ID G5C2H0_HETGA Unreviewed; 462 AA.
AC G5C2H0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Dipeptidyl peptidase 1 {ECO:0000256|ARBA:ARBA00014709};
DE EC=3.4.14.1 {ECO:0000256|ARBA:ARBA00012059};
DE AltName: Full=Cathepsin C {ECO:0000256|ARBA:ARBA00029779};
DE AltName: Full=Cathepsin J {ECO:0000256|ARBA:ARBA00029762};
DE AltName: Full=Dipeptidyl peptidase I {ECO:0000256|ARBA:ARBA00032961};
DE AltName: Full=Dipeptidyl transferase {ECO:0000256|ARBA:ARBA00030778};
GN Name=CTSC {ECO:0000313|EMBL:JAN98325.1};
GN ORFNames=GW7_12090 {ECO:0000313|EMBL:EHB15731.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB15731.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB15731.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAN98325.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:JAN98325.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except
CC when Xaa is Arg or Lys, or Yaa or Zaa is Pro.; EC=3.4.14.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000738};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
CC heavy- and light chains. {ECO:0000256|ARBA:ARBA00011610}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; JH173078; EHB15731.1; -; Genomic_DNA.
DR EMBL; GEBF01005307; JAN98325.1; -; Transcribed_RNA.
DR RefSeq; XP_004868266.1; XM_004868209.2.
DR AlphaFoldDB; G5C2H0; -.
DR STRING; 10181.G5C2H0; -.
DR MEROPS; C01.070; -.
DR Ensembl; ENSHGLT00100017547; ENSHGLP00100017362; ENSHGLG00100012805.
DR GeneID; 101697606; -.
DR KEGG; hgl:101697606; -.
DR CTD; 1075; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; G5C2H0; -.
DR OMA; HWDWRNV; -.
DR OrthoDB; 5475703at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000001420; Expressed in liver and 10 other cell types or tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02621; Peptidase_C1A_CathepsinC; 1.
DR Gene3D; 2.40.128.80; Cathepsin C, exclusion domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR039412; CatC.
DR InterPro; IPR014882; CathepsinC_exc.
DR InterPro; IPR036496; CathepsinC_exc_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF942; DIPEPTIDYL PEPTIDASE 1; 1.
DR Pfam; PF08773; CathepsinC_exc; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF75001; Dipeptidyl peptidase I (cathepsin C), exclusion domain; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..462
FT /note="Dipeptidyl peptidase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007361741"
FT DOMAIN 230..457
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 462 AA; 52296 MW; E226E3171CF796E4 CRC64;
MGLRPHSLLA ALLLLLLGLR GVRCDTPANC TYPDLLGTWV FQVGPGGSGR DVNCSAMEPP
EKKVAVHLKK MDTAYDDFGN TGYFTIIYNQ GFEIVLNDYK WFAFFKYETK GSKVISYCQE
TMTGWVHDVL GRNWACFVGK KVESPENVNV NTAYLESHLE KYSNRLYKYD HKFVKAINAV
QKSWTATTYK EYETLTLREM ARRRGGHNQI IPRPKPAPLS AEIQQKILQL PKSWDWRDVH
GMNFVSPVRN QGYCGSCYSF ASMGMLEARI RILTNNTQTP ILSPQEVVSC SQYAQGCEGG
FPYLIAGKYA QDFGFVEESC FPYTGTDAPC KMKEDCMRYY TSEYHYVGGF YGGCNEALMK
LELVQHGPMA VAFEVCDDFM HYHKGIYHHT GLRDPFNPFE LTNHAVLLVG YGTDSANGMD
YWIVKNSWGT SWGEKGYFRI LRGTDECAIE SIAMAATPIP KL
//
