XPP1_MOUSE
ID XPP1_MOUSE Reviewed; 623 AA.
AC Q6P1B1; Q91Y37;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Xaa-Pro aminopeptidase 1;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Cytosolic aminopeptidase P;
DE AltName: Full=Soluble aminopeptidase P;
DE Short=sAmp;
DE AltName: Full=X-Pro aminopeptidase 1;
DE AltName: Full=X-prolyl aminopeptidase 1, soluble;
GN Name=Xpnpep1 {ECO:0000312|EMBL:AAH65174.1, ECO:0000312|MGI:MGI:2180003};
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] {ECO:0000305, ECO:0000312|EMBL:AAK48945.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAK48945.1};
RA Ryan J.W., Bondarev I.;
RT "Mouse soluble (cytosolic) aminopeptidase P.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAH65174.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH65174.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH65174.1};
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=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: Contributes to the degradation of bradykinin. Catalyzes the
CC removal of a penultimate prolyl residue from the N-termini of peptides,
CC such as Arg-Pro-Pro (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9; Evidence={ECO:0000250|UniProtKB:Q9NQW7};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NQW7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000255}.
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DR EMBL; AF363970; AAK48945.1; -; mRNA.
DR EMBL; BC065174; AAH65174.1; -; mRNA.
DR CCDS; CCDS89415.1; -.
DR RefSeq; NP_573479.3; NM_133216.3.
DR RefSeq; XP_011245461.1; XM_011247159.2.
DR RefSeq; XP_011245462.1; XM_011247160.1.
DR AlphaFoldDB; Q6P1B1; -.
DR SMR; Q6P1B1; -.
DR BioGRID; 228414; 14.
DR IntAct; Q6P1B1; 1.
DR MINT; Q6P1B1; -.
DR STRING; 10090.ENSMUSP00000138250; -.
DR MEROPS; M24.009; -.
DR iPTMnet; Q6P1B1; -.
DR PhosphoSitePlus; Q6P1B1; -.
DR SwissPalm; Q6P1B1; -.
DR EPD; Q6P1B1; -.
DR jPOST; Q6P1B1; -.
DR MaxQB; Q6P1B1; -.
DR PaxDb; Q6P1B1; -.
DR PRIDE; Q6P1B1; -.
DR ProteomicsDB; 300010; -.
DR Antibodypedia; 31645; 198 antibodies from 34 providers.
DR DNASU; 170750; -.
DR Ensembl; ENSMUST00000236058; ENSMUSP00000157689; ENSMUSG00000025027.
DR Ensembl; ENSMUST00000237294; ENSMUSP00000158390; ENSMUSG00000025027.
DR GeneID; 170750; -.
DR KEGG; mmu:170750; -.
DR UCSC; uc008hwf.2; mouse.
DR CTD; 7511; -.
DR MGI; MGI:2180003; Xpnpep1.
DR VEuPathDB; HostDB:ENSMUSG00000025027; -.
DR eggNOG; KOG2413; Eukaryota.
DR GeneTree; ENSGT00940000157716; -.
DR InParanoid; Q6P1B1; -.
DR OMA; YRPGKWG; -.
DR OrthoDB; 417805at2759; -.
DR PhylomeDB; Q6P1B1; -.
DR TreeFam; TF314183; -.
DR BioGRID-ORCS; 170750; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Xpnpep1; mouse.
DR PRO; PR:Q6P1B1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6P1B1; protein.
DR Bgee; ENSMUSG00000025027; Expressed in gastrula and 260 other tissues.
DR ExpressionAtlas; Q6P1B1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.40.350.10; -; 2.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Metalloprotease; Protease; Reference proteome.
FT CHAIN 1..623
FT /note="Xaa-Pro aminopeptidase 1"
FT /id="PRO_0000185084"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 489
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 498
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 523
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 523
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 537
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 537
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT CONFLICT 347
FT /note="W -> R (in Ref. 1; AAK48945)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="A -> T (in Ref. 1; AAK48945)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="P -> A (in Ref. 1; AAK48945)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="N -> T (in Ref. 1; AAK48945)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="S -> T (in Ref. 1; AAK48945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 69591 MW; 3DACC2C5EDA74B9A CRC64;
MAPKVTSELL RQLRQAMRNS EYVAEPIQAY IIPSGDAHQS EYIAPCDCRR AFVSGFDGSA
GTAIITEEHA AMWTDGRYFL QAAKQMDNNW TLMKMGLKDT PTQEDWLVSV LPEGSRVGVD
PLIIPTDYWK KMAKVLRSAG HHLVPVKENL VDKIWTDRPE RPCKPLLTLG LDYTGISWKE
KVADLRLKMA ERSIAWFVVT ALDEIAWLFN LRGSDVEHNP VFFSYAIVGL ETIMLFIDGD
RVDAPGVKQH LLLDLGLEAE YRIQVLPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE
AIPKDHRCCM PYTPICIAKA VKNSAESDGM RRAHIKDAVA LCELFNWLEQ EVPKGGVTEI
SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP ETNRTLSLDE VYLIDSGAQY
KDGTTDVTRT MHFGTPTAYE KECFTYVLKG HIAVSAAVFP TGTKGHLLDS FARSALWDSG
LDYLHGTGHG VGSFLNVHEG PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV
LVVPAKTKYN FNNRGSLTFE PLTLVPIQTK MIDVNALTDK ECDWLNSYHQ TCRDVVGKEL
QSQGRQEALE WLIRETEPVS RQH
