PEPD_HUMAN
ID PEPD_HUMAN Reviewed; 493 AA.
AC P12955; A8K3Z1; A8K416; A8K696; A8MX47; B4DDB7; B4DGJ1; E9PCE8; Q8TBN9;
AC Q9BT75;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 232.
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; Synonyms=PRD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver, and Placenta;
RX PubMed=2925654; DOI=10.1016/s0021-9258(18)83768-1;
RA Endo F., Tanoue A., Nakai H., Hata A., Indo Y., Titani K., Matsuda I.;
RT "Primary structure and gene localization of human prolidase.";
RL J. Biol. Chem. 264:4476-4481(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP PHE-435.
RC TISSUE=Brain, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-435.
RC TISSUE=Kidney, Skin, and Uterus;
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 [6]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, AND
RP COFACTOR.
RG Protein structure factory (PSF);
RT "Crystal structure of human prolidase: the molecular basis of PD disease.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [12]
RP VARIANT PD ASN-276.
RX PubMed=2365824; DOI=10.1172/jci114708;
RA Tanoue A., Endo F., Kitano A., Matsuda I.;
RT "A single nucleotide change in the prolidase gene in fibroblasts from two
RT patients with polypeptide positive prolidase deficiency. Expression of the
RT mutant enzyme in NIH 3T3 cells.";
RL J. Clin. Invest. 86:351-355(1990).
RN [13]
RP VARIANTS PD ARG-448 AND GLU-452 DEL.
RX PubMed=8198124;
RA Ledoux P., Scriver C.R., Hechtman P.;
RT "Four novel PEPD alleles causing prolidase deficiency.";
RL Am. J. Hum. Genet. 54:1014-1021(1994).
RN [14]
RP VARIANTS PD GLN-184; ASP-278; ARG-448 AND GLU-452 DEL.
RX PubMed=8900231;
RA Ledoux P., Scriver C.R., Hechtman P.;
RT "Expression and molecular analysis of mutations in prolidase deficiency.";
RL Am. J. Hum. Genet. 59:1035-1039(1996).
RN [15]
RP VARIANT PD ARG-448.
RX PubMed=12384772; DOI=10.1007/s00439-002-0792-5;
RA Forlino A., Lupi A., Vaghi P., Icaro Cornaglia A., Calligaro A.,
RA Campari E., Cetta G.;
RT "Mutation analysis of five new patients affected by prolidase deficiency:
RT the lack of enzyme activity causes necrosis-like cell death in cultured
RT fibroblasts.";
RL Hum. Genet. 111:314-322(2002).
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 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:0000269|Ref.11};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|Ref.11};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC P12955; P54253: ATXN1; NbExp=4; IntAct=EBI-948765, EBI-930964;
CC P12955; P54274: TERF1; NbExp=2; IntAct=EBI-948765, EBI-710997;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P12955-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12955-2; Sequence=VSP_042629;
CC Name=3;
CC IsoId=P12955-3; Sequence=VSP_045370;
CC -!- MASS SPECTROMETRY: Mass=54251.73; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- DISEASE: Prolidase deficiency (PD) [MIM:170100]: A multisystem disorder
CC associated with massive iminodipeptiduria and lack of or reduced
CC prolidase activity in erythrocytes, leukocytes, or cultured
CC fibroblasts. Clinical features include skin ulcers, developmental
CC delay, recurrent infections, and a characteristic facies.
CC {ECO:0000269|PubMed:12384772, ECO:0000269|PubMed:2365824,
CC ECO:0000269|PubMed:8198124, ECO:0000269|PubMed:8900231}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type
CC prolidase subfamily. {ECO:0000305}.
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DR EMBL; J04605; AAA60064.1; -; mRNA.
DR EMBL; BT006692; AAP35338.1; -; mRNA.
DR EMBL; AK290756; BAF83445.1; -; mRNA.
DR EMBL; AK290781; BAF83470.1; -; mRNA.
DR EMBL; AK291561; BAF84250.1; -; mRNA.
DR EMBL; AK293126; BAG56678.1; -; mRNA.
DR EMBL; AK294619; BAG57802.1; -; mRNA.
DR EMBL; AC008744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004305; AAH04305.1; -; mRNA.
DR EMBL; BC015027; AAH15027.1; -; mRNA.
DR EMBL; BC028295; AAH28295.1; -; mRNA.
DR CCDS; CCDS42544.1; -. [P12955-1]
DR CCDS; CCDS54244.1; -. [P12955-3]
DR CCDS; CCDS54245.1; -. [P12955-2]
DR PIR; A32454; A32454.
DR RefSeq; NP_000276.2; NM_000285.3. [P12955-1]
DR RefSeq; NP_001159528.1; NM_001166056.1. [P12955-2]
DR RefSeq; NP_001159529.1; NM_001166057.1. [P12955-3]
DR PDB; 2IW2; X-ray; 1.82 A; A/B=2-493.
DR PDB; 2OKN; X-ray; 2.45 A; A/B=2-493.
DR PDB; 5M4G; X-ray; 1.48 A; A/B=6-488.
DR PDB; 5M4J; X-ray; 1.55 A; A/B=6-489.
DR PDB; 5M4L; X-ray; 1.49 A; A/B=6-489.
DR PDB; 5M4Q; X-ray; 1.73 A; A/B=6-489.
DR PDB; 5MBY; X-ray; 1.55 A; A/B=6-490.
DR PDB; 5MBZ; X-ray; 1.50 A; A/B=6-489.
DR PDB; 5MC0; X-ray; 1.56 A; A/B=6-486.
DR PDB; 5MC1; X-ray; 1.43 A; A/B=6-490.
DR PDB; 5MC2; X-ray; 1.70 A; A/B=6-488.
DR PDB; 5MC3; X-ray; 1.52 A; A/B=6-489.
DR PDB; 5MC4; X-ray; 1.80 A; A/B=6-487.
DR PDB; 5MC5; X-ray; 1.90 A; A/B=6-484.
DR PDB; 6H2P; X-ray; 1.48 A; A/B=1-493.
DR PDB; 6H2Q; X-ray; 1.78 A; A/B=1-493.
DR PDB; 6QSB; X-ray; 1.99 A; A/B=1-493.
DR PDB; 6QSC; X-ray; 1.57 A; A/B=1-493.
DR PDB; 6SRE; X-ray; 1.39 A; A/B=6-489.
DR PDB; 6SRF; X-ray; 1.85 A; A/B=6-493.
DR PDB; 6SRG; X-ray; 2.56 A; A/B=1-493.
DR PDBsum; 2IW2; -.
DR PDBsum; 2OKN; -.
DR PDBsum; 5M4G; -.
DR PDBsum; 5M4J; -.
DR PDBsum; 5M4L; -.
DR PDBsum; 5M4Q; -.
DR PDBsum; 5MBY; -.
DR PDBsum; 5MBZ; -.
DR PDBsum; 5MC0; -.
DR PDBsum; 5MC1; -.
DR PDBsum; 5MC2; -.
DR PDBsum; 5MC3; -.
DR PDBsum; 5MC4; -.
DR PDBsum; 5MC5; -.
DR PDBsum; 6H2P; -.
DR PDBsum; 6H2Q; -.
DR PDBsum; 6QSB; -.
DR PDBsum; 6QSC; -.
DR PDBsum; 6SRE; -.
DR PDBsum; 6SRF; -.
DR PDBsum; 6SRG; -.
DR AlphaFoldDB; P12955; -.
DR SMR; P12955; -.
DR BioGRID; 111208; 49.
DR DIP; DIP-50038N; -.
DR IntAct; P12955; 14.
DR STRING; 9606.ENSP00000244137; -.
DR BindingDB; P12955; -.
DR ChEMBL; CHEMBL4185; -.
DR MEROPS; M24.007; -.
DR GlyGen; P12955; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P12955; -.
DR MetOSite; P12955; -.
DR PhosphoSitePlus; P12955; -.
DR SwissPalm; P12955; -.
DR BioMuta; PEPD; -.
DR DMDM; 50403718; -.
DR REPRODUCTION-2DPAGE; IPI00257882; -.
DR CPTAC; CPTAC-1170; -.
DR CPTAC; CPTAC-1192; -.
DR EPD; P12955; -.
DR jPOST; P12955; -.
DR MassIVE; P12955; -.
DR MaxQB; P12955; -.
DR PaxDb; P12955; -.
DR PeptideAtlas; P12955; -.
DR PRIDE; P12955; -.
DR ProteomicsDB; 19434; -.
DR ProteomicsDB; 52886; -. [P12955-1]
DR ProteomicsDB; 52887; -. [P12955-2]
DR Antibodypedia; 2792; 256 antibodies from 28 providers.
DR DNASU; 5184; -.
DR Ensembl; ENST00000244137.12; ENSP00000244137.5; ENSG00000124299.15. [P12955-1]
DR Ensembl; ENST00000397032.8; ENSP00000380226.3; ENSG00000124299.15. [P12955-2]
DR Ensembl; ENST00000436370.7; ENSP00000391890.2; ENSG00000124299.15. [P12955-3]
DR GeneID; 5184; -.
DR KEGG; hsa:5184; -.
DR MANE-Select; ENST00000244137.12; ENSP00000244137.5; NM_000285.4; NP_000276.2.
DR UCSC; uc002nur.5; human. [P12955-1]
DR CTD; 5184; -.
DR DisGeNET; 5184; -.
DR GeneCards; PEPD; -.
DR GeneReviews; PEPD; -.
DR HGNC; HGNC:8840; PEPD.
DR HPA; ENSG00000124299; Tissue enhanced (intestine, kidney).
DR MalaCards; PEPD; -.
DR MIM; 170100; phenotype.
DR MIM; 613230; gene.
DR neXtProt; NX_P12955; -.
DR OpenTargets; ENSG00000124299; -.
DR Orphanet; 742; Prolidase deficiency.
DR PharmGKB; PA33181; -.
DR VEuPathDB; HostDB:ENSG00000124299; -.
DR eggNOG; KOG2737; Eukaryota.
DR GeneTree; ENSGT00940000153657; -.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; P12955; -.
DR OMA; DQKFIYN; -.
DR PhylomeDB; P12955; -.
DR TreeFam; TF313396; -.
DR BRENDA; 3.4.13.9; 2681.
DR PathwayCommons; P12955; -.
DR SignaLink; P12955; -.
DR BioGRID-ORCS; 5184; 16 hits in 1080 CRISPR screens.
DR ChiTaRS; PEPD; human.
DR EvolutionaryTrace; P12955; -.
DR GeneWiki; PEPD; -.
DR GenomeRNAi; 5184; -.
DR Pharos; P12955; Tchem.
DR PRO; PR:P12955; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P12955; protein.
DR Bgee; ENSG00000124299; Expressed in ileal mucosa and 190 other tissues.
DR ExpressionAtlas; P12955; baseline and differential.
DR Genevisible; P12955; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; TAS:ProtInc.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
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 3D-structure; Acetylation; Alternative splicing; Collagen degradation;
KW Dipeptidase; Direct protein sequencing; Disease variant; Hydrolase;
KW Manganese; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..493
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000185087"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 370
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 412
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 68..131
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045370"
FT VAR_SEQ 184..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042629"
FT VARIANT 184
FT /note="R -> Q (in PD; dbSNP:rs121917722)"
FT /evidence="ECO:0000269|PubMed:8900231"
FT /id="VAR_011614"
FT VARIANT 276
FT /note="D -> N (in PD; dbSNP:rs121917721)"
FT /evidence="ECO:0000269|PubMed:2365824"
FT /id="VAR_004404"
FT VARIANT 278
FT /note="G -> D (in PD; dbSNP:rs121917723)"
FT /evidence="ECO:0000269|PubMed:8900231"
FT /id="VAR_011615"
FT VARIANT 388
FT /note="R -> H (in dbSNP:rs2230062)"
FT /id="VAR_051574"
FT VARIANT 435
FT /note="L -> F (in dbSNP:rs17570)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_014723"
FT VARIANT 448
FT /note="G -> R (in PD; dbSNP:rs121917724)"
FT /evidence="ECO:0000269|PubMed:12384772,
FT ECO:0000269|PubMed:8198124, ECO:0000269|PubMed:8900231"
FT /id="VAR_004405"
FT VARIANT 452
FT /note="Missing (in PD; dbSNP:rs757386104)"
FT /evidence="ECO:0000269|PubMed:8198124,
FT ECO:0000269|PubMed:8900231"
FT /id="VAR_004406"
FT CONFLICT 48
FT /note="L -> R (in Ref. 3; BAF84250)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="R -> L (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="W -> R (in Ref. 3; BAF83470)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="M -> I (in Ref. 3; BAF83445)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="C -> S (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="E -> G (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 283..284
FT /note="CF -> SV (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="A -> R (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="R -> L (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="V -> D (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..330
FT /note="MH -> ID (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="V -> A (in Ref. 3; BAG56678)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="T -> I (in Ref. 1; AAA60064)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="C -> R (in Ref. 3; BAF83470)"
FT /evidence="ECO:0000305"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5MC1"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5MC0"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6SRE"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5M4L"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 189..212
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:5MC1"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:6SRE"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 300..319
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 326..343
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:6SRE"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:6SRE"
FT TURN 442..445
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:6SRE"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:6SRE"
FT HELIX 472..480
FT /evidence="ECO:0007829|PDB:6SRE"
SQ SEQUENCE 493 AA; 54548 MW; E8C4A2497E44BA22 CRC64;
MAAATGPSFW LGNETLKVPL ALFALNRQRL CERLRKNPAV QAGSIVVLQG GEETQRYCTD
TGVLFRQESF FHWAFGVTEP GCYGVIDVDT GKSTLFVPRL PASHATWMGK IHSKEHFKEK
YAVDDVQYVD EIASVLTSQK PSVLLTLRGV NTDSGSVCRE ASFDGISKFE VNNTILHPEI
VECRVFKTDM ELEVLRYTNK ISSEAHREVM KAVKVGMKEY ELESLFEHYC YSRGGMRHSS
YTCICGSGEN SAVLHYGHAG APNDRTIQNG DMCLFDMGGE YYCFASDITC SFPANGKFTA
DQKAVYEAVL RSSRAVMGAM KPGVWWPDMH RLADRIHLEE LAHMGILSGS VDAMVQAHLG
AVFMPHGLGH FLGIDVHDVG GYPEGVERID EPGLRSLRTA RHLQPGMVLT VEPGIYFIDH
LLDEALADPA RASFLNREVL QRFRGFGGVR IEEDVVVTDS GIELLTCVPR TVEEIEACMA
GCDKAFTPFS GPK
