PCP_MOUSE
ID PCP_MOUSE Reviewed; 491 AA.
AC Q7TMR0; Q3TLW3; Q3V302; Q8BKK3; Q8R0T8; Q9D049;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Lysosomal Pro-X carboxypeptidase;
DE EC=3.4.16.2;
DE AltName: Full=Proline carboxypeptidase;
DE AltName: Full=Prolylcarboxypeptidase;
DE Short=PRCP;
DE Flags: Precursor;
GN Name=Prcp;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, Ovary, and Spinal ganglion;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, 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: Cleaves C-terminal amino acids linked to proline in peptides
CC such as angiotensin II, III and des-Arg9-bradykinin. This cleavage
CC occurs at acidic pH, but enzymatic activity is retained with some
CC substrates at neutral pH (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino
CC acid.; EC=3.4.16.2;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TMR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TMR0-2; Sequence=VSP_039456;
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; AK011816; BAB27858.1; -; mRNA.
DR EMBL; AK051677; BAC34716.1; -; mRNA.
DR EMBL; AK054462; BAE20697.1; -; mRNA.
DR EMBL; AK166282; BAE38679.1; -; mRNA.
DR EMBL; BC026424; AAH26424.1; -; mRNA.
DR EMBL; BC055022; AAH55022.1; -; mRNA.
DR CCDS; CCDS21452.1; -. [Q7TMR0-1]
DR RefSeq; NP_082519.1; NM_028243.3. [Q7TMR0-1]
DR AlphaFoldDB; Q7TMR0; -.
DR SMR; Q7TMR0; -.
DR BioGRID; 215382; 8.
DR STRING; 10090.ENSMUSP00000075429; -.
DR BindingDB; Q7TMR0; -.
DR ChEMBL; CHEMBL1255149; -.
DR ESTHER; mouse-pcp; Prolylcarboxypeptidase.
DR MEROPS; S28.001; -.
DR GlyGen; Q7TMR0; 5 sites.
DR PhosphoSitePlus; Q7TMR0; -.
DR EPD; Q7TMR0; -.
DR jPOST; Q7TMR0; -.
DR MaxQB; Q7TMR0; -.
DR PaxDb; Q7TMR0; -.
DR PeptideAtlas; Q7TMR0; -.
DR PRIDE; Q7TMR0; -.
DR ProteomicsDB; 287967; -. [Q7TMR0-1]
DR ProteomicsDB; 287968; -. [Q7TMR0-2]
DR Antibodypedia; 2472; 260 antibodies from 27 providers.
DR DNASU; 72461; -.
DR Ensembl; ENSMUST00000076052; ENSMUSP00000075429; ENSMUSG00000061119. [Q7TMR0-1]
DR GeneID; 72461; -.
DR KEGG; mmu:72461; -.
DR UCSC; uc009iij.2; mouse. [Q7TMR0-2]
DR UCSC; uc009iik.2; mouse. [Q7TMR0-1]
DR CTD; 5547; -.
DR MGI; MGI:1919711; Prcp.
DR VEuPathDB; HostDB:ENSMUSG00000061119; -.
DR eggNOG; KOG2183; Eukaryota.
DR GeneTree; ENSGT00940000158099; -.
DR HOGENOM; CLU_020959_0_0_1; -.
DR InParanoid; Q7TMR0; -.
DR OMA; TLEDYAM; -.
DR OrthoDB; 555765at2759; -.
DR PhylomeDB; Q7TMR0; -.
DR TreeFam; TF314414; -.
DR BRENDA; 3.4.16.2; 3474.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 72461; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Prcp; mouse.
DR PRO; PR:Q7TMR0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TMR0; protein.
DR Bgee; ENSMUSG00000061119; Expressed in undifferentiated genital tubercle and 197 other tissues.
DR ExpressionAtlas; Q7TMR0; baseline and differential.
DR Genevisible; Q7TMR0; MM.
DR GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI.
DR GO; GO:0097009; P:energy homeostasis; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0002353; P:plasma kallikrein-kinin cascade; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:MGI.
DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IMP:MGI.
DR Gene3D; 1.20.120.980; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008758; Peptidase_S28.
DR InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR Pfam; PF05577; Peptidase_S28; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..43
FT /evidence="ECO:0000250"
FT /id="PRO_0000027310"
FT CHAIN 44..491
FT /note="Lysosomal Pro-X carboxypeptidase"
FT /id="PRO_0000027311"
FT REGION 192..332
FT /note="SKS domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 428
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 453
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 213..370
FT /evidence="ECO:0000250"
FT DISULFID 231..308
FT /evidence="ECO:0000250"
FT DISULFID 262..341
FT /evidence="ECO:0000250"
FT DISULFID 362..392
FT /evidence="ECO:0000250"
FT VAR_SEQ 102..491
FT /note="GFMWDVAEELKAMLVFAEHRYYGESLPFGQDSFKDSQHLNFLTSEQALADFA
FT ELIRHLEKTIPGAQGQPVIAIGGSYGGMLAAWFRMKYPHIVVGALAASAPIWQLDGMVP
FT CGEFMKIVTNDFRKSGPYCSESIRKSWNVIDKLSGSGSGLQSLTNILHLCSPLTSEKIP
FT TLKGWIAETWVNLAMVNYPYACNFLQPLPAWPIKEVCQYLKNPNVSDTVLLQNIFQALS
FT VYYNYSGQAACLNISQTTTSSLGSMGWSFQACTEMVMPFCTNGIDDMFEPFLWDLEKYS
FT NDCFNQWGVKPRPHWMTTMYGGKNISSHSNIIFSNGELDPWSGGGVTRDITDTLVAINI
FT HDGAHHLDLRAHNAFDPSSVLLSRLLEVKHMKKWILDFYSNIQ -> VCIH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039456"
FT CONFLICT 426
FT /note="E -> K (in Ref. 1; BAE38679 and 2; AAH55022)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="H -> P (in Ref. 1; BAE38679 and 2; AAH55022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 55027 MW; EC97198BF9E097EF CRC64;
MGCRALLLLS FLLLGAATTI PPRLKTLGSP HLSASPTPDP AVARKYSVLY FEQKVDHFGF
ADMRTFKQRY LVADKHWQRN GGSILFYTGN EGDIVWFCNN TGFMWDVAEE LKAMLVFAEH
RYYGESLPFG QDSFKDSQHL NFLTSEQALA DFAELIRHLE KTIPGAQGQP VIAIGGSYGG
MLAAWFRMKY PHIVVGALAA SAPIWQLDGM VPCGEFMKIV TNDFRKSGPY CSESIRKSWN
VIDKLSGSGS GLQSLTNILH LCSPLTSEKI PTLKGWIAET WVNLAMVNYP YACNFLQPLP
AWPIKEVCQY LKNPNVSDTV LLQNIFQALS VYYNYSGQAA CLNISQTTTS SLGSMGWSFQ
ACTEMVMPFC TNGIDDMFEP FLWDLEKYSN DCFNQWGVKP RPHWMTTMYG GKNISSHSNI
IFSNGELDPW SGGGVTRDIT DTLVAINIHD GAHHLDLRAH NAFDPSSVLL SRLLEVKHMK
KWILDFYSNI Q
