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Q91YP2 (NEUL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurolysin, mitochondrial
EC=3.4.24.16
Alternative name(s):
Microsomal endopeptidase
Short name=MEP
Mitochondrial oligopeptidase M
Neurotensin endopeptidase
Gene names
Name:Nln
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Mitochondrion intermembrane space By similarity. Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial intermembrane space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion
Chain38 – 704667Neurolysin, mitochondrial
PRO_0000319046

Sites

Active site4981 By similarity
Metal binding4971Zinc; catalytic By similarity
Metal binding5011Zinc; catalytic By similarity
Metal binding5041Zinc; catalytic By similarity

Amino acid modifications

Modified residue321Phosphoserine By similarity
Modified residue6641N6-acetyllysine By similarity

Experimental info

Sequence conflict441G → V in BAE27114. Ref.1
Sequence conflict329 – 3313LGE → HAS in AAH25520. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q91YP2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E4F342E346AB0E07

FASTA70480,429
        10         20         30         40         50         60 
MITLCLSALR GLHRAGGSRI RLRMTLGREA ASPLQAMSSY TAAGRNVLRW DLSPEQIRTR 

        70         80         90        100        110        120 
TEELIAQTKQ VYDTVGTINL EDVTYENCLQ VLADIEVKYI VERTMLDFPQ HVSSDREVRA 

       130        140        150        160        170        180 
ASTEADKRLS RFDIEMSMRE DVFQRIVHLQ ETCDLEKIKP EARRYLEKSI KMGKRNGLHL 

       190        200        210        220        230        240 
PEHVKNEIKS MKKRMSELCI DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK 

       250        260        270        280        290        300 
VTLKYPHYFP VMKKCCVPET RRKMEMAFHT RCKEENTIIL QQLLPLRAQV AKLLGYNTHA 

       310        320        330        340        350        360 
DFVLELNTAK STSHVATFLD DLSQKLKPLG EAEREFILSL KKKECEERGF AYDGKINAWD 

       370        380        390        400        410        420 
LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL LGLSFEQVAD AHVWNKSVSL 

       430        440        450        460        470        480 
YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMSVA ALVVNFSQPI 

       490        500        510        520        530        540 
AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID 

       550        560        570        580        590        600 
SLRKLSKHYR DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NASLDAASEY 

       610        620        630        640        650        660 
AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC FRKEGIMNPE 

       670        680        690        700 
VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG LNAS

« Hide

References

[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK079090 mRNA. Translation: BAC37533.1.
AK146364 mRNA. Translation: BAE27114.1.
BC016224 mRNA. Translation: AAH16224.1.
BC025520 mRNA. Translation: AAH25520.1.
IPIIPI00314829.
RefSeqNP_083723.1. NM_029447.2.
UniGeneMm.127692.

3D structure databases

HSSPHSSP built from PDB template 1I1I based on UniProtKB P42676.
ProteinModelPortalQ91YP2.
SMRQ91YP2. Positions 37-701.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ91YP2.

Protein family/group databases

MEROPSM03.002.

PTM databases

PhosphoSiteQ91YP2.

Proteomic databases

PRIDEQ91YP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109315; ENSMUSP00000104938; ENSMUSG00000021710.
GeneID75805.
KEGGmmu:75805.
NMPDRfig|10090.3.peg.28361.
UCSCuc007rsp.1. mouse.

Organism-specific databases

CTD57486.
MGIMGI:1923055. Nln.

Phylogenomic databases

GeneTreeENSGT00550000074738.
HOVERGENHBG000238.
OrthoDBEOG4CG07P.

Gene expression databases

ArrayExpressQ91YP2.
BgeeQ91YP2.
CleanExMM_NLN.
GenevestigatorQ91YP2.

Family and domain databases

InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
Gene3DG3DSA:1.10.1370.10. G3DSA:1.10.1370.10. 2 hits.
G3DSA:1.20.1050.40. G3DSA:1.20.1050.40. 1 hit.
G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
KOK01393.
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio344006.
SOURCESearch...

Entry information

Entry nameNEUL_MOUSE
AccessionPrimary (citable) accession number: Q91YP2
Secondary accession number(s): Q3UJP1, Q8R3F4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 1, 2001
Last modified: November 16, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents