| Tag | Content |
|---|
| CPLM ID | CPLM-007583 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Neurolysin, mitochondrial |
Protein Synonyms/Alias | Microsomal endopeptidase; MEP; Mitochondrial oligopeptidase M; Neurotensin endopeptidase |
Gene Name | Nln |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 58 | DLSPEQIKTRTEQLI | acetylation | [1] | | 69 | EQLIAQTKQVYDTVG | acetylation | [1] | | 238 | LEKTDEDKYKVTLKY | acetylation | [1] | | 253 | PHYFPVMKKCCVPET | acetylation | [1] | | 424 | SVSLYTVKDKATGEV | acetylation | [1] | | 664 | MNPEVGMKYRNLILK | acetylation | [1] | | 693 | LQREPNQKAFLMSRG | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. |
Sequence Annotation | ACT_SITE 498 498 By similarity.
METAL 497 497 Zinc; catalytic (By similarity).
METAL 501 501 Zinc; catalytic (By similarity).
METAL 504 504 Zinc; catalytic (By similarity).
MOD_RES 664 664 N6-acetyllysine (By similarity). |
Keyword | 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease; Reference proteome; Transit peptide; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 704 AA |
Protein Sequence | MITLCLSTLR GLHRAGGSRL QLTMTLGKEL ASPLQAMSSY TAAGRNVLRW DLSPEQIKTR 60
TEQLIAQTKQ VYDTVGTIAL KEVTYENCLQ VLADIEVTYI VERTMLDFPQ HVSSDREVRA 120
ASTEADKKLS RFDIEMSMRE DVFQRIVHLQ ETCDLEKIKP EARRYLEKSI KMGKRNGLHL 180
SEHIRNEIKS MKKRMSELCI DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK 240
VTLKYPHYFP VMKKCCVPET RRKMEMAFHT RCKQENTAIL QQLLPLRAQV AKLLGYNTHA 300
DFVLELNTAK STSRVAAFLD DLSQKLKPLG EAEREFILSL KKKECEERGF EYDGKINAWD 360
LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL LGLSFEQVPD AHVWNKSVSL 420
YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMSVA ALVVNFSQPV 480
AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD 540
SLRKLSKHYK DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NATLDAASEY 600
AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC FKKEGIMNPE 660
VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG LNGS 704 |
Gene Ontology | GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |