PEPD_MOUSE
ID PEPD_MOUSE Reviewed; 493 AA.
AC Q11136; P97735; Q3TH86; Q9CWK4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
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 4;
DE AltName: Full=Peptidase D;
DE AltName: Full=Proline dipeptidase;
DE Short=Prolidase;
GN Name=Pepd; Synonyms=Pep4;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RA Ledoux P., Savoie P., Scriver C., Hechtman P.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8765744; DOI=10.1016/0167-4781(96)00084-x;
RA Ishii T., Tsujino S., Matsunobu S., Endo F., Sato K., Sakuragawa N.;
RT "Cloning of mouse prolidase cDNA: predominant expression of prolidase mRNA
RT in kidney.";
RL Biochim. Biophys. Acta 1308:15-16(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Embryonic stem cell, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
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: 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.
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.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type
CC prolidase subfamily. {ECO:0000305}.
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DR EMBL; U51014; AAA92975.1; -; mRNA.
DR EMBL; D82983; BAB11685.1; -; mRNA.
DR EMBL; AK010581; BAB27043.1; -; mRNA.
DR EMBL; AK145843; BAE26691.1; -; mRNA.
DR EMBL; AK168384; BAE40312.1; -; mRNA.
DR EMBL; BC086644; AAH86644.1; -; mRNA.
DR CCDS; CCDS21143.1; -.
DR RefSeq; NP_032846.2; NM_008820.2.
DR AlphaFoldDB; Q11136; -.
DR SMR; Q11136; -.
DR BioGRID; 202110; 18.
DR STRING; 10090.ENSMUSP00000075683; -.
DR MEROPS; M24.007; -.
DR iPTMnet; Q11136; -.
DR PhosphoSitePlus; Q11136; -.
DR SwissPalm; Q11136; -.
DR EPD; Q11136; -.
DR jPOST; Q11136; -.
DR MaxQB; Q11136; -.
DR PaxDb; Q11136; -.
DR PRIDE; Q11136; -.
DR ProteomicsDB; 288095; -.
DR Antibodypedia; 2792; 256 antibodies from 28 providers.
DR DNASU; 18624; -.
DR Ensembl; ENSMUST00000075068; ENSMUSP00000075683; ENSMUSG00000063931.
DR GeneID; 18624; -.
DR KEGG; mmu:18624; -.
DR UCSC; uc009gjj.2; mouse.
DR CTD; 5184; -.
DR MGI; MGI:97542; Pepd.
DR VEuPathDB; HostDB:ENSMUSG00000063931; -.
DR eggNOG; KOG2737; Eukaryota.
DR GeneTree; ENSGT00940000153657; -.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; Q11136; -.
DR OMA; DQKFIYN; -.
DR OrthoDB; 352329at2759; -.
DR PhylomeDB; Q11136; -.
DR TreeFam; TF313396; -.
DR BioGRID-ORCS; 18624; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Pepd; mouse.
DR PRO; PR:Q11136; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q11136; protein.
DR Bgee; ENSMUSG00000063931; Expressed in small intestine Peyer's patch and 266 other tissues.
DR ExpressionAtlas; Q11136; baseline and differential.
DR Genevisible; Q11136; MM.
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; IDA:MGI.
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 1: Evidence at protein 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..493
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000185088"
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"
FT CONFLICT 22
FT /note="L -> I (in Ref. 1; AAA92975)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="G -> R (in Ref. 1; AAA92975)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="G -> C (in Ref. 2; BAB11685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55029 MW; 5CC6BC66665BEACA CRC64;
MASTVRPSFS LGNETLKVPL ALFALNRQRL CERLRKNGAV QAASAVVLQG GEEMQRYCTD
TSIIFRQESF FHWAFGVVES GCYGVIDVDT GKSTLFVPRL PDSYATWMGK IHSKEYFKEK
YAVDDVQYTD EIASVLTSRN PSVLLTLRGV NTDSGSVCRE ASFEGISKFN VNNTILHPEI
VECRVFKTDM ELEVLRYTNR ISSEAHREVM KAVKVGMKEY EMESLFQHYC YSRGGMRHTS
YTCICCSGEN AAVLHYGHAG APNDRTIKDG DICLFDMGGE YYCFASDITC SFPANGKFTE
DQKAIYEAVL RSCRTVMSTM KPGVWWPDMH RLADRIHLEE LARIGLLSGS VDAMLQVHLG
AVFMPHGLGH FLGLDVHDVG GYPEGVERID EPGLRSLRTA RHLEPGMVLT VEPGIYFIDH
LLDQALADPA QACFFNQEVL QRFRNFGGVR IEEDVVVTDS GMELLTCVPR TVEEIEACMA
GCDKASVPFS GQK
