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Protein

Neurolysin, mitochondrial

Gene

Nln

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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
  3. peptidase activity Source: MGI
  4. peptide binding Source: MGI

GO - Biological processi

  1. regulation of gluconeogenesis Source: MGI
  2. regulation of skeletal muscle fiber differentiation Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1923055. Nln.

Subcellular locationi

Mitochondrion intermembrane space By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: UniProtKB-SubCell
  2. mitochondrion Source: MGI
  3. plasma membrane Source: MGI
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_0000319046Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ91YP2.
PaxDbiQ91YP2.
PRIDEiQ91YP2.

PTM databases

PhosphoSiteiQ91YP2.

Expressioni

Gene expression databases

BgeeiQ91YP2.
CleanExiMM_NLN.
ExpressionAtlasiQ91YP2. baseline and differential.
GenevestigatoriQ91YP2.

Interactioni

Protein-protein interaction databases

IntActiQ91YP2. 1 interaction.
MINTiMINT-4122037.

Structurei

3D structure databases

ProteinModelPortaliQ91YP2.
SMRiQ91YP2. Positions 37-701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiQ91YP2.
KOiK01393.
OMAiFENWVWE.
OrthoDBiEOG7SR4KW.
PhylomeDBiQ91YP2.
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.

Q91YP2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MITLCLSALR GLHRAGGSRI RLRMTLGREA ASPLQAMSSY TAAGRNVLRW
60 70 80 90 100
DLSPEQIRTR TEELIAQTKQ VYDTVGTINL EDVTYENCLQ VLADIEVKYI
110 120 130 140 150
VERTMLDFPQ HVSSDREVRA ASTEADKRLS RFDIEMSMRE DVFQRIVHLQ
160 170 180 190 200
ETCDLEKIKP EARRYLEKSI KMGKRNGLHL PEHVKNEIKS MKKRMSELCI
210 220 230 240 250
DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK VTLKYPHYFP
260 270 280 290 300
VMKKCCVPET RRKMEMAFHT RCKEENTIIL QQLLPLRAQV AKLLGYNTHA
310 320 330 340 350
DFVLELNTAK STSHVATFLD DLSQKLKPLG EAEREFILSL KKKECEERGF
360 370 380 390 400
AYDGKINAWD LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL
410 420 430 440 450
LGLSFEQVAD AHVWNKSVSL YTVKDKATGE VLGQFYLDLY PREGKYNHAA
460 470 480 490 500
CFGLQPGCLL PDGSRMMSVA ALVVNFSQPI AGRPSLLRHD EVRTYFHEFG
510 520 530 540 550
HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID SLRKLSKHYR
560 570 580 590 600
DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NASLDAASEY
610 620 630 640 650
AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC
660 670 680 690 700
FRKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG

LNAS
Length:704
Mass (Da):80,429
Last modified:December 1, 2001 - v1
Checksum:iE4F342E346AB0E07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441G → V in BAE27114. (PubMed:16141072)Curated
Sequence conflicti329 – 3313LGE → HAS in AAH25520. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK079090 mRNA. Translation: BAC37533.1.
AK146364 mRNA. Translation: BAE27114.1.
BC016224 mRNA. Translation: AAH16224.1.
BC025520 mRNA. Translation: AAH25520.1.
CCDSiCCDS36772.1.
RefSeqiNP_083723.1. NM_029447.2.
UniGeneiMm.127692.

Genome annotation databases

EnsembliENSMUST00000109315; ENSMUSP00000104938; ENSMUSG00000021710.
GeneIDi75805.
KEGGimmu:75805.
UCSCiuc007rsp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK079090 mRNA. Translation: BAC37533.1.
AK146364 mRNA. Translation: BAE27114.1.
BC016224 mRNA. Translation: AAH16224.1.
BC025520 mRNA. Translation: AAH25520.1.
CCDSiCCDS36772.1.
RefSeqiNP_083723.1. NM_029447.2.
UniGeneiMm.127692.

3D structure databases

ProteinModelPortaliQ91YP2.
SMRiQ91YP2. Positions 37-701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91YP2. 1 interaction.
MINTiMINT-4122037.

Protein family/group databases

MEROPSiM03.002.

PTM databases

PhosphoSiteiQ91YP2.

Proteomic databases

MaxQBiQ91YP2.
PaxDbiQ91YP2.
PRIDEiQ91YP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109315; ENSMUSP00000104938; ENSMUSG00000021710.
GeneIDi75805.
KEGGimmu:75805.
UCSCiuc007rsp.1. mouse.

Organism-specific databases

CTDi57486.
MGIiMGI:1923055. Nln.

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiQ91YP2.
KOiK01393.
OMAiFENWVWE.
OrthoDBiEOG7SR4KW.
PhylomeDBiQ91YP2.
TreeFamiTF300459.

Miscellaneous databases

NextBioi344006.
PROiQ91YP2.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YP2.
CleanExiMM_NLN.
ExpressionAtlasiQ91YP2. baseline and differential.
GenevestigatoriQ91YP2.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c and C57BL/6J.
    Tissue: Diencephalon.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiNEUL_MOUSE
AccessioniPrimary (citable) accession number: Q91YP2
Secondary accession number(s): Q3UJP1, Q8R3F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 1, 2001
Last modified: February 4, 2015
This is version 101 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.