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Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)]

 CATC_BOVIN              Reviewed;         463 AA.
Q3ZCJ8;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 1.
25-OCT-2017, entry version 78.
RecName: Full=Dipeptidyl peptidase 1;
EC=3.4.14.1;
AltName: Full=Cathepsin C;
AltName: Full=Cathepsin J;
AltName: Full=Dipeptidyl peptidase I;
Short=DPP-I;
Short=DPPI;
AltName: Full=Dipeptidyl transferase;
Contains:
RecName: Full=Dipeptidyl peptidase 1 exclusion domain chain;
AltName: Full=Dipeptidyl peptidase I exclusion domain chain;
Contains:
RecName: Full=Dipeptidyl peptidase 1 heavy chain;
AltName: Full=Dipeptidyl peptidase I heavy chain;
Contains:
RecName: Full=Dipeptidyl peptidase 1 light chain;
AltName: Full=Dipeptidyl peptidase I light chain;
Flags: Precursor;
Name=CTSC;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Can
act as both an exopeptidase and endopeptidase. Can degrade
glucagon. Plays a role in the generation of cytotoxic lymphocyte
effector function (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
Note=Binds 1 Cl(-) ion per heavy chain. {ECO:0000250};
-!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
heavy- and light chains. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; BC102115; AAI02116.1; -; mRNA.
RefSeq; NP_001028789.1; NM_001033617.2.
UniGene; Bt.49573; -.
ProteinModelPortal; Q3ZCJ8; -.
SMR; Q3ZCJ8; -.
STRING; 9913.ENSBTAP00000014735; -.
BindingDB; Q3ZCJ8; -.
ChEMBL; CHEMBL1075050; -.
MEROPS; C01.070; -.
PaxDb; Q3ZCJ8; -.
PeptideAtlas; Q3ZCJ8; -.
PRIDE; Q3ZCJ8; -.
GeneID; 352958; -.
KEGG; bta:352958; -.
CTD; 1075; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
HOGENOM; HOG000068022; -.
HOVERGEN; HBG005248; -.
InParanoid; Q3ZCJ8; -.
KO; K01275; -.
PRO; PR:Q3ZCJ8; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005764; C:lysosome; IBA:GO_Central.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
Gene3D; 2.40.128.80; -; 1.
InterPro; IPR014882; CathepsinC_exc.
InterPro; IPR036496; CathepsinC_exc_dom_sf.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08773; CathepsinC_exc; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF75001; SSF75001; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
2: Evidence at transcript level;
Chloride; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
Lysosome; Protease; Reference proteome; Signal; Thiol protease;
Zymogen.
SIGNAL 1 24 {ECO:0000250}.
CHAIN 25 134 Dipeptidyl peptidase 1 exclusion domain
chain.
/FTId=PRO_0000238121.
PROPEP 135 230 {ECO:0000250}.
/FTId=PRO_0000238122.
CHAIN 231 394 Dipeptidyl peptidase 1 heavy chain.
{ECO:0000250}.
/FTId=PRO_0000238123.
CHAIN 395 463 Dipeptidyl peptidase 1 light chain.
{ECO:0000250}.
/FTId=PRO_0000238124.
ACT_SITE 258 258 {ECO:0000250}.
ACT_SITE 405 405 {ECO:0000250}.
ACT_SITE 427 427 {ECO:0000250}.
BINDING 302 302 Chloride. {ECO:0000250}.
BINDING 304 304 Chloride; via amide nitrogen.
{ECO:0000250}.
BINDING 347 347 Chloride. {ECO:0000250}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 118 {ECO:0000250}.
DISULFID 54 136 {ECO:0000250}.
DISULFID 255 298 {ECO:0000250}.
DISULFID 291 331 {ECO:0000250}.
DISULFID 321 337 {ECO:0000250}.
SEQUENCE 463 AA; 51949 MW; 5602557E041FB29C CRC64;
MGPWSGSRLV ALLLLVYGAG SVRGDTPANC TYPDLLGTWV FQVGSSGSQR DVNCSVMGPP
EKKVVVHLKK LDTAYDDFGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GGKVTSYCHE
TMTGWVHDVL GRNRACFTGR KTGNTSENVN VNTARLAGLE ETYSNRLYRY NHDFVKAINA
IQKSWTAAPY MEYETLTLKE MIRRGGGHSR RIPRPKPAPI TAEIQKKILH LPTSWDWRNV
HGINFVTPVR NQGSCGSCYS FASMGMMEAR IRILTNNTQT PILSPQEVVS CSQYAQGCEG
GFPYLIAGKY AQDFGLVEED CFPYTGTDSP CRLKEGCFRY YSSEYHYVGG FYGGCNEALM
KLELVHQGPM AVAFEVYDDF LHYRKGVYHH TGLRDPFNPF ELTNHAVLLV GYGTDAASGL
DYWIVKNSWG TSWGENGYFR IRRGTDECAI ESIALAATPI PKL


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