ID   CATL2_BOVIN             Reviewed;         334 AA.
AC   Q5E998;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Cathepsin L2;
DE            EC=3.4.22.43;
DE   Flags: Precursor;
GN   Name=CTSV; Synonyms=CTSL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Cysteine protease. May have an important role in corneal
CC       physiology (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The recombinant enzyme hydrolyzes proteins (serum albumin,
CC         collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec
CC         > Z-Val-Arg-NHMec).; EC=3.4.22.43;
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
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   EMBL; BT021022; AAX09039.1; -; mRNA.
DR   AlphaFoldDB; Q5E998; -.
DR   SMR; Q5E998; -.
DR   MEROPS; C01.032; -.
DR   PRIDE; Q5E998; -.
DR   InParanoid; Q5E998; -.
DR   Proteomes; UP000009136; Unplaced.
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:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW   Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000238118"
FT   CHAIN           114..334
FT                   /note="Cathepsin L2"
FT                   /id="PRO_0000238119"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        135..178
FT                   /evidence="ECO:0000250"
FT   DISULFID        169..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..323
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  37393 MW;  ECA2BA83241BDBC9 CRC64;
     MNPSFFLTVL CLGVASAAPK LDPNLDAHWH QWKATHRRLY GMNEEEWRRA VWEKNKKIID
     LHNQEYSEGK HGFRMAMNAF GDMTNEEFRQ VMNGFQNQKH KKGKLFHEPL LVDVPKSVDW
     TKKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGKLVS LSEQNLVDCS RAQGNQGCNG
     GLMDNAFQYI KDNGCLDSEE SYPYLATDTN SCNYKPECSA ANDTGFVDIP QREKALMKAV
     ATVGPISVAI DAGHTSFQFY KSGIYYDPDC SSKDLDHGVL VVGYGFEGTD SNNNKFWIVK
     NSWGPEWGWN GYVKMAKDQN NHCGIATAAS YPTV