PEPD_RAT
ID PEPD_RAT Reviewed; 492 AA.
AC Q5I0D7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Xaa-Pro dipeptidase;
DE Short=X-Pro dipeptidase;
DE EC=3.4.13.9;
DE AltName: Full=Imidodipeptidase;
DE AltName: Full=Peptidase D;
DE AltName: Full=Proline dipeptidase;
DE Short=Prolidase;
GN Name=Pepd;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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: Splits dipeptides with a prolyl or hydroxyprolyl residue in
CC the C-terminal position. Plays an important role in collagen metabolism
CC because of the high level of iminoacids in collagen (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-
CC hydroxyproline analogs. No action on Pro-|-Pro.; EC=3.4.13.9;
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 -!- SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type
CC prolidase subfamily. {ECO:0000305}.
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DR EMBL; BC088440; AAH88440.1; -; mRNA.
DR RefSeq; NP_001009641.1; NM_001009641.1.
DR AlphaFoldDB; Q5I0D7; -.
DR SMR; Q5I0D7; -.
DR STRING; 10116.ENSRNOP00000028701; -.
DR MEROPS; M24.007; -.
DR iPTMnet; Q5I0D7; -.
DR PhosphoSitePlus; Q5I0D7; -.
DR jPOST; Q5I0D7; -.
DR PaxDb; Q5I0D7; -.
DR PRIDE; Q5I0D7; -.
DR Ensembl; ENSRNOT00000077404; ENSRNOP00000095277; ENSRNOG00000052945.
DR GeneID; 292808; -.
DR KEGG; rno:292808; -.
DR UCSC; RGD:1594571; rat.
DR CTD; 5184; -.
DR RGD; 1594571; Pepd.
DR eggNOG; KOG2737; Eukaryota.
DR GeneTree; ENSGT00940000153657; -.
DR InParanoid; Q5I0D7; -.
DR OrthoDB; 352329at2759; -.
DR PhylomeDB; Q5I0D7; -.
DR PRO; PR:Q5I0D7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
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 InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
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.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Collagen degradation; Dipeptidase; Hydrolase; Manganese;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..492
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000328065"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P12955, ECO:0000255"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12955"
SQ SEQUENCE 492 AA; 54751 MW; 97359DB0E3CADB15 CRC64;
MASTVRPSFS LGNETLKVPL ALFALNRQRL CERLRKNGAV QAGSAVVLQG GEEMQRYCTD
TSIIFRQESF FHWAFGVIES GCYGVIDVDT GKSTLFVPRL PASYATWMGK IHSKEHFKEK
YAVDDVQYAD EIASVLTSRN PSVLLTLRGV NTDSGNVCRE ASFEGISKFT VNNTILHPEI
VECRVFKTDM ELEVLRYTNR ISSEAHREVM KAVKVGMKEY EMESLFQHYC YSKGGMRHTS
YTCICCSGEN AAVLHYGHAG APNDRTIKDG DICLFDMGGE YYCFASDITC SFPANGKFTD
DQKAIYEAVL RSCRTVMSTM KPGVWWPDMH RLADRIHLEE LTRIGLLSGS VDAMLQVHLG
AVFMPHGLGH FLGLDVHDVG GYPEGVERID EPGLRSLRTA RHLEPGMVLT VEPGIYFIDH
LLDQALADPA QACFFNQEVL QRFRNFGGVR IEEDVVVTDS GMELLTCVPR TVEEIEACMA
GCDKALAPSG PK
