ID G1PG63_MYOLU Unreviewed; 359 AA.
AC G1PG63;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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|Ensembl:ENSMLUP00000009608.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009608.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000009608.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000009608.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAPE02025376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PG63; -.
DR STRING; 59463.ENSMLUP00000009608; -.
DR Ensembl; ENSMLUT00000010541.2; ENSMLUP00000009608.2; ENSMLUG00000010550.2.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155787; -.
DR HOGENOM; CLU_048219_0_0_1; -.
DR InParanoid; G1PG63; -.
DR OMA; HWDWRNV; -.
DR TreeFam; TF313225; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0016505; F:peptidase activator activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0031642; P:negative regulation of myelination; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1903980; P:positive regulation of microglial cell activation; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
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:UP000001074};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT DOMAIN 127..354
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 359 AA; 40651 MW; D292D0479FE9E09B CRC64;
LQYKQEGSKV TSYCDETMTG WVHDVLGRNW ACFTGKKVGT AAENVRVNAA HLEGLQEKYS
NRLYKYNHDF VKAINAVQKS WTATTYLEYE TLTLREMIRR SGGLRQRLPR PKPAPLTAEI
HEKLLHLPTS WDWRNVHGTN FVTPVRNQAS CGSCYSFASM GMLEARIRIL TNNTQSPILS
PQEVVSCSQY AQGCEGGFPY LIAGKYAQDF GLVEEACFPY TGTDSPCKMK EDCFRYYTSE
YHYVGGFYGG CNEALMKLEL VHHGPMAVAF EVYDDFLHYN QGIYHHTGLK DPFNPFELTN
HAVLLVGYGT DPKTGLDYWI VKNSWGTSWG EQGYFRIRRG TDECAIESIA MAATPIPKL
//
