XPP1_BOVIN
ID XPP1_BOVIN Reviewed; 623 AA.
AC Q1JPJ2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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;
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; BT025361; ABF57317.1; -; mRNA.
DR EMBL; BC133601; AAI33602.1; -; mRNA.
DR RefSeq; NP_001069070.1; NM_001075602.1.
DR RefSeq; XP_005225789.1; XM_005225732.3.
DR RefSeq; XP_005225790.1; XM_005225733.3.
DR RefSeq; XP_005225791.1; XM_005225734.1.
DR RefSeq; XP_010818332.1; XM_010820030.2.
DR RefSeq; XP_015316219.1; XM_015460733.1.
DR AlphaFoldDB; Q1JPJ2; -.
DR SMR; Q1JPJ2; -.
DR STRING; 9913.ENSBTAP00000052124; -.
DR MEROPS; M24.009; -.
DR PaxDb; Q1JPJ2; -.
DR PeptideAtlas; Q1JPJ2; -.
DR PRIDE; Q1JPJ2; -.
DR GeneID; 513156; -.
DR KEGG; bta:513156; -.
DR CTD; 7511; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_2_1; -.
DR InParanoid; Q1JPJ2; -.
DR OrthoDB; 417805at2759; -.
DR TreeFam; TF314183; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000326627"
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"
SQ SEQUENCE 623 AA; 69790 MW; BC9A609A53E9E030 CRC64;
MAPKITSELL RQLRQAMRNL EYVTEPIQAY IIPSGDAHQS EYIAPCDCRR AFVSGFDGSA
GTAIVTEEHA AMWTDGRYFL QAAKQMDSNW TLMKMGLKDT PTQEDWLVSV LPEGSRVGVD
PLIIPTDYWK KMAKVLRSAG HHLIPVKDNL VDKIWTDRPE RPCKPLITLG LDYTGISWKD
KVADLRLKMA ERNVVWFVVT ALDEIAWLFN LRGSDVEHNP VFFSYAILGL ETIMLFIDGD
RIDAPIVKEH LLLDLGLEAE YRIQVLPYKS ILSELKILCA SLSPREKVWV SDKASYAVSE
AIPKDHRCCM PYTPICIAKA VKNSAESEGM RRAHIKDAVA LCELFNWLEK EVPKGGVTEI
SAANKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP ETNRTLSLDE VYLIDSGAQY
KDGTTDVTRT MHFGTPTAYE KECFTYVLKG HIAVSAAVFP TGTKGHLLDS FARSALWDSG
LDYLHGTGHG VGSFLNVHEG PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV
LVVPVKTKYN FNNRGSLTFE PLTLVPIQTK MIDVDSLTDK ECDWLNSYHL TCRDVIGKEL
QKQGRQEALE WLIRETQPIS KQP
