XPP1_RAT
ID XPP1_RAT Reviewed; 623 AA.
AC O54975;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
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|RGD:621274}; Synonyms=App;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAB95331.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-19; 85-89; 96-105;
RP 107-112; 372-385; 422-442 AND 599-606, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000312|EMBL:AAB95331.1};
RX PubMed=10095056; DOI=10.1016/s0167-4781(99)00005-6;
RA Czirjak G., Burkhart W.A., Moyer M.B., Antal J., Shears S.B., Enyedi P.;
RT "Cloning and functional expression of the cytoplasmic form of rat
RT aminopeptidase P.";
RL Biochim. Biophys. Acta 1444:326-336(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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:0000269|PubMed:10095056};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by inositol hexakisphosphate.
CC {ECO:0000269|PubMed:10095056}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NQW7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10095056}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including liver,
CC adrenal decapsular tissue, adrenal capsular tissue, corpus luteum,
CC testis, submandibular gland, thymus, brain, cerebellum and heart.
CC Highest levels in testis. {ECO:0000269|PubMed:10095056}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000255}.
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DR EMBL; AF038591; AAB95331.1; -; mRNA.
DR EMBL; BC061758; AAH61758.1; -; mRNA.
DR RefSeq; NP_571988.1; NM_131913.1.
DR AlphaFoldDB; O54975; -.
DR SMR; O54975; -.
DR BioGRID; 250985; 2.
DR STRING; 10116.ENSRNOP00000031325; -.
DR MEROPS; M24.009; -.
DR iPTMnet; O54975; -.
DR PhosphoSitePlus; O54975; -.
DR jPOST; O54975; -.
DR PaxDb; O54975; -.
DR PeptideAtlas; O54975; -.
DR PRIDE; O54975; -.
DR GeneID; 170751; -.
DR KEGG; rno:170751; -.
DR UCSC; RGD:621274; rat.
DR CTD; 7511; -.
DR RGD; 621274; Xpnpep1.
DR VEuPathDB; HostDB:ENSRNOG00000012084; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_2_1; -.
DR InParanoid; O54975; -.
DR OrthoDB; 417805at2759; -.
DR PhylomeDB; O54975; -.
DR PRO; PR:O54975; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012084; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; O54975; baseline and differential.
DR Genevisible; O54975; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0004177; F:aminopeptidase activity; IDA: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:RGD.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA: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; Direct protein sequencing;
KW Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease;
KW Reference proteome.
FT CHAIN 1..623
FT /note="Xaa-Pro aminopeptidase 1"
FT /id="PRO_0000185085"
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; 69658 MW; 42D21C2617F88225 CRC64;
MAPKVTSELL RQLRQAMRNS ECVAEPIQAY IIPSGDAHQS EYIAPCDCRR AFVSGFDGSA
GTAIITEEHA AMWTDGRYFL QAAKQMDNNW TLMKMGLKDT PTQEDWLVSV LPEGSRVGVD
PLIIPTDYWK KMAKVLRSAG HHLVPVKENL VDKIWTDRPE RPCKPLLTLG LDYTGISWKE
KVADLRLKMA ERSIVWFVVT ALDEIAWLFN LRGSDVEHNP VFFSYAIIGL ERIMLFIDGD
RIDAPGVKQH LLLDLGLEAE YKIQVLPYKS ILSELKTLCA DLSPREKVWV SDKASYAVSE
AIPKDHRCCM PYTPICIAKA VKNSAESAGM RRAHIKDAVA LCELFNWLEQ EVPKGGVTEI
SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPIP ETNRTLSLDE VYLIDSGAQY
KDGTTDVTRT MHFGTPTAYE KECFTYVLKG HIAVSAAVFP TGTKGHLLDS FARSALWDSG
LDYLHGTGHG VGSFLNVHEG PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV
LVVPAKTKYN FNNRGSLTFE PLTLVPIQTK MIDVDALTDK ECDWLNSYHQ TCRDVIGKEL
QTQGRQEALE WLLRETEPIS RQH
