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Database: UniProt
Entry: A0A5A9NMD3_9TELE
LinkDB: A0A5A9NMD3_9TELE
Original site: A0A5A9NMD3_9TELE 
ID   A0A5A9NMD3_9TELE        Unreviewed;       336 AA.
AC   A0A5A9NMD3;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Cathepsin L {ECO:0000313|EMBL:KAA0711204.1};
GN   ORFNames=E1301_Tti002688 {ECO:0000313|EMBL:KAA0711204.1};
OS   Triplophysa tibetana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Nemacheilidae; Triplophysa.
OX   NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0711204.1, ECO:0000313|Proteomes:UP000324632};
RN   [1] {ECO:0000313|EMBL:KAA0711204.1, ECO:0000313|Proteomes:UP000324632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0711204.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAA0711204.1};
RX   PubMed=30977968;
RA   Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA   Wang W., Yang R.;
RT   "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT   to the harsh high-altitude environment of the Tibetan Plateau.";
RL   Mol. Ecol. Resour. 19:1027-1036(2019).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAA0711204.1}.
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DR   EMBL; SOYY01000015; KAA0711204.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5A9NMD3; -.
DR   Proteomes; UP000324632; Chromosome 15.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411:SF1011; CATHEPSIN L.1; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324632};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..336
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023061160"
FT   DOMAIN          26..86
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          118..335
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   336 AA;  36760 MW;  D410D4DD526B7B55 CRC64;
     MRMLVAIAAV LVAASAASLS LEDMEFHAWK LKFGKSYGSV VEESQRKLTW LSNRKLVLVH
     NMLADQGIKS YRLGMTYFAD MDNEEYRRVI FHGCLSSFNR TKPRDGATFF RLAGGAVLPD
     SVDWRDKGFV TDIKDQKQCG SCWAFSATGS LEGQTFRKTG KLVSLSEQQL VDCSGSFGNF
     GCGGGLMDQA FQYIEANKGL DTEESYPYEG QDGQCRFNPN TVGAKCTGYV DVNTGDESAL
     QEAVATIGPI SVAIDAGHSS FQLYESGVYD EPECSSSELD HGVLAVGYGT QDGENYWLVK
     NSFSWGLGWG HKGYIMMSRN KSNQCGIATA ASYPMV
//
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