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Sequence of AMPN_PIG

EC Number:3.4.11.2

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
membrane alanyl aminopeptidase
P15145
Sus scrofa
963
108832
Reaction
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
Other sequences found for EC No. 3.4.11.2

General information:

Sequence
show sequence in fasta format
  0 MAKGFYISKA LGILGILLGV AAVATIIALS VVYAQEKNKN AEHVPQAPTS PTITTTAAIT
 60 LDQSKPWNRY RLPTTLLPDS YNVTLRPYLT PNADGLYIFK GKSIVRLLCQ EPTDVIIIHS
120 KKLNYTTQGH MVVLRGVGDS QVPEIDRTEL VELTEYLVVH LKGSLQPGHM YEMESEFQGE
180 LADDLAGFYR SEYMEGNVKK VLATTQMQST DARKSFPCFD EPAMKATFNI TLIHPNNLTA
240 LSNMPPKGSS TPLAEDPNWS VTEFETTPVM STYLLAYIVS EFQSVNETAQ NGVLIRIWAR
300 PNAIAEGHGM YALNVTGPIL NFFANHYNTS YPLPKSDQIA LPDFNAGAME NWGLVTYREN
360 ALLFDPQSSS ISNKERVVTV IAHELAHQWF GNLVTLAWWN DLWLNEGFAS YVEYLGADHA
420 EPTWNLKDLI VPGDVYRVMA VDALASSHPL TTPAEEVNTP AQISEMFDSI SYSKGASVIR
480 MLSNFLTEDL FKEGLASYLH AFAYQNTTYL DLWEHLQKAV DAQTSIRLPD TVRAIMDRWT
540 LQMGFPVITV DTKTGNISQK HFLLDSESNV TRSSAFDYLW IVPISSIKNG VMQDHYWLRD
600 VSQAQNDLFK TASDDWVLLN VNVTGYFQVN YDEDNWRMIQ HQLQTNLSVI PVINRAQVIY
660 DSFNLATAHM VPVTLALDNT LFLNGEKEYM PWQAALSSLS YFSLMFDRSE VYGPMKKYLR
720 KQVEPLFQHF ETLTKNWTER PENLMDQYSE INAISTACSN GLPQCENLAK TLFDQWMSDP
780 ENNPIHPNLR STIYCNAIAQ GGQDQWDFAW GQLQQAQLVN EADKLRSALA CSNEVWLLNR
840 YLGYTLNPDL IRKQDATSTI NSIASNVIGQ PLAWDFVQSN WKKLFQDYGG GSFSFSNLIQ
900 GVTRRFSSEF ELQQLEQFKK NNMDVGFGSG TRALEQALEK TKANIKWVKE NKEVVLNWFI
960 EHS
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1028365
Delmas B.,Gelfi J.,Kut E.,Sjoestroem H.,Noren O.,Laude H.
Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site.
J. Virol.
68
5216-5224
1994
1028366
Olsen J.,Sjoestroem H.,Noren O.
Cloning of the pig aminopeptidase N gene. Identification of possible regulatory elements and the exon distribution in relation to the membrane-spanning region.
FEBS Lett.
251
275-281
1989
1028367
See H.,Reithmeier R.A.F.
Identification and characterization of the major stilbene-disulphonate- and concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N.
Biochem. J.
271
147-155
1990
1028368
Winteroe A.K.,Fredholm M.,Davies W.
Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones.
Mamm. Genome
7
509-517
1996
1028369
Delmas B.,Gelfi J.,L'Haridon R.,Vogel L.K.,Sjostrom H.,Noren O.,Laude H.
Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV.
Nature
357
417-420
1992
1028370
Delmas B.,Gelfi J.,Sjostrom H.,Noren O.,Laude H.
Further characterization of aminopeptidase-N as a receptor for coronaviruses.
Adv. Exp. Med. Biol.
342
293-298
1993
1028371
Terashima H.,Bunnett N.W.
Purification and characterization of aminopeptidase M from muscle and mucosa of the pig intestine.
J. Gastroenterol.
30
696-704
1995
1028372
Benbacer L.,Kut E.,Besnardeau L.,Laude H.,Delmas B.
Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus.
J. Virol.
71
734-737
1997
1028373
Hegyi A.,Kolb A.F.
Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N.
J. Gen. Virol.
79
1387-1391
1998
1028374
Benajiba A.,Maroux S.
Subunit structured of pig small-intestinal brush-border aminopeptidase N.
Biochem. J.
197
573-580
1981
1028375
Danielsen E.M.
Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte.
EMBO J.
6
2891-2896
1987
1028376
Reguera J.,Santiago C.,Mudgal G.,Ordono D.,Enjuanes L.,Casasnovas J.M.
Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies.
PLoS Pathog.
8
0-0
2012