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Protein

Neurolysin, mitochondrial

Gene

Nln

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A.

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)DescriptionActionsGraphical viewLength
Metal bindingi497Zinc; catalyticPROSITE-ProRule annotation1
Active sitei498PROSITE-ProRule annotation1
Metal bindingi501Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi504Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: RGD
  • oligopeptidase activity Source: RGD

GO - Biological processi

  • peptide metabolic process Source: GO_Central
  • proteolysis Source: RGD
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621518. Nln.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • mitochondrial intermembrane space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 37Mitochondrion1 PublicationAdd BLAST37
ChainiPRO_000002857838 – 704Neurolysin, mitochondrialAdd BLAST667

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei664N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP42676.
PRIDEiP42676.

PTM databases

iPTMnetiP42676.
PhosphoSitePlusiP42676.
SwissPalmiP42676.

Miscellaneous databases

PMAP-CutDBP42676.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011561.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059652.

Structurei

Secondary structure

1704
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni43 – 45Combined sources3
Helixi54 – 75Combined sources22
Helixi80 – 82Combined sources3
Turni85 – 88Combined sources4
Helixi89 – 107Combined sources19
Helixi109 – 112Combined sources4
Helixi116 – 137Combined sources22
Helixi140 – 152Combined sources13
Helixi160 – 175Combined sources16
Turni176 – 179Combined sources4
Helixi182 – 187Combined sources6
Helixi189 – 208Combined sources20
Beta strandi212 – 216Combined sources5
Turni217 – 222Combined sources6
Helixi225 – 229Combined sources5
Beta strandi231 – 233Combined sources3
Beta strandi235 – 244Combined sources10
Helixi245 – 254Combined sources10
Helixi258 – 268Combined sources11
Turni269 – 272Combined sources4
Helixi273 – 293Combined sources21
Helixi299 – 304Combined sources6
Helixi312 – 347Combined sources36
Helixi358 – 360Combined sources3
Helixi361 – 372Combined sources12
Helixi377 – 380Combined sources4
Helixi381 – 383Combined sources3
Helixi386 – 401Combined sources16
Beta strandi403 – 407Combined sources5
Beta strandi419 – 425Combined sources7
Turni426 – 428Combined sources3
Beta strandi431 – 438Combined sources8
Beta strandi450 – 455Combined sources6
Beta strandi468 – 473Combined sources6
Beta strandi481 – 483Combined sources3
Helixi489 – 507Combined sources19
Beta strandi510 – 512Combined sources3
Helixi513 – 515Combined sources3
Turni522 – 526Combined sources5
Helixi527 – 533Combined sources7
Helixi534 – 537Combined sources4
Helixi539 – 545Combined sources7
Beta strandi549 – 551Combined sources3
Helixi557 – 565Combined sources9
Turni566 – 570Combined sources5
Helixi571 – 588Combined sources18
Helixi596 – 606Combined sources11
Helixi618 – 621Combined sources4
Beta strandi625 – 628Combined sources4
Helixi635 – 649Combined sources15
Helixi651 – 654Combined sources4
Helixi659 – 669Combined sources11
Turni670 – 672Combined sources3
Helixi673 – 675Combined sources3
Helixi678 – 686Combined sources9
Helixi693 – 699Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I1IX-ray2.30P24-704[»]
2O3EX-ray2.20A24-701[»]
4FXYX-ray2.80P/Q24-704[»]
ProteinModelPortaliP42676.
SMRiP42676.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42676.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2089. Eukaryota.
COG0339. LUCA.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP42676.
KOiK01393.
PhylomeDBiP42676.
TreeFamiTF300459.

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.

P42676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITLCLSTLR GLHRAGGSRL QLTMTLGKEL ASPLQAMSSY TAAGRNVLRW
60 70 80 90 100
DLSPEQIKTR TEQLIAQTKQ VYDTVGTIAL KEVTYENCLQ VLADIEVTYI
110 120 130 140 150
VERTMLDFPQ HVSSDREVRA ASTEADKKLS RFDIEMSMRE DVFQRIVHLQ
160 170 180 190 200
ETCDLEKIKP EARRYLEKSI KMGKRNGLHL SEHIRNEIKS MKKRMSELCI
210 220 230 240 250
DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK VTLKYPHYFP
260 270 280 290 300
VMKKCCVPET RRKMEMAFHT RCKQENTAIL QQLLPLRAQV AKLLGYNTHA
310 320 330 340 350
DFVLELNTAK STSRVAAFLD DLSQKLKPLG EAEREFILSL KKKECEERGF
360 370 380 390 400
EYDGKINAWD LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL
410 420 430 440 450
LGLSFEQVPD AHVWNKSVSL YTVKDKATGE VLGQFYLDLY PREGKYNHAA
460 470 480 490 500
CFGLQPGCLL PDGSRMMSVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG
510 520 530 540 550
HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD SLRKLSKHYK
560 570 580 590 600
DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NATLDAASEY
610 620 630 640 650
AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC
660 670 680 690 700
FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG

LNGS
Length:704
Mass (Da):80,254
Last modified:November 1, 1995 - v1
Checksum:iE33F7967A79343D1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128K → R in AAH72687 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87157 mRNA. Translation: CAA60630.1.
BC072687 mRNA. Translation: AAH72687.1.
RefSeqiNP_446422.2. NM_053970.2.
UniGeneiRn.11029.

Genome annotation databases

GeneIDi117041.
KEGGirno:117041.
UCSCiRGD:621518. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87157 mRNA. Translation: CAA60630.1.
BC072687 mRNA. Translation: AAH72687.1.
RefSeqiNP_446422.2. NM_053970.2.
UniGeneiRn.11029.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I1IX-ray2.30P24-704[»]
2O3EX-ray2.20A24-701[»]
4FXYX-ray2.80P/Q24-704[»]
ProteinModelPortaliP42676.
SMRiP42676.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059652.

Protein family/group databases

MEROPSiM03.002.

PTM databases

iPTMnetiP42676.
PhosphoSitePlusiP42676.
SwissPalmiP42676.

Proteomic databases

PaxDbiP42676.
PRIDEiP42676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117041.
KEGGirno:117041.
UCSCiRGD:621518. rat.

Organism-specific databases

CTDi57486.
RGDi621518. Nln.

Phylogenomic databases

eggNOGiKOG2089. Eukaryota.
COG0339. LUCA.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP42676.
KOiK01393.
PhylomeDBiP42676.
TreeFamiTF300459.

Miscellaneous databases

EvolutionaryTraceiP42676.
PMAP-CutDBP42676.
PROiP42676.

Gene expression databases

BgeeiENSRNOG00000011561.

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...

Entry informationi

Entry nameiNEUL_RAT
AccessioniPrimary (citable) accession number: P42676
Secondary accession number(s): Q6GQQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 136 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.