PPGB_MOUSE
ID PPGB_MOUSE Reviewed; 474 AA.
AC P16675; Q8VEF6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Lysosomal protective protein;
DE EC=3.4.16.5;
DE AltName: Full=Carboxypeptidase C;
DE AltName: Full=Carboxypeptidase L;
DE AltName: Full=Cathepsin A;
DE AltName: Full=Protective protein cathepsin A;
DE Short=PPCA;
DE AltName: Full=Protective protein for beta-galactosidase;
DE Contains:
DE RecName: Full=Lysosomal protective protein 32 kDa chain;
DE Contains:
DE RecName: Full=Lysosomal protective protein 20 kDa chain;
DE Flags: Precursor;
GN Name=Ctsa; Synonyms=Ppgb;
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].
RX PubMed=2106523; DOI=10.1016/s0021-9258(19)39616-4;
RA Galjart N.J., Gillemans N., Meijer D., D'Azzo A.;
RT "Mouse 'protective protein'. cDNA cloning, sequence comparison, and
RT expression.";
RL J. Biol. Chem. 265:4678-4684(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140 AND ASN-327.
RC TISSUE=Epidermis;
RX PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA Nishimura S.;
RT "High throughput quantitative glycomics and glycoform-focused proteomics of
RT murine dermis and epidermis.";
RL Mol. Cell. Proteomics 4:1977-1989(2005).
RN [4]
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: Protective protein appears to be essential for both the
CC activity of beta-galactosidase and neuraminidase, it associates with
CC these enzymes and exerts a protective function necessary for their
CC stability and activity. This protein is also a carboxypeptidase and can
CC deamidate tachykinins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity.;
CC EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074,
CC ECO:0000255|PROSITE-ProRule:PRU10075};
CC -!- SUBUNIT: Heterodimer of a 32 kDa chain and a 20 kDa chain; disulfide-
CC linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; J05261; AAA39982.1; -; mRNA.
DR EMBL; BC018534; AAH18534.1; -; mRNA.
DR CCDS; CCDS17062.1; -.
DR PIR; A35732; A35732.
DR RefSeq; NP_001033581.1; NM_001038492.2.
DR PDB; 7KDV; EM; 4.59 A; B/D/F/H/J/L=24-474.
DR PDBsum; 7KDV; -.
DR AlphaFoldDB; P16675; -.
DR SMR; P16675; -.
DR BioGRID; 202325; 21.
DR STRING; 10090.ENSMUSP00000099382; -.
DR ChEMBL; CHEMBL3259490; -.
DR ESTHER; mouse-Ppgb; Carboxypeptidase_S10.
DR MEROPS; S10.002; -.
DR GlyConnect; 2492; 5 N-Linked glycans (2 sites).
DR GlyGen; P16675; 2 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; P16675; -.
DR PhosphoSitePlus; P16675; -.
DR SwissPalm; P16675; -.
DR CPTAC; non-CPTAC-3865; -.
DR EPD; P16675; -.
DR jPOST; P16675; -.
DR PaxDb; P16675; -.
DR PeptideAtlas; P16675; -.
DR PRIDE; P16675; -.
DR ProteomicsDB; 291713; -.
DR Antibodypedia; 27832; 486 antibodies from 36 providers.
DR DNASU; 19025; -.
DR Ensembl; ENSMUST00000103093; ENSMUSP00000099382; ENSMUSG00000017760.
DR GeneID; 19025; -.
DR KEGG; mmu:19025; -.
DR UCSC; uc008nwm.2; mouse.
DR CTD; 5476; -.
DR MGI; MGI:97748; Ctsa.
DR VEuPathDB; HostDB:ENSMUSG00000017760; -.
DR eggNOG; KOG1282; Eukaryota.
DR GeneTree; ENSGT00880000138014; -.
DR HOGENOM; CLU_008523_13_3_1; -.
DR InParanoid; P16675; -.
DR PhylomeDB; P16675; -.
DR TreeFam; TF323769; -.
DR BRENDA; 3.4.16.5; 3474.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 19025; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ctsa; mouse.
DR PRO; PR:P16675; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P16675; protein.
DR Bgee; ENSMUSG00000017760; Expressed in stroma of bone marrow and 268 other tissues.
DR ExpressionAtlas; P16675; baseline and differential.
DR Genevisible; P16675; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006508; P:proteolysis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
DR Gene3D; 3.40.50.1820; -; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..23
FT CHAIN 24..474
FT /note="Lysosomal protective protein"
FT /id="PRO_0000004277"
FT CHAIN 24..320
FT /note="Lysosomal protective protein 32 kDa chain"
FT /id="PRO_0000004278"
FT CHAIN 321..474
FT /note="Lysosomal protective protein 20 kDa chain"
FT /id="PRO_0000004279"
FT ACT_SITE 173
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /evidence="ECO:0000250"
FT ACT_SITE 451
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT DISULFID 83..356
FT /evidence="ECO:0000250"
FT DISULFID 235..251
FT /evidence="ECO:0000250"
FT DISULFID 236..241
FT /evidence="ECO:0000250"
FT DISULFID 276..325
FT /evidence="ECO:0000250"
FT CONFLICT 425
FT /note="G -> W (in Ref. 2; AAH18534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53844 MW; 8F4D5A7F4FEBC6CE CRC64;
MPGTALSPLL LLLLLSWASR NEAAPDQDEI DCLPGLAKQP SFRQYSGYLR ASDSKHFHYW
FVESQNDPKN SPVVLWLNGG PGCSSLDGLL TEHGPFLIQP DGVTLEYNPY AWNLIANVLY
IESPAGVGFS YSDDKMYVTN DTEVAENNYE ALKDFFRLFP EYKDNKLFLT GESYAGIYIP
TLAVLVMQDP SMNLQGLAVG NGLASYEQND NSLVYFAYYH GLLGNRLWTS LQTHCCAQNK
CNFYDNKDPE CVNNLLEVSR IVGKSGLNIY NLYAPCAGGV PGRHRYEDTL VVQDFGNIFT
RLPLKRRFPE ALMRSGDKVR LDPPCTNTTA PSNYLNNPYV RKALHIPESL PRWDMCNFLV
NLQYRRLYQS MNSQYLKLLS SQKYQILLYN GDVDMACNFM GDEWFVDSLN QKMEVQRRPW
LVDYGESGEQ VAGFVKECSH ITFLTIKGAG HMVPTDKPRA AFTMFSRFLN KEPY
