ID   PPGB_BOVIN              Reviewed;         479 AA.
AC   Q3MI05;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Lysosomal protective protein;
DE            EC=3.4.16.5;
DE   AltName: Full=Cathepsin A;
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; BC104495; AAI04496.1; -; mRNA.
DR   RefSeq; NP_001030403.1; NM_001035326.1.
DR   AlphaFoldDB; Q3MI05; -.
DR   SMR; Q3MI05; -.
DR   STRING; 9913.ENSBTAP00000039003; -.
DR   ESTHER; bovin-ppgb; Carboxypeptidase_S10.
DR   MEROPS; S10.002; -.
DR   GlyCosmos; Q3MI05; 2 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000039003; -.
DR   GeneID; 518169; -.
DR   KEGG; bta:518169; -.
DR   CTD; 5476; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_3_1; -.
DR   InParanoid; Q3MI05; -.
DR   OrthoDB; 1647009at2759; -.
DR   TreeFam; TF323769; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
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:SF497; LYSOSOMAL PROTECTIVE PROTEIN; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW   Protease; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..479
FT                   /note="Lysosomal protective protein"
FT                   /id="PRO_0000236219"
FT   CHAIN           28..325
FT                   /note="Lysosomal protective protein 32 kDa chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000236220"
FT   CHAIN           326..479
FT                   /note="Lysosomal protective protein 20 kDa chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000236221"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..361
FT                   /evidence="ECO:0000250"
FT   DISULFID        239..255
FT                   /evidence="ECO:0000250"
FT   DISULFID        240..245
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  53980 MW;  A37CC37D5C575FBF CRC64;
     MFRAALWPPV LLLLQLLLLA CAPGGEGAHD QDEIRFLPGL AKQPSFRQYS GYLKGSGSKR
     LHYWFVESQK DPKSSPVVLW LNGGPGCSSL DGLLTEHGPF LIQPDGVTLE YNPYSWNLIA
     NVLYLESPAG VGFSYSDDKS YATNDTEVAQ SNFEALKDFF CLFPEYKGNE LFLTGESYAG
     IYIPTLAVLV MQDPSMNLQG LAVGNGLSSY EQNDNSLVYF AYYHGLLGNR LWSSLQTHCC
     SQNQCNFHDN KEPECVANLQ EVSHIVASSG LNIYNLYAPC AGGVPSHVRH EKDTVVVQDL
     GNIFTRLPLK RVWHQTLLRS GEKVHLDPPC TNTTAASNYL NDPHVRKALH IPEQLPRWDL
     CNFLVNIQYR RLYQSMCSQY LKLLSAQKYR ILLYNGDVDM ACNFMGDEWF VDSLNQKMEV
     QRRPWLVDYG ESGEQIAGFV KEFSHIAFLT IKGAGHMVPT DKPQAALTMF SRFLNRQPY
//