AMPB_MOUSE
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 03-AUG-2022, entry version 159.
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}.
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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 iPTMnet; Q8VCT3; -.
DR PhosphoSitePlus; Q8VCT3; -.
DR SwissPalm; Q8VCT3; -.
DR EPD; Q8VCT3; -.
DR jPOST; Q8VCT3; -.
DR MaxQB; Q8VCT3; -.
DR PaxDb; Q8VCT3; -.
DR PeptideAtlas; Q8VCT3; -.
DR PRIDE; Q8VCT3; -.
DR ProteomicsDB; 296030; -.
DR Antibodypedia; 34521; 216 antibodies from 25 providers.
DR DNASU; 215615; -.
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 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; 775595at2759; -.
DR PhylomeDB; Q8VCT3; -.
DR TreeFam; TF300758; -.
DR BioGRID-ORCS; 215615; 5 hits in 74 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 258 other tissues.
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:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 1.
DR Gene3D; 2.60.40.1730; -; 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; IPR015571; Pept_M1_aminopeptidase-B.
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; PTHR45726; 1.
DR PANTHER; PTHR45726:SF1; PTHR45726:SF1; 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; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 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
