RNPL1_MOUSE
ID RNPL1_MOUSE Reviewed; 720 AA.
AC G5E872;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Aminopeptidase RNPEPL1 {ECO:0000305};
DE EC=3.4.11.- {ECO:0000250|UniProtKB:Q9HAU8};
DE AltName: Full=Methionyl aminopeptidase {ECO:0000305};
DE EC=3.4.11.18 {ECO:0000250|UniProtKB:Q9HAU8};
GN Name=Rnpepl1 {ECO:0000312|MGI:MGI:1914170};
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).
CC -!- FUNCTION: Broad specificity aminopeptidase which preferentially
CC hydrolyzes an N-terminal methionine, citrulline or glutamine.
CC {ECO:0000250|UniProtKB:Q9HAU8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000250|UniProtKB:Q9HAU8};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15144};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144};
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AC119846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15180.2; -.
DR RefSeq; NP_852070.3; NM_181405.4.
DR AlphaFoldDB; G5E872; -.
DR SMR; G5E872; -.
DR STRING; 10090.ENSMUSP00000027487; -.
DR MEROPS; M01.022; -.
DR iPTMnet; G5E872; -.
DR PhosphoSitePlus; G5E872; -.
DR EPD; G5E872; -.
DR PaxDb; G5E872; -.
DR PRIDE; G5E872; -.
DR ProteomicsDB; 300460; -.
DR Antibodypedia; 34524; 85 antibodies from 15 providers.
DR DNASU; 108657; -.
DR Ensembl; ENSMUST00000027487; ENSMUSP00000027487; ENSMUSG00000026269.
DR GeneID; 108657; -.
DR KEGG; mmu:108657; -.
DR UCSC; uc007cbw.2; mouse.
DR CTD; 57140; -.
DR MGI; MGI:1914170; Rnpepl1.
DR VEuPathDB; HostDB:ENSMUSG00000026269; -.
DR eggNOG; KOG1047; Eukaryota.
DR GeneTree; ENSGT00940000160400; -.
DR HOGENOM; CLU_014505_2_1_1; -.
DR InParanoid; G5E872; -.
DR OMA; CAKPFVF; -.
DR OrthoDB; 775595at2759; -.
DR PhylomeDB; G5E872; -.
DR TreeFam; TF300758; -.
DR BioGRID-ORCS; 108657; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rnpepl1; mouse.
DR PRO; PR:G5E872; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; G5E872; protein.
DR Bgee; ENSMUSG00000026269; Expressed in saccule of membranous labyrinth and 263 other tissues.
DR ExpressionAtlas; G5E872; baseline and differential.
DR GO; GO:0070006; F:metalloaminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
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; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR033525; RNPEPL1.
DR PANTHER; PTHR45726; PTHR45726; 1.
DR PANTHER; PTHR45726:SF2; PTHR45726:SF2; 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.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..720
FT /note="Aminopeptidase RNPEPL1"
FT /id="PRO_0000439278"
FT REGION 671..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15144,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 321..325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT SITE 437
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
SQ SEQUENCE 720 AA; 79535 MW; 1B2CA5A171FCACC0 CRC64;
MAAQCCCRKA PGAEAAPARP PPEPPPALDV ASASSAQLFR LRHLQLGLEL RPEARELAGC
LVLELCALRP APRALVLDAH PALRLHSVSF RRASAVSESP CTFAFPAPGS GPPLPGFADA
PGAESASCPL AFRLDPFTDY GSSLTVTLPP EVQAHQPFQV ILRYTSTDAP AIWWLDPELT
YGNAKPFVFT QGHSVCNRSF FPCFDTPAVK CTYSAVVKAP LGVQVLMSAT QSVYVEEEGL
YHFHMEHPVP AYLVALVAGD LKPADIGPRS RVWAEPCLLP TATSKLSGAV EQWLSAAERL
YGPYMWGRYD IVFLPPSFPI VAMENPCLTF IISSILESDE FLVIDVIHEV AHSWFGNAVT
NATWEEMWLS EGLATYAQRR ITTETYGAAF TCLETAFRLD ALHRQMRLLG EDSPVSKLQV
KLEPGVNPSH LMNLFTYEKG YCFVYYLSQL CGGPQRFDDF LRAYVEKYKF TSVVAQDLLD
SFLSFFPELK EQSVDCRAGL EFERWLNATG PPLAEPDLSQ GSSLTRPVEA LFQLWTAEPL
EQAAASASAI DISKWRTFQT ALFLDRLLDG SPLPQEVVMS LSKCYSSLLD SMNAEIRIRW
LQIVVRNDYY PDLHRVRRFL ESQMSRMYTI PLYEDLCTGA LKSFALEVFY QTQGRLHPNL
RRTIQQILSQ GLGPSAEPST EPSTDLGGAE ADTNPDSPAL LLGDEAPSST ISLRDVNVSA
