PEPL1_MOUSE
ID PEPL1_MOUSE Reviewed; 524 AA.
AC Q6NSR8; A2ACM6; Q66JY0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable aminopeptidase NPEPL1;
DE EC=3.4.11.-;
DE AltName: Full=Aminopeptidase-like 1;
GN Name=Npepl1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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: Probably catalyzes the removal of unsubstituted N-terminal
CC amino acids from various peptides. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; AL669896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069933; AAH69933.1; -; mRNA.
DR EMBL; BC080707; AAH80707.1; -; mRNA.
DR CCDS; CCDS17148.1; -.
DR RefSeq; NP_998898.1; NM_213733.2.
DR AlphaFoldDB; Q6NSR8; -.
DR SMR; Q6NSR8; -.
DR STRING; 10090.ENSMUSP00000042808; -.
DR MEROPS; M17.006; -.
DR iPTMnet; Q6NSR8; -.
DR PhosphoSitePlus; Q6NSR8; -.
DR SwissPalm; Q6NSR8; -.
DR EPD; Q6NSR8; -.
DR jPOST; Q6NSR8; -.
DR MaxQB; Q6NSR8; -.
DR PaxDb; Q6NSR8; -.
DR PRIDE; Q6NSR8; -.
DR ProteomicsDB; 288096; -.
DR Antibodypedia; 29150; 81 antibodies from 22 providers.
DR DNASU; 228961; -.
DR Ensembl; ENSMUST00000044415; ENSMUSP00000042808; ENSMUSG00000039263.
DR GeneID; 228961; -.
DR KEGG; mmu:228961; -.
DR UCSC; uc008oeo.2; mouse.
DR CTD; 79716; -.
DR MGI; MGI:2448523; Npepl1.
DR VEuPathDB; HostDB:ENSMUSG00000039263; -.
DR eggNOG; KOG2597; Eukaryota.
DR GeneTree; ENSGT00530000063255; -.
DR HOGENOM; CLU_013734_3_1_1; -.
DR InParanoid; Q6NSR8; -.
DR OMA; MVCEQSD; -.
DR OrthoDB; 562530at2759; -.
DR PhylomeDB; Q6NSR8; -.
DR TreeFam; TF314954; -.
DR BioGRID-ORCS; 228961; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Npepl1; mouse.
DR PRO; PR:Q6NSR8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6NSR8; protein.
DR Bgee; ENSMUSG00000039263; Expressed in internal carotid artery and 231 other tissues.
DR ExpressionAtlas; Q6NSR8; baseline and differential.
DR Genevisible; Q6NSR8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR041417; NPEPL1_N.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF18295; Pdase_M17_N2; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..524
FT /note="Probable aminopeptidase NPEPL1"
FT /id="PRO_0000165829"
FT ACT_SITE 272
FT /evidence="ECO:0000255"
FT ACT_SITE 346
FT /evidence="ECO:0000255"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 524 AA; 55940 MW; 4B45CD164D1F65CC CRC64;
MASVGLQFQA SAGDADPQSR PLLLLGQLQH LHRVPWSHVR GKLQPRVTEE LWQAALATLN
PNPTDSCPLY LNCATVAALP SRVSRHNSPS AAHFITRLVR TCLPPGTHRC ILMVCEQTEV
FASACALARA FPLFTHRSGA SRRAEKRTVM VEFFLVGQDN GPVEVSTLQC LTNATEGVRL
AARIVDTPCN EMNTDIFLEE IIQVGKELGI TPTIIRDEQL KTKGFGGIYG VGKAALHPPA
LAILSHTPDG ATQTIAWVGK GIVYDTGGLS IKGKTTMPGM KRDCGGAAAV LGAFRAAIKQ
GFKDNLHAVF CLAENAVGPN ATRPDDIHLL YSGKTVEINN TDAEGRLVLA DGVSYACKDL
GADIIVDMAT LTGAQGIATG KYHAAVLTNS AEWEAACVKA GRKCGDLVHP LVYCPELHFS
EFTSAVADMK NSVADRDNSP SSCAGLFIAS HIGFDWPGVW VHLDIAAPVH AGERATGFGV
ALLLALFGRA SEDPLLNLVS PLDCEVDAQE GDNMGRDSKR RRLV
