ID   NEUL_MOUSE              Reviewed;         704 AA.
AC   Q91YP2; Q3UJP1; Q8R3F4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Neurolysin, mitochondrial;
DE            EC=3.4.24.16;
DE   AltName: Full=Neurotensin endopeptidase;
DE   AltName: Full=Mitochondrial oligopeptidase M;
DE   AltName: Full=Microsomal endopeptidase;
DE            Short=MEP;
DE   Flags: Precursor;
GN   Name=Nln;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin
CC       and dynorphin A (By similarity).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage in neurotensin: 10-
CC       Pro-|-Tyr-11.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space (By
CC       similarity). Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
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DR   EMBL; AK079090; BAC37533.1; -; mRNA.
DR   EMBL; AK146364; BAE27114.1; -; mRNA.
DR   EMBL; BC016224; AAH16224.1; -; mRNA.
DR   EMBL; BC025520; AAH25520.1; -; mRNA.
DR   IPI; IPI00314829; -.
DR   RefSeq; NP_083723.1; -.
DR   UniGene; Mm.127692; -.
DR   HSSP; P42676; 1I1I.
DR   MEROPS; M03.002; -.
DR   PhosphoSite; Q91YP2; -.
DR   PRIDE; Q91YP2; -.
DR   Ensembl; ENSMUSG00000021710; Mus musculus.
DR   GeneID; 75805; -.
DR   KEGG; mmu:75805; -.
DR   NMPDR; fig|10090.3.peg.28361; -.
DR   MGI; MGI:1923055; Nln.
DR   HOGENOM; Q91YP2; -.
DR   HOVERGEN; Q91YP2; -.
DR   BRENDA; 3.4.24.16; 244.
DR   NextBio; 344006; -.
DR   ArrayExpress; Q91YP2; -.
DR   Bgee; Q91YP2; -.
DR   CleanEx; MM_NLN; -.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion;
KW   Phosphoprotein; Protease; Transit peptide; Zinc.
FT   TRANSIT       1     37       Mitochondrion.
FT   CHAIN        38    704       Neurolysin, mitochondrial.
FT                                /FTId=PRO_0000319046.
FT   ACT_SITE    498    498       By similarity.
FT   METAL       497    497       Zinc; catalytic (By similarity).
FT   METAL       501    501       Zinc; catalytic (By similarity).
FT   METAL       504    504       Zinc; catalytic (By similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   CONFLICT     44     44       G -> V (in Ref. 1; BAE27114).
FT   CONFLICT    329    331       LGE -> HAS (in Ref. 2; AAH25520).
SQ   SEQUENCE   704 AA;  80429 MW;  E4F342E346AB0E07 CRC64;
     MITLCLSALR GLHRAGGSRI RLRMTLGREA ASPLQAMSSY TAAGRNVLRW DLSPEQIRTR
     TEELIAQTKQ VYDTVGTINL EDVTYENCLQ VLADIEVKYI VERTMLDFPQ HVSSDREVRA
     ASTEADKRLS RFDIEMSMRE DVFQRIVHLQ ETCDLEKIKP EARRYLEKSI KMGKRNGLHL
     PEHVKNEIKS MKKRMSELCI DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK
     VTLKYPHYFP VMKKCCVPET RRKMEMAFHT RCKEENTIIL QQLLPLRAQV AKLLGYNTHA
     DFVLELNTAK STSHVATFLD DLSQKLKPLG EAEREFILSL KKKECEERGF AYDGKINAWD
     LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL LGLSFEQVAD AHVWNKSVSL
     YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMSVA ALVVNFSQPI
     AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID
     SLRKLSKHYR DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NASLDAASEY
     AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC FRKEGIMNPE
     VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG LNAS
//