ID   CATL1_SHEEP             Reviewed;         217 AA.
AC   Q10991;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Cathepsin L1;
DE            EC=3.4.22.15;
DE   Contains:
DE     RecName: Full=Cathepsin L1 heavy chain;
DE   Contains:
DE     RecName: Full=Cathepsin L1 light chain;
GN   Name=CTSL; Synonyms=CTSL1;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=96321328; PubMed=8759291; DOI=10.1016/0305-0491(96)00010-7;
RA   Ritonja A., Coetzer T.H.T., Pike R.N., Dennison C.;
RT   "The amino acid sequences, structure comparisons and inhibition
RT   kinetics of sheep cathepsin L and sheep stefin B.";
RL   Comp. Biochem. Physiol. 114B:193-198(1996).
CC   -!- FUNCTION: Important for the overall degradation of proteins in
CC       lysosomes.
CC   -!- CATALYTIC ACTIVITY: Specificity close to that of papain. As
CC       compared to cathepsin B, cathepsin L exhibits higher activity
CC       toward protein substrates, but has little activity on Z-Arg-Arg-
CC       NHMec, and no peptidyl-dipeptidase activity.
CC   -!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide
CC       bonds.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
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DR   HSSP; O60911; 1FH0.
DR   SMR; Q10991; 2-217.
DR   MEROPS; C01.032; -.
DR   HOVERGEN; Q10991; -.
DR   BRENDA; 3.4.22.15; 271.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   PANTHER; PTHR12411; Peptidase_C1A; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   ProDom; PD000158; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 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   Direct protein sequencing; Disulfide bond; Hydrolase; Lysosome;
KW   Protease; Thiol protease.
FT   CHAIN         1    175       Cathepsin L1 heavy chain.
FT                                /FTId=PRO_0000026260.
FT   PROPEP      176    176
FT                                /FTId=PRO_0000026261.
FT   CHAIN       177    217       Cathepsin L1 light chain.
FT                                /FTId=PRO_0000026262.
FT   ACT_SITE     25     25       By similarity.
FT   ACT_SITE    163    163       By similarity.
FT   ACT_SITE    184    184       By similarity.
FT   DISULFID     22     65       By similarity.
FT   DISULFID    156    206       Interchain (between heavy and light
FT                                chains) (By similarity).
SQ   SEQUENCE   217 AA;  23608 MW;  552F6ED563564406 CRC64;
     VPKSVDWTKK GYVTPVKNQG QCGSCWAFSA TGALEGQMFR KTGKLVSLSE QNLVDSSRPQ
     GNQGCNGGLM DNAFQYIKEN GGLDSEESYP YEATDTSCNY KPEYSAAKDT GFVDIPQREK
     ALMKAVATVG PISVAIDAGH SSFQFYKSGI YYDPDCSSKD LDHGVLVVGY GFEGTNNKFW
     IVKNSWGPEW GNKGYVKMAK DQNNHCGIAT AASYPTV
//