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Protein

Neurolysin, mitochondrial

Gene

NLN

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A.By similarity

Catalytic activityi

Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi497 – 4971Zinc; catalyticPROSITE-ProRule annotation
Active sitei498 – 4981PROSITE-ProRule annotation
Metal bindingi501 – 5011Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi504 – 5041Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM03.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurolysin, mitochondrial (EC:3.4.24.16)
Alternative name(s):
Microsomal endopeptidase
Short name:
MEP
Mitochondrial oligopeptidase M
Neurotensin endopeptidase
Gene namesi
Name:NLN
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Mitochondrion intermembrane space By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionAdd
BLAST
Chaini38 – 704667Neurolysin, mitochondrialPRO_0000319048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei664 – 6641N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ5R9V6.

Structurei

3D structure databases

ProteinModelPortaliQ5R9V6.
SMRiQ5R9V6. Positions 37-701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG000238.
InParanoidiQ5R9V6.
KOiK01393.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5R9V6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIARCLLAVR SLRRVGGSRI LLRMTLGREV MSPLQAMSSY TVTGRNVLRW
60 70 80 90 100
DLSPEQIKTR TEELIVQTKQ VYDAVGMLGI EEVTYENCLQ ALADIEVKYI
110 120 130 140 150
VERTMLDFPQ HVSSDKEVRA ASTEADKRLS RFDIEMSMRG DIFERIVRLQ
160 170 180 190 200
ETCDLGKIKP EARRYLEKSI KMGKRNGLHL PEQVQNEIKS MKKRMSELCI
210 220 230 240 250
DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKIDDDKYK ITLKYPHYFP
260 270 280 290 300
VMKKCCIPET RRRMEMAFNT RCKEENTIIL QQLLPLRAKV AKLLGYSTHA
310 320 330 340 350
DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILNL KKKECEDRGF
360 370 380 390 400
EYDGKINAWD LYYYMTQTEE LKYSIDQEFL KEYFPIEVVT EGLLNTYQEL
410 420 430 440 450
LGLSFEQVTD AHVWNKNVTL YTVKDKATGE VLGQFYLDLY PRDRKYNHAA
460 470 480 490 500
CFGLQPGCLL PDGSRMMAVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG
510 520 530 540 550
HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD SLRRLSKHYK
560 570 580 590 600
DGSPISDDLL EKLVASRLIN TGLLTLRQIV LSKVDQSLHT NTSLDAASEY
610 620 630 640 650
AKYCSEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC
660 670 680 690 700
FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLHNFLKREP NQKAFLMSRG

LHAS
Length:704
Mass (Da):80,798
Last modified:December 21, 2004 - v1
Checksum:iCDE234F0F169D7C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859276 mRNA. Translation: CAH91454.1.
RefSeqiNP_001127421.1. NM_001133949.2.
UniGeneiPab.7982.

Genome annotation databases

GeneIDi100174491.
KEGGipon:100174491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859276 mRNA. Translation: CAH91454.1.
RefSeqiNP_001127421.1. NM_001133949.2.
UniGeneiPab.7982.

3D structure databases

ProteinModelPortaliQ5R9V6.
SMRiQ5R9V6. Positions 37-701.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM03.002.

Proteomic databases

PRIDEiQ5R9V6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174491.
KEGGipon:100174491.

Organism-specific databases

CTDi57486.

Phylogenomic databases

HOVERGENiHBG000238.
InParanoidiQ5R9V6.
KOiK01393.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiNEUL_PONAB
AccessioniPrimary (citable) accession number: Q5R9V6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.