DNPEP_MOUSE
ID DNPEP_MOUSE Reviewed; 473 AA.
AC Q9Z2W0; Q56A00;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0000305};
DE EC=3.4.11.21 {ECO:0000250|UniProtKB:Q9ULA0};
GN Name=Dnpep {ECO:0000312|MGI:MGI:1278328};
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 [MRNA].
RX PubMed=9632644; DOI=10.1074/jbc.273.26.15961;
RA Wilk S., Wilk E., Magnusson R.P.;
RT "Purification, characterization, and cloning of a cytosolic aspartyl
RT aminopeptidase.";
RL J. Biol. Chem. 273:15961-15970(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [5]
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: Aminopeptidase with specificity towards an acidic amino acid
CC at the N-terminus. Likely to play an important role in intracellular
CC protein and peptide metabolism (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: One of the zinc ions is readily exchangeable with
CC other divalent cations such as manganese, which strongly stimulates the
CC enzymatic activity. {ECO:0000250}.
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR EMBL; AF005051; AAD01212.1; -; mRNA.
DR EMBL; AK166276; BAE38675.1; -; mRNA.
DR EMBL; CH466548; EDL00396.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00398.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00400.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00401.1; -; Genomic_DNA.
DR EMBL; BC092232; AAH92232.1; -; mRNA.
DR CCDS; CCDS15070.1; -.
DR RefSeq; NP_001104301.1; NM_001110831.1.
DR RefSeq; NP_058574.3; NM_016878.4.
DR RefSeq; XP_006496468.1; XM_006496405.1.
DR RefSeq; XP_006496469.1; XM_006496406.1.
DR AlphaFoldDB; Q9Z2W0; -.
DR SMR; Q9Z2W0; -.
DR BioGRID; 199263; 6.
DR IntAct; Q9Z2W0; 1.
DR STRING; 10090.ENSMUSP00000109235; -.
DR MEROPS; M18.002; -.
DR iPTMnet; Q9Z2W0; -.
DR PhosphoSitePlus; Q9Z2W0; -.
DR SwissPalm; Q9Z2W0; -.
DR REPRODUCTION-2DPAGE; Q9Z2W0; -.
DR EPD; Q9Z2W0; -.
DR jPOST; Q9Z2W0; -.
DR MaxQB; Q9Z2W0; -.
DR PaxDb; Q9Z2W0; -.
DR PRIDE; Q9Z2W0; -.
DR ProteomicsDB; 277586; -.
DR Antibodypedia; 34327; 207 antibodies from 28 providers.
DR DNASU; 13437; -.
DR Ensembl; ENSMUST00000066668; ENSMUSP00000070821; ENSMUSG00000026209.
DR Ensembl; ENSMUST00000113605; ENSMUSP00000109235; ENSMUSG00000026209.
DR Ensembl; ENSMUST00000187836; ENSMUSP00000139739; ENSMUSG00000026209.
DR GeneID; 13437; -.
DR KEGG; mmu:13437; -.
DR UCSC; uc007bot.2; mouse.
DR CTD; 23549; -.
DR MGI; MGI:1278328; Dnpep.
DR VEuPathDB; HostDB:ENSMUSG00000026209; -.
DR eggNOG; KOG2596; Eukaryota.
DR GeneTree; ENSGT00390000003164; -.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; Q9Z2W0; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 769270at2759; -.
DR TreeFam; TF300487; -.
DR BRENDA; 3.4.11.21; 3474.
DR BioGRID-ORCS; 13437; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dnpep; mouse.
DR PRO; PR:Q9Z2W0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9Z2W0; protein.
DR Bgee; ENSMUSG00000026209; Expressed in intestinal villus and 244 other tissues.
DR ExpressionAtlas; Q9Z2W0; baseline and differential.
DR Genevisible; Q9Z2W0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Zinc.
FT CHAIN 1..473
FT /note="Aspartyl aminopeptidase"
FT /id="PRO_0000173452"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT CONFLICT 61
FT /note="K -> N (in Ref. 1; AAD01212)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="L -> S (in Ref. 1; AAD01212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 52207 MW; 0350CC27C4A5AC8E CRC64;
MAMNGRARKE AIQATARELL KFVNRSPSPF HVVAECRSRL LQAGFRELKE TEGWDIVPEN
KYFLTRNSSS IIAFAVGGQY VPGNGFSLIG AHTDSPCLRV KRKSRRSQVG YHQVGVETYG
GGIWSTWFDR DLTLAGRVII KCPTSGRLEQ RLVHIERPIL RIPHLAIHLQ RNINENFGPN
TEIHLVPILA TAVQEELEKG TPEPGPLGAT DERHHSVLMS LLCTHLGLSP DSIMEMELCL
ADTQPAVLGG AYEEFIFAPR LDNLHSCFCA LQALIDSCAS PASLARDPHV RMVTLYDNEE
VGSESAQGAQ SLLTELILRR ISASPQRLTA FEEAIPKSFM ISADMAHAVH PNYSDKHEEN
HRPLFHKGPV IKVNSKQRYA SNAVSESMIR EVAGQVGVPL QDLMVRNDSP CGTTIGPILA
SRLGLRVLDL GSPQLAMHSI RETACTTGVL QTLTLFKGFF ELFPSVSRNL LVD
