ID A0A485P4F3_LYNPA Unreviewed; 459 AA.
AC A0A485P4F3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Cathepsin f {ECO:0000313|EMBL:VFV39178.1};
GN ORFNames=LYPA_23C000181 {ECO:0000313|EMBL:VFV39178.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV39178.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV39178.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; CAAGRJ010027056; VFV39178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485P4F3; -.
DR Proteomes; UP000386466; 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; cd02248; Peptidase_C1A; 1.
DR Gene3D; 1.10.287.2250; -; 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:SF444; CATHEPSIN F; 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 Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000386466};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..459
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019811757"
FT DOMAIN 162..219
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 246..457
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 459 AA; 50880 MW; D8DB760F8ACF620C CRC64;
MAPWLLLLSL LGLLPