CATC_SCHMA
ID CATC_SCHMA Reviewed; 454 AA.
AC Q26563;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Cathepsin C;
DE EC=3.4.22.-;
DE Flags: Precursor;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Liberian;
RA Butler R., Michel A., Kunz W., Klinkert M.-Q.;
RT "Sequence of Schistosoma mansoni cathepsin C and its structural comparison
RT with papain and cathepsins B and L of the parasite.";
RL Protein Pept. Lett. 2:313-320(1995).
CC -!- FUNCTION: Thiol protease. Has a role as a digestive enzyme.
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
CC Note=Binds 1 Cl(-) ion per heavy chain. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089}.
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DR EMBL; Z32531; CAA83543.1; -; mRNA.
DR AlphaFoldDB; Q26563; -.
DR SMR; Q26563; -.
DR STRING; 6183.Smp_019030.1; -.
DR MEROPS; C01.070; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_048219_0_0_1; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02621; Peptidase_C1A_CathepsinC; 1.
DR Gene3D; 2.40.128.80; -; 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; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
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; SSF54001; 1.
DR SUPFAM; SSF75001; SSF75001; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..217
FT /evidence="ECO:0000255"
FT /id="PRO_0000026356"
FT CHAIN 218..454
FT /note="Cathepsin C"
FT /id="PRO_0000026357"
FT ACT_SITE 247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT BINDING 291
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..107
FT /evidence="ECO:0000250"
FT DISULFID 244..287
FT /evidence="ECO:0000250"
FT DISULFID 280..321
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 51281 MW; E2D8A1F6AAD4CBC6 CRC64;
MHWVFHCILI ILACLRFTCA DTPANCTYED AHGRWKFHIG DYQSKCPEKL NSKQSVVISL
LYPDIAIDEF GNRGHWTLIY NQGFEVTINH RKWLVIFAYK SNGEFNCHKS MPMWTHDTLI
DSGSVCSGKI GVHDKFHINK LFGSKSFGRT LYHINPSFVG KINAHQKSWR GEIYPELSKY
TIDELRNRAG GVKSMVTRPS VLNRKTPSKE LISLTGNLPL EFDWTSPPDG SRSPVTPIRN
QGICGSCYAS PSAAALEARI RLVSNFSEQP ILSPQTVVDC SPYSEGCNGG FPFLIAGKYG
EDFGLPQKIV IPYTGEDTGK CTVSKNCTRY YTTDYSYIGG YYGATNEKLM QLELISNGPF
PVGFEVYEDF QFYKEGIYHH TTVQTDHYNF NPFELTNHAV LLVGYGVDKL SGEPYWKVKN
SWGVEWGEQG YFRILRGTDE CGVESLGVRF DPVL
