ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q91YP2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name NEUL_MOUSE
Primary accession number Q91YP2
Secondary accession numbers Q3UJP1 Q8R3F4
Integrated into Swiss-Prot on February 26, 2008
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Neurolysin, mitochondrial [Precursor]
Synonyms EC 3.4.24.16
Neurotensin endopeptidase
Mitochondrial oligopeptidase M
Microsomal endopeptidase
MEP
Gene name
Name: Nln
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/c, and C57BL/6J;
TISSUE=Diencephalon;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK079090; BAC37533.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK146364; BAE27114.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016224; AAH16224.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025520; AAH25520.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_083723.1; -.
UniGene Mm.127692
3D structure databases
HSSP P42676; 1I1I. [HSSP ENTRY / PDB]
ModBase Q91YP2.
Protein family/group databases
MEROPS M03.002; -.
PTM databases
PhosphoSite Q91YP2; -.
Organism-specific databases
MGI MGI:1923055; Nln.
Gene expression databases
ArrayExpress Q91YP2; -.
CleanEx MM_NLN; -.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004222; Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001567; Pept_M3A_M3B.
IPR006025; Pept_M_Zn_BS.
Graphical view of domain structure.
Pfam PF01432; Peptidase_M3; 1.
Pfam graphical view of domain structure.
PROSITE PS00142; ZINC_PROTEASE; 1.
ProtoNet Q91YP2.
Genome annotation databases
Ensembl ENSMUSG00000021710; Mus musculus. [Contig view]
GeneID 75805; -.
KEGG mmu:75805; -.
NMPDR fig|10090.3.peg.28361; -.
Phylogenomic databases
HOGENOM Q91YP2; -.
HOVERGEN Q91YP2; -.
Other
NextBio 344006; -.
SOURCE Nln; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Phosphoprotein; Protease; Transit peptide; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    37  37     Mitochondrion. 
CHAIN   38   704  667     Neurolysin, mitochondrial. PRO_0000319046
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   32    32        Phosphoserine (By similarity). 
CONFLICT   44    44        G -> V (in Ref. 1; BAE27114). 
CONFLICT   329   331        LGE -> HAS (in Ref. 2; AAH25520). 
Sequence information
Length: 704 AA [This is the length of the unprocessed precursor] Molecular weight: 80429 Da [This is the MW of the unprocessed precursor] CRC64: E4F342E346AB0E07 [This is a checksum on the sequence]
        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 

Q91YP2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!