ID AMPB_MOUSE STANDARD; PRT; 650 AA. AC Q8VCT3; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Aminopeptidase B (EC 3.4.11.6) (Ap-B) (Arginyl aminopeptidase) DE (Arginine aminopeptidase) (Cytosol aminopeptidase IV). GN RNPEP. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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 a N-terminal Arg and Lys from CC oligopeptides when P1' is not Pro. Also acts on 2-naphthylamides CC of Arg 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 peptidase family M1. 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; -. DR HSSP; P09960; 1HS6. DR MEROPS; M01.014; -. DR MGD; MGI:2384902; Rnpep. DR GO; GO:0005576; C:extracellular; ISS. DR GO; GO:0005794; C:Golgi apparatus; ISS. DR GO; GO:0005886; C:plasma membrane; ISS. DR GO; GO:0030601; F:aminopeptidase B activity; ISS. DR GO; GO:0008270; F:zinc ion binding; ISS. DR GO; GO:0016485; P:protein processing; ISS. DR GO; GO:0006508; P:proteolysis and peptidolysis; ISS. DR InterPro; IPR008938; ARM. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR006025; Pept_M_Zn_BS. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW Aminopeptidase; Hydrolase; Zinc; Metalloprotease. FT METAL 325 325 Zinc (catalytic) (By similarity). FT ACT_SITE 326 326 By similarity. FT METAL 329 329 Zinc (catalytic) (By similarity). FT METAL 348 348 Zinc (catalytic) (By similarity). FT ACT_SITE 414 414 Proton donor (Potential). 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 //