XPP3_PONAB
ID XPP3_PONAB Reviewed; 507 AA.
AC Q5R9W8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Xaa-Pro aminopeptidase 3 {ECO:0000250|UniProtKB:Q9NQH7};
DE Short=X-Pro aminopeptidase 3;
DE EC=3.4.11.9 {ECO:0000250|UniProtKB:Q9NQH7};
DE AltName: Full=Aminopeptidase P3;
DE Short=APP3;
DE Flags: Precursor;
GN Name=XPNPEP3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity
CC towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B-
CC mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a
CC function as an adapter protein for TNFRSF1B; the effect is independent
CC of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced
CC via TNF-TNFRSF1B signaling. {ECO:0000250|UniProtKB:Q9NQH7}.
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:Q9NQH7};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NQH7};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9NQH7};
CC -!- SUBUNIT: Homodimer. Interacts with TNFRSF1B/TNFR2 (activated) and
CC TRAF2. {ECO:0000250|UniProtKB:Q9NQH7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NQH7}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9NQH7}. Note=Mainly mitochondrial.
CC Translocates to the cytoplasm following TNFRSF1B activation.
CC {ECO:0000250|UniProtKB:Q9NQH7}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; CR859263; CAH91442.1; -; mRNA.
DR RefSeq; NP_001127419.1; NM_001133947.1.
DR AlphaFoldDB; Q5R9W8; -.
DR SMR; Q5R9W8; -.
DR STRING; 9601.ENSPPYP00000013233; -.
DR MEROPS; M24.026; -.
DR PRIDE; Q5R9W8; -.
DR GeneID; 100174489; -.
DR KEGG; pon:100174489; -.
DR CTD; 63929; -.
DR eggNOG; KOG2414; Eukaryota.
DR InParanoid; Q5R9W8; -.
DR OrthoDB; 352329at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Metalloprotease; Mitochondrion; Protease; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..507
FT /note="Xaa-Pro aminopeptidase 3"
FT /id="PRO_0000255655"
FT REGION 54..79
FT /note="Interaction with TNFRSF1B"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 431
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 451
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
SQ SEQUENCE 507 AA; 57032 MW; A51A46CCFDFDED1B CRC64;
MPWLLSAPKL VPAVANVRGL SGCMLCSQRR YSLQPVPERR IPNRYLGQPS PFTHPHLLRP
GEVTPGLSQV EYALRRHKLM SLIQKEAQGQ SGTDQTVVVL SNPTYYMSND IPYTFHQDNN
FLYLCGFQEP DSILVLQSLP GKQLPSHKAI LFVPRRDPSR ELWDGPRSGT DGAIALTGVD
EAYTLEEFQH LLPKMKAETN MVWYDWMRPS HAQLHSDYMQ PLTEAKAKSK NKVRGVQQLI
QRLRLIKSPA EIERMQIAGK LTSQAFIETM FASKAPVEEG FLYAKFEFEC RARGADILAY
PPVVAGGNRS NTLHYVKNNQ LIKDGEMVLL DGGCESSCYV SDITRTWPVN GRFTAPQAEL
YEAILEIQRD CLALCFPGTS LENIYSMMLT LIGQKLKDLG IMKNIKENNA FKAARKYCPH
HVGHYLGMDV HDTPDMPRSL PLQPGMVITI EPGIYIPEDD KDAPEKFRGL GVRIEDDVVV
TQDSPLILSA DCPKEMNDIE QICSRAS
