| Tag | Content |
|---|
| CPLM ID | CPLM-001434 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP-dependent zinc metalloprotease YME1L1 |
Protein Synonyms/Alias | ATP-dependent metalloprotease FtsH1; YME1-like protein 1 |
Gene Name | Yme1l1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 69 | DLGLSELKIGQIDKM | ubiquitination | [1] | | 179 | NIAPSFVKGFLLRDR | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Putative ATP-dependent protease which plays a role in mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity, and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Requires to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1). Seems to act in the processing of OPA1 (By similarity). |
Sequence Annotation | NP_BIND 321 328 ATP (Potential).
ACT_SITE 542 542 By similarity.
METAL 541 541 Zinc; catalytic (By similarity).
METAL 545 545 Zinc; catalytic (By similarity).
METAL 619 619 Zinc; catalytic (By similarity). |
Keyword | ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 715 AA |
Protein Sequence | MFSLSSTVQP QVTIPLSHLI NAFHSPKNIS VSVNTPVSQK QHRDTVPEHE APSSEPVLNL 60
RDLGLSELKI GQIDKMVENL LPGFYKDKRV SSCWHTSHIS AQSFFENKYG HLDMFSTLRS 120
SSLYRQHPKT LRSICSDLQY FPVFIQSRGF KTLKSRTRRL QSTSERLVEA QNIAPSFVKG 180
FLLRDRGTDL ESLDKLMKTK NIPEAHQDAF KTGFAEGFLK AQALTQKTND SLRRTRLILF 240
VLLLFGIYGL LKNPFLSVRF RTTTGLDSAV DPVQMKNVTF EHVKGVEEAK QELQEVVEFL 300
KNPQKFTVLG GKLPKGILLV GPPGTGKTLL ARAVAGEADV PFYYASGSEF DEMFVGVGAS 360
RIRNLFREAK ANAPCVIFID ELDSVGGKRI ESPMHPYSRQ TINQLLAEMD GFKPNEGVII 420
IGATNFPEAL DNALIRPGRF DMQVTVPRPD VKGRTEILKW YLNKIKFDKS VDPEIIARGT 480
VGFSGAELEN LVNQAALKAA VDGKEMVTMK ELEFSKDKIL MGPERRSVEI DNKNKTITAY 540
HESGHAIIAY YTKDAMPINK ATIMPRGPTL GHVSLLPEND RWNETRAQLL AQMDVSMGGR 600
VAEELIFGTD HITTGASSDF DNATKIAKRM VTKFGMSEKL GVMTYSDTGK LSPETQSAIE 660
QEIRILLRES YERAKHILKT HAKEHKNLAE ALLTYETLDA KEIQIVLEGK KLEVR 715 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. GO:0008283; P:cell proliferation; ISS:UniProtKB. GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; ISS:UniProtKB. GO:0007005; P:mitochondrion organization; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |