|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1016/S0006-291X(87)80475-8; PubMed=3555489 [NCBI, ExPASy, EBI, Israel, Japan]
Malfroy B.,
Schofield P.R.,
Kuang W.-J.,
Seeburg P.H.,
Mason A.J.,
Henzel W.J.;
"Molecular cloning and amino acid sequence of rat enkephalinase.";
Biochem. Biophys. Res. Commun. 144:59-66(1987).
|
[2]
|
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
|
[3]
|
ACTIVE SITE ARG-103.
PubMed=2703483 [NCBI, ExPASy, EBI, Israel, Japan]
Bateman R.C. Jr.,
Jackson D.,
Slaughter C.A.,
Unnithan S.,
Chai Y.G.,
Moomaw C.,
Hersh L.B.;
"Identification of the active-site arginine in rat neutral endopeptidase 24.11 (enkephalinase) as arginine 102 and analysis of a glutamine 102 mutant.";
J. Biol. Chem. 264:6151-6157(1989).
|
[4]
|
INHIBITION BY SIALORPHIN.
DOI=10.1073/pnas.1431850100; PubMed=12835417 [NCBI, ExPASy, EBI, Israel, Japan]
Rougeot C.,
Messaoudi M.,
Hermitte V.,
Rigault A.G.,
Blisnick T.,
Dugave C.,
Desor D.,
Rougeon F.;
"Sialorphin, a natural inhibitor of rat membrane-bound neutral endopeptidase that displays analgesic activity.";
Proc. Natl. Acad. Sci. U.S.A. 100:8549-8554(2003).
|
|
|
|
- FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Involved in the degradation of atrial natriuretic factor (ANF).
- CATALYTIC ACTIVITY: Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
- COFACTOR: Binds 1 zinc ion per subunit.
- ENZYME REGULATION: Inhibited in a dose dependent manner by sialorphin.
- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
- SIMILARITY: Belongs to the peptidase M13 family [view classification].
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 750 AA [This is the length of the unprocessed precursor] |
Molecular weight: 85795 Da [This is the MW of the unprocessed precursor] |
CRC64: 609D4716C4B15CBC [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MGRSESQMDI TDINAPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS
70 80 90 100 110 120
DCIKSAARLI QNMDASAEPC TDFFKYACGG WLKRNVIPET SSRYSNFDIL RDELEVILKD
130 140 150 160 170 180
VLQEPKTEDI VAVQKAKTLY RSCINESAID SRGGQPLLTL LPDIYGWPVA SQNWEQTYGT
190 200 210 220 230 240
SWTAEKSIAQ LNSKYGKKVL INFFVGTDDK NSTQHIIHFD QPRLGLPSRD YYECTGIYKE
250 260 270 280 290 300
ACTAYVDFMI SVARLIRQEQ RLPIDENQLS LEMNKVMELE KEIANATTKP EDRNDPMLLY
310 320 330 340 350 360
NKMTLAKLQN NFSLEINGKP FSWSNFTNEI MSTVNINIQN EEEVVVYAPE YLTKLKPILT
370 380 390 400 410 420
KYSPRDLQNL MSWRFIMDLV SSLSRNYKES RNAFRKALYG TTSETATWRR CANYVNGNME
430 440 450 460 470 480
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKKAE EKALAIKERI
490 500 510 520 530 540
GYPDDIISNE NKLNNEYLEL NYKEEEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA
550 560 570 580 590 600
VVNAFYSSGR NQIVFPAGIL QPPFFSARQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
610 620 630 640 650 660
GDLVDWWTQQ SANNFKDQSQ CMVYQYGNFT WDLAGGQHLN GINTLGENIA DNGGIGQAYR
670 680 690 700 710 720
AYQNYVKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
730 740 750
GTLQNSAEFA DAFHCRKNSY MNPERKCRVW
|
P07861 in FASTA format |
|