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Sequence of MEP1B_HUMAN

EC Number:3.4.24.63

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
meprin B
Q16820
Homo sapiens
701
79571
Reaction
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-/-Leu-, -Leu6-/-Cys-, -Ala14-/-Leu- and -Cys19-/-Gly- bonds in insulin B chain
Other sequences found for EC No. 3.4.24.63

General information:

Sequence
show sequence in fasta format
  0 MDLWNLSWFL FLDALLVISG LATPENFDVD GGMDQDIFDI NEGLGLDLFE GDIRLDRAQI
 60 RNSIIGEKYR WPHTIPYVLE DSLEMNAKGV ILNAFERYRL KTCIDFKPWA GETNYISVFK
120 GSGCWSSVGN RRVGKQELSI GANCDRIATV QHEFLHALGF WHEQSRSDRD DYVRIMWDRI
180 LSGREHNFNT YSDDISDSLN VPYDYTSVMH YSKTAFQNGT EPTIVTRISD FEDVIGQRMD
240 FSDSDLLKLN QLYNCSSSLS FMDSCSFELE NVCGMIQSSG DNADWQRVSQ VPRGPESDHS
300 NMGQCQGSGF FMHFDSSSVN VGATAVLESR TLYPKRGFQC LQFYLYNSGS ESDQLNIYIR
360 EYSADNVDGN LTLVEEIKEI PTGSWQLYHV TLKVTKKFRV VFEGRKGSGA SLGGLSIDDI
420 NLSETRCPHH IWHIRNFTQF IGSPNGTLYS PPFYSSKGYA FQIYLNLAHV TNAGIYFHLI
480 SGANDDQLQW PCPWQQATMT LLDQNPDIRQ RMSNQRSITT DPFMTTDNGN YFWDRPSKVG
540 TVALFSNGTQ FRRGGGYGTS AFITHERLKS RDFIKGDDVY ILLTVEDISH LNSTQIQLTP
600 APSVQDLCSK TTCKNDGVCT VRDGKAECRC QSGEDWWYMG ERCEKRGSTR DTIVIAVSST
660 VAVFALMLII TLVSVYCTRK KYRERMSSNR PNLTPQNQHA F
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1212638
Eldering J.A.,Gruenberg J.,Hahn D.,Croes H.J.,Fransen J.A.,Sterchi E.E.
Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells.
Eur. J. Biochem.
247
920-932
1997
1212640
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
1212641
Dumermuth E.,Eldering J.A.,Gruenberg J.,Jiang W.,Sterchi E.E.
Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells.
FEBS Lett.
335
367-375
1993
1212642
Pischitzis A.,Hahn D.,Leuenberger B.,Sterchi E.E.
N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase beta (human meprinbeta). A 13-amino-acid sequence is required for proteolytic processing and subsequent secretion.
Eur. J. Biochem.
261
421-429
1999
1212643
Leuenberger B.,Hahn D.,Pischitzis A.,Hansen M.K.,Sterchi E.E.
Human meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion.
Biochem. J.
369
659-665
2003
1212644
Villa J.P.,Bertenshaw G.P.,Bond J.S.
Critical amino acids in the active site of meprin metalloproteinases for substrate and peptide bond specificity.
J. Biol. Chem.
278
42545-42550
2003
1212645
Banerjee S.,Bond J.S.
Prointerleukin-18 is activated by meprin beta in vitro and in vivo in intestinal inflammation.
J. Biol. Chem.
283
31371-31377
2008
1212646
Huguenin M.,Muller E.J.,Trachsel-Rosmann S.,Oneda B.,Ambort D.,Sterchi E.E.,Lottaz D.
The metalloprotease meprinbeta processes E-cadherin and weakens intercellular adhesion.
PLoS ONE
3
0-0
2008
1212647
Hedrich J.,Lottaz D.,Meyer K.,Yiallouros I.,Jahnen-Dechent W.,Stocker W.,Becker-Pauly C.
Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases.
Biochemistry
49
8599-8607
2010
1212648
Ambort D.,Brellier F.,Becker-Pauly C.,Stocker W.,Andrejevic-Blant S.,Chiquet M.,Sterchi E.E.
Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading.
Matrix Biol.
29
31-42
2010
1212649
Becker-Pauly C.,Barre O.,Schilling O.,Auf dem Keller U.,Ohler A.,Broder C.,Schutte A.,Kappelhoff R.,Stocker W.,Overall C.M.
Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates.
Mol. Cell. Proteomics
10
0-0
2011
1212650
Jefferson T.,Auf dem Keller U.,Bellac C.,Metz V.V.,Broder C.,Hedrich J.,Ohler A.,Maier W.,Magdolen V.,Sterchi E.,Bond J.S.,Jayakumar A.,Traupe H.,Chalaris A.,Rose-John S.,Pietrzik C.U.,Postina R.,Overall C.M.,Becker-Pauly C.
The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin beta and ADAM10.
Cell. Mol. Life Sci.
70
309-333
2013
1212651
Arolas J.L.,Broder C.,Jefferson T.,Guevara T.,Sterchi E.E.,Bode W.,Stocker W.,Becker-Pauly C.,Gomis-Ruth F.X.
Structural basis for the sheddase function of human meprin beta metalloproteinase at the plasma membrane.
Proc. Natl. Acad. Sci. U.S.A.
109
16131-16136
2012
1212652
de Ligt J.,Willemsen M.H.,van Bon B.W.,Kleefstra T.,Yntema H.G.,Kroes T.,Vulto-van Silfhout A.T.,Koolen D.A.,de Vries P.,Gilissen C.,del Rosario M.,Hoischen A.,Scheffer H.,de Vries B.B.,Brunner H.G.,Veltman J.A.,Vissers L.E.
Diagnostic exome sequencing in persons with severe intellectual disability.
N. Engl. J. Med.
367
1921-1929
2012