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Sequence of MMEL1_RAT

EC Number:3.4.24.11

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
neprilysin
P0C1T0
Rattus norvegicus
774
89197
Reaction
preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'
Other sequences found for EC No. 3.4.24.11

General information:

Sequence
show sequence in fasta format
  0 MGKSESSVGM MERADNCGRR RLGFVECGLL VLLTLLLMGA IVTLGVFYSI GKQLPLLNSL
 60 LHVSRHERTV VKRVLRDSSQ KSDICTTPSC VIAAARILQN MDQSKKPCDN FYQYACGGWL
120 RHHVIPETNS RYSVFDILRD ELEVILKGVL EDSSVQHRPA VEKAKTLYRS CMNQSVIEKR
180 DSEPLLNVLD MIGGWPVAMD KWNETMGPKW ELERQLAVLN SQFNRRVLID LFIWNDDQNS
240 SRHVIYIDQP TLGMPSREYY FKEDSHRVRE AYLQFMTSVA TMLRRDLNLP GETDLVQEEM
300 AQVLHLETHL ANATVPQEKR HDVTALYHRM GLEELQERFG LKGFNWTLFI QNVLSSVQVE
360 LLPNEEVVVY GIPYLENLEE IIDVFPAQTL QNYLVWRLVL DRIGSLSQRF KEARVDYRKA
420 LYGTTMEEVR WRECVSYVNS NMESAVGSLY IKRAFSKDSK SIVSELIEKI RSVFVDNLDE
480 LNWMDEESKK KAQEKALNIR EQIGYPDYIL EDNNRHLDEE YSSLTFSEDL YFENGLQNLK
540 NNAQRSLKKL REKVDQNLWI IGAAVVNAFY SPNRNLIVFP AGILQPPFFS KDQPQALNFG
600 GIGMVIGHEI THGFDDNGRN FDKNGNMLDW WSNFSARHFR QQSQCMIYQY SNFSWELADN
660 QNVNGFSTLG ENIADNGGVR QAYKAYLQWL AEGGRDQRLP GLNLTYAQLF FINYAQVWCG
720 SYRPEFAIQS IKTDVHSPLN AQVLGSLQNL PGFSEAFHCP RGSPMHPMNR CRIW
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
954916
Ouimet T.,Facchinetti P.,Rose C.,Bonhomme M.-C.,Gros C.,Schwartz J.-C.
Neprilysin II: a putative novel metalloprotease and its isoforms in CNS and testis.
Biochem. Biophys. Res. Commun.
271
565-570
2000
954918
Gibbs R.A.,Weinstock G.M.,Metzker M.L.,Muzny D.M.,Sodergren E.J.,Scherer S.,Scott G.,Steffen D.,Worley K.C.,Burch P.E.,Okwuonu G.,Hines S.,Lewis L.,Deramo C.,Delgado O.,Dugan-Rocha S.,Miner G.,Morgan M.,Hawes A.,Gill R.,Holt R.A.,Adams M.D.,Amanatides P.G.,Baden-Tillson H.,Barnstead M.,Chin S.,Evans C.A.,Ferriera S.,Fosler C.,Glodek A.,Gu Z.,Jennings D.,Kraft C.L.,Nguyen T.,Pfannkoch C.M.,Sitter C.,Sutton G.G.,Venter J.C.,Woodage T.,Smith D.,Lee H.-M.,Gustafson E.,Cahill P.,Kana A.,Doucette-Stamm L.,Weinstock K.,Fechtel K.,Weiss R.B.,Dunn D.M.,Green E.D.,Blakesley R.W.,Bouffard G.G.,De Jong P.J.,Osoegawa K.,Zhu B.,Marra M.,Schein J.,Bosdet I.,Fjell C.,Jones S.,Krzywinski M.,Mathewson C.,Siddiqui A.,Wye N.,McPherson J.,Zhao S.,Fraser C.M.,Shetty J.,Shatsman S.,Geer K.,Chen Y.,Abramzon S.,Nierman W.C.,Havlak P.H.,Chen R.,Durbin K.J.,Egan A.,Ren Y.,Song X.