGRF DMQVTVPRPD VKGRTEILKW YLNKIKFDKS VDPEIIARGT
VGFSGAELEN LVNQAALKAA VDGKEMVTMK ELEFSKDKIL MGPERRSVEI DNKNKTITAY
HESGHAIIAY YTKDAMPINK ATIMPRGPTL GHVSLLPEND RWNEIRAQLL AQMDVSMGGR
VAEELIFGTD HITTGASSDF DNATKIAKRM VTKFGMSEKL GVMTYSDTGK LSPETQSAIE
QEIRILLRES YERAKHILKT HAKEHKNLAE ALLTYETLDA KEIQIVLEGK KLEVR
