ID AMPB_MOUSE Reviewed; 650 AA. AC Q8VCT3; Q3TX27; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 05-DEC-2018, entry version 142. DE RecName: Full=Aminopeptidase B; DE Short=AP-B; DE EC=3.4.11.6; DE AltName: Full=Arginine aminopeptidase; DE AltName: Full=Arginyl aminopeptidase; DE AltName: Full=Cytosol aminopeptidase IV; GN Name=Rnpep; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] 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). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). 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). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal Arg and Lys from oligopeptides when CC P1' is not Pro. Also acts on arylamides of Arg and Lys.; CC EC=3.4.11.6; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}. 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; AK159195; BAE34890.1; -; mRNA. DR EMBL; AK159445; BAE35089.1; -; mRNA. DR EMBL; AK159625; BAE35239.1; -; mRNA. DR EMBL; CH466520; EDL39584.1; -; Genomic_DNA. DR EMBL; BC019200; AAH19200.1; -; mRNA. DR CCDS; CCDS15317.1; -. DR RefSeq; NP_001153096.1; NM_001159624.1. DR RefSeq; NP_663392.2; NM_145417.3. DR UniGene; Mm.291048; -. DR ProteinModelPortal; Q8VCT3; -. DR SMR; Q8VCT3; -. DR BioGrid; 229640; 2. DR IntAct; Q8VCT3; 2. DR MINT; Q8VCT3; -. DR STRING; 10090.ENSMUSP00000076564; -. DR BindingDB; Q8VCT3; -. DR ChEMBL; CHEMBL2836; -. DR MEROPS; M01.014; -. DR iPTMnet; Q8VCT3; -. DR PhosphoSitePlus; Q8VCT3; -. DR SwissPalm; Q8VCT3; -. DR EPD; Q8VCT3; -. DR MaxQB; Q8VCT3; -. DR PaxDb; Q8VCT3; -. DR PeptideAtlas; Q8VCT3; -. DR PRIDE; Q8VCT3; -. DR Ensembl; ENSMUST00000077340; ENSMUSP00000076564; ENSMUSG00000041926. DR GeneID; 215615; -. DR KEGG; mmu:215615; -. DR UCSC; uc007csy.2; mouse. DR CTD; 6051; -. DR MGI; MGI:2384902; Rnpep. DR eggNOG; KOG1047; Eukaryota. DR eggNOG; COG0308; LUCA. DR GeneTree; ENSGT00940000160431; -. DR HOGENOM; HOG000293296; -. DR HOVERGEN; HBG001274; -. DR InParanoid; Q8VCT3; -. DR KO; K01260; -. DR OMA; FEMEKPI; -. DR OrthoDB; EOG091G02UX; -. DR TreeFam; TF300758; -. DR ChiTaRS; Rnpep; mouse. DR PRO; PR:Q8VCT3; -. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000041926; Expressed in 285 organ(s), highest expression level in bone marrow macrophage. DR CleanEx; MM_RNPEP; -. DR ExpressionAtlas; Q8VCT3; baseline and differential. DR Genevisible; Q8VCT3; MM. DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0043005; C:neuron projection; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0030141; C:secretory granule; ISO:MGI. DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB. DR GO; GO:0050897; F:cobalt ion binding; ISO:MGI. DR GO; GO:0005507; F:copper ion binding; ISO:MGI. DR GO; GO:0070006; F:metalloaminopeptidase activity; ISO:MGI. DR GO; GO:0042277; F:peptide binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISO:MGI. DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI. DR GO; GO:0006508; P:proteolysis; ISO:MGI. DR CDD; cd09599; M1_LTA4H; 1. DR Gene3D; 1.10.390.10; -; 1. DR Gene3D; 1.25.40.320; -; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf. DR InterPro; IPR034015; M1_LTA4H. DR InterPro; IPR015571; Pept_M1_aminopeptidase-B. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR015211; Peptidase_M1_C. DR InterPro; IPR014782; Peptidase_M1_N. DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf. DR PANTHER; PTHR11533; PTHR11533; 1. DR PANTHER; PTHR11533:SF153; PTHR11533:SF153; 1. DR Pfam; PF09127; Leuk-A4-hydro_C; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR SMART; SM01263; Leuk-A4-hydro_C; 1. DR SUPFAM; SSF48371; SSF48371; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW Acetylation; Aminopeptidase; Complete proteome; Hydrolase; KW Metal-binding; Metalloprotease; Protease; Reference proteome; KW Secreted; Zinc. FT CHAIN 1 650 Aminopeptidase B. FT /FTId=PRO_0000095089. FT REGION 298 302 Substrate binding. {ECO:0000250}. FT ACT_SITE 326 326 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 325 325 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 329 329 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 348 348 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT SITE 414 414 Transition state stabilizer. FT {ECO:0000250}. FT MOD_RES 446 446 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9H4A4}. FT CONFLICT 11 11 A -> G (in Ref. 3; AAH19200). FT {ECO:0000305}. FT CONFLICT 127 127 R -> P (in Ref. 3; AAH19200). FT {ECO:0000305}. SQ SEQUENCE 650 AA; 72416 MW; 95138D47E57E3C61 CRC64; MESGGPGNYS AAARRPLHSA QAVDVASASS FRAFEILHLH LDLRAEFGPP GPGPGSRGLS GTATLELRCL LPEGASELRL DSHSCLEVTA ATLRRGQPGD QQAPAEPVPF HTQPFSHYGQ ALCVAFRQPC 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 //