-Z.,Li B.,Liu Y.,Qin X.,Cawley S.,Cooney A.J.,D'Souza L.M.,Martin K.,Wu J.Q.,Gonzalez-Garay M.L.,Jackson A.R.,Kalafus K.J.,McLeod M.P.,Milosavljevic A.,Virk D.,Volkov A.,Wheeler D.A.,Zhang Z.,Bailey J.A.,Eichler E.E.,Tuzun E.,Birney E.,Mongin E.,Ureta-Vidal A.,Woodwark C.,Zdobnov E.,Bork P.,Suyama M.,Torrents D.,Alexandersson M.,Trask B.J.,Young J.M.,Huang H.,Wang H.,Xing H.,Daniels S.,Gietzen D.,Schmidt J.,Stevens K.,Vitt U.,Wingrove J.,Camara F.,Mar Alba M.,Abril J.F.,Guigo R.,Smit A.,Dubchak I.,Rubin E.M.,Couronne O.,Poliakov A.,Huebner N.,Ganten D.,Goesele C.,Hummel O.,Kreitler T.,Lee Y.-A.,Monti J.,Schulz H.,Zimdahl H.,Himmelbauer H.,Lehrach H.,Jacob H.J.,Bromberg S.,Gullings-Handley J.,Jensen-Seaman M.I.,Kwitek A.E.,Lazar J.,Pasko D.,Tonellato P.J.,Twigger S.,Ponting C.P.,Duarte J.M.,Rice S.,Goodstadt L.,Beatson S.A.,Emes R.D.,Winter E.E.,Webber C.,Brandt P.,Nyakatura G.,Adetobi M.,Chiaromonte F.,Elnitski L.,Eswara P.,Hardison R.C.,Hou M.,Kolbe D.,Makova K.,Miller W.,Nekrutenko A.,Riemer C.,Schwartz S.,Taylor J.,Yang S.,Zhang Y.,Lindpaintner K.,Andrews T.D.,Caccamo M.,Clamp M.,Clarke L.,Curwen V.,Durbin R.M.,Eyras E.,Searle S.M.,Cooper G.M.,Batzoglou S.,Brudno M.,Sidow A.,Stone E.A.,Payseur B.A.,Bourque G.,Lopez-Otin C.,Puente X.S.,Chakrabarti K.,Chatterji S.,Dewey C.,Pachter L.,Bray N.,Yap V.B.,Caspi A.,Tesler G.,Pevzner P.A.,Haussler D.,Roskin K.M.,Baertsch R.,Clawson H.,Furey T.S.,Hinrichs A.S.,Karolchik D.,Kent W.J.,Rosenbloom K.R.,Trumbower H.,Weirauch M.,Cooper D.N.,Stenson P.D.,Ma B.,Brent M.,Arumugam M.,Shteynberg D.,Copley R.R.,Taylor M.S.,Riethman H.,Mudunuri U.,Peterson J.,Guyer M.,Felsenfeld A.,Old S.,Mockrin S.,Collins F.S.
Genome sequence of the Brown Norway rat yields insights into mammalian evolution.
Nature
428
493-521
2004
954919
Facchinetti P.,Rose C.,Schwartz J.C.,Ouimet T.
Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: a comparison with neprilysin and endothelin-converting enzyme-1.
Neuroscience
118
627-639
2003
954920
Voisin S.,Rognan D.,Gros C.,Ouimet T.
A three-dimensional model of the neprilysin 2 active site based on the X-ray structure of neprilysin. Identification of residues involved in substrate hydrolysis and inhibitor binding of neprilysin 2.
J. Biol. Chem.
279
46172-46181
2004
954921
Rose C.,Voisin S.,Gros C.,Schwartz J.-C.,Ouimet T.
Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin.
Biochem. J.
363
697-705
2002
954922
Voisin S.,Ouimet T.
The ultimate tryptophan residue of neprilysin 2 is not involved in protein maturation and enzymatic activity.
Biochem. Biophys. Res. Commun.
335
356-360
2005