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 29-MAY-2024, entry version 168. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project: RT 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, Pancreas, RC 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 expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Exopeptidase which selectively removes arginine and/or lysine CC residues from the N-terminus of several peptide substrates including CC Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)- CC somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene CC B4 (LTB-4) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1' CC is not Pro. Also acts on arylamides of Arg and Lys.; 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 AlphaFoldDB; Q8VCT3; -. DR SMR; Q8VCT3; -. DR BioGRID; 229640; 3. DR IntAct; Q8VCT3; 1. DR STRING; 10090.ENSMUSP00000076564; -. DR BindingDB; Q8VCT3; -. DR ChEMBL; CHEMBL2836; -. DR DrugCentral; Q8VCT3; -. DR MEROPS; M01.014; -. DR GlyGen; Q8VCT3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8VCT3; -. DR PhosphoSitePlus; Q8VCT3; -. DR SwissPalm; Q8VCT3; -. DR EPD; Q8VCT3; -. DR jPOST; Q8VCT3; -. DR MaxQB; Q8VCT3; -. DR PaxDb; 10090-ENSMUSP00000076564; -. DR PeptideAtlas; Q8VCT3; -. DR ProteomicsDB; 296030; -. DR Pumba; Q8VCT3; -. DR Antibodypedia; 34521; 241 antibodies from 25 providers. DR DNASU; 215615; -. DR Ensembl; ENSMUST00000077340.14; ENSMUSP00000076564.8; ENSMUSG00000041926.16. DR GeneID; 215615; -. DR KEGG; mmu:215615; -. DR UCSC; uc007csy.2; mouse. DR AGR; MGI:2384902; -. DR CTD; 6051; -. DR MGI; MGI:2384902; Rnpep. DR VEuPathDB; HostDB:ENSMUSG00000041926; -. DR eggNOG; KOG1047; Eukaryota. DR GeneTree; ENSGT00940000160431; -. DR HOGENOM; CLU_014505_2_1_1; -. DR InParanoid; Q8VCT3; -. DR OMA; FEMEKPI; -. DR OrthoDB; 443480at2759; -. DR PhylomeDB; Q8VCT3; -. DR TreeFam; TF300758; -. DR BioGRID-ORCS; 215615; 5 hits in 79 CRISPR screens. DR ChiTaRS; Rnpep; mouse. DR PRO; PR:Q8VCT3; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q8VCT3; Protein. DR Bgee; ENSMUSG00000041926; Expressed in granulocyte and 262 other cell types or tissues. DR ExpressionAtlas; Q8VCT3; baseline and differential. 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: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:0016485; P:protein processing; ISO:MGI. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR CDD; cd09599; M1_LTA4H; 1. DR Gene3D; 3.30.2010.30; -; 1. DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1. DR Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1. DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1. DR InterPro; IPR045357; Aminopeptidase_N-like_N. DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf. DR InterPro; IPR034015; M1_LTA4H. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR015211; Peptidase_M1_C. DR InterPro; IPR014782; Peptidase_M1_dom. DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf. DR PANTHER; PTHR45726:SF1; AMINOPEPTIDASE B; 1. DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1. DR Pfam; PF09127; Leuk-A4-hydro_C; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR Pfam; PF17900; Peptidase_M1_N; 1. DR PRINTS; PR00756; ALADIPTASE. DR SMART; SM01263; Leuk-A4-hydro_C; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW Acetylation; Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Secreted; Zinc. FT CHAIN 1..650 FT /note="Aminopeptidase B" FT /id="PRO_0000095089" FT ACT_SITE 326 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 298..302 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 325 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 329 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT SITE 414 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT MOD_RES 446 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9H4A4" FT CONFLICT 11 FT /note="A -> G (in Ref. 3; AAH19200)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="R -> P (in Ref. 3; AAH19200)" FT /evidence="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 //