CATL1_CHICK
ID CATL1_CHICK Reviewed; 218 AA.
AC P09648;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Procathepsin L;
DE EC=3.4.22.15;
DE AltName: Full=Cathepsin L1;
DE Contains:
DE RecName: Full=Cathepsin L heavy chain;
DE Contains:
DE RecName: Full=Cathepsin L light chain;
DE Contains:
DE RecName: Full=Cathepsin L;
DE Flags: Fragments;
GN Name=CTSL; Synonyms=CTSL1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3305012; DOI=10.1111/j.1432-1033.1987.tb13298.x;
RA Wada K., Takai T., Tanabe T.;
RT "Amino acid sequence of chicken liver cathepsin L.";
RL Eur. J. Biochem. 167:13-18(1987).
RN [2]
RP PROTEIN SEQUENCE OF 1-37 AND 177-216.
RC TISSUE=Liver;
RX PubMed=3792553; DOI=10.1016/0014-5793(86)81137-1;
RA Wada K., Tanabe T.;
RT "N-terminal amino acid sequences of the heavy and light chains of chicken
RT liver cathepsin L.";
RL FEBS Lett. 209:330-334(1986).
RN [3]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3676277; DOI=10.1021/bi00392a017;
RA Dufour E., Obled A., Valin C., Bechet D., Ribadeau-Dumas B., Huet J.-C.;
RT "Purification and amino acid sequence of chicken liver cathepsin L.";
RL Biochemistry 26:5689-5695(1987).
CC -!- FUNCTION: Important for the overall degradation of proteins in
CC lysosomes.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specificity close to that of papain. As compared to cathepsin
CC B, cathepsin L exhibits higher activity toward protein substrates,
CC but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-
CC dipeptidase activity.; EC=3.4.22.15;
CC -!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide bonds.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P06797}. Apical
CC cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P06797}; Extracellular side
CC {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule {ECO:0000250|UniProtKB:P25975}. Secreted,
CC extracellular space {ECO:0000250|UniProtKB:P06797}. Secreted
CC {ECO:0000250|UniProtKB:P06797}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR PIR; S00081; KHCHL.
DR AlphaFoldDB; P09648; -.
DR SMR; P09648; -.
DR STRING; 9031.ENSGALP00000020559; -.
DR MEROPS; C01.032; -.
DR PaxDb; P09648; -.
DR VEuPathDB; HostDB:geneid_427466; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; P09648; -.
DR PhylomeDB; P09648; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR CDD; cd02248; Peptidase_C1A; 1.
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; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lysosome; Membrane; Protease;
KW Reference proteome; Secreted; Thiol protease.
FT CHAIN 1..218
FT /note="Cathepsin L"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT /id="PRO_0000450795"
FT CHAIN 1..176
FT /note="Cathepsin L heavy chain"
FT /id="PRO_0000026263"
FT CHAIN 177..218
FT /note="Cathepsin L light chain"
FT /id="PRO_0000026264"
FT ACT_SITE 25
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
FT DISULFID 22..65
FT /evidence="ECO:0000250"
FT DISULFID 56..99
FT /evidence="ECO:0000250"
FT DISULFID 158..207
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="Q -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..42
FT /note="RTK -> FKT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..98
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="N -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="I -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_CONS 176..177
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23963 MW; D26E21BC071686C2 CRC64;
APRSVDWREK GYVTPVKDQG QCGSCWAFST TGALEGQHFR TKGKLVSLSE QNLVDCSRPE
GNQGCNGGLM DQAFQYVQDN GGIDSEESYP YTAKDDEDCR YKAEYNAAND TGFVDIPQGH
ERALMKAVAS VGPVSVAIDA GHSSFQFYQS GIYYEPDCSS EDLDHGVLVV GYGFEGGKKY
WIVKNSWGEK WGDKGYIYMA KDRKNHCGIA TAASYPLV
