ID AMPB_MOUSE Reviewed; 650 AA. AC Q8VCT3; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 21-AUG-2007, entry version 49. DE Aminopeptidase B (EC 3.4.11.6) (Ap-B) (Arginyl aminopeptidase) DE (Arginine aminopeptidase) (Cytosol aminopeptidase IV). GN Name=Rnpep; 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 TISSUE=Kidney; 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: Exopeptidase which selectively removes arginine and/or CC lysine residues from the N-terminus of several peptide substrates CC including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(- CC 1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) CC into leukotriene B4 (LTB-4) (By similarity). CC -!- CATALYTIC ACTIVITY: Release of N-terminal Arg and Lys from CC oligopeptides when P1' is not Pro. Also acts on arylamides of Arg CC and Lys. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the peptidase M1 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC019200; AAH19200.1; -; mRNA. DR UniGene; Mm.291048; -. DR HSSP; P09960; 1HS6. DR MEROPS; M01.014; -. DR Ensembl; ENSMUSG00000041926; Mus musculus. DR KEGG; mmu:215615; -. DR MGI; MGI:2384902; Rnpep. DR ArrayExpress; Q8VCT3; -. DR GermOnline; ENSMUSG00000041926; Mus musculus. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0030601; F:aminopeptidase B activity; ISS:UniProtKB. DR InterPro; IPR015211; Leuk-A4-hydro_C. DR InterPro; IPR015571; Pept_M1_aminopeptidase-B. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR014782; Peptidase_M1_N. DR PANTHER; PTHR11533:SF5; Pept_M1_aminopeptidase-B; 1. DR PANTHER; PTHR11533; Peptidase_M1; 1. DR Pfam; PF09127; Leuk-A4-hydro_C; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 2: Evidence at transcript level; KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease; KW Secreted; Zinc. FT CHAIN 1 650 Aminopeptidase B. FT /FTId=PRO_0000095089. FT ACT_SITE 326 326 By similarity. FT ACT_SITE 414 414 Proton donor (Potential). FT METAL 325 325 Zinc (catalytic) (By similarity). FT METAL 329 329 Zinc (catalytic) (By similarity). FT METAL 348 348 Zinc (catalytic) (By similarity). SQ SEQUENCE 650 AA; 72343 MW; 87CA577E8D20D258 CRC64; MESGGPGNYS GAARRPLHSA QAVDVASASS FRAFEILHLH LDLRAEFGPP GPGPGSRGLS GTATLELRCL LPEGASELRL DSHSCLEVTA ATLRRGQPGD QQAPAEPVPF HTQPFSHYGQ ALCVAFPQPC GAADRFELEL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP CFDTPAVKCT YSALIEVPDG FTAVMSADTW EKRGPNKFFF QMSHPIPSYL IALAIGDLAS AEVGPRSRVW AEPCLIEAAK EEYSGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST ILFGAAYTCL EAATGRALLR QHMNVSGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGYCF VSYLAHLVGD QDQFDKFLKA YVDEFKFQSI LAEDFLEFYL EYFPELKKKG VDSIPGFEFD RWLNTPGWPP YLPDLSPGDS LMKPAEELAE LWVTSEPDMQ AIEAVAISTW KTYQLVYFLD KILQKSPLPP GNVKKLGETY PKISNAQNAE LRLRWGQIIL KNDYQEEFQK VKDFLQSQGK QKYTLPLYHA MMGGSEMART LAKDTFAATA SQLHSNVVNY VQQILAPKDS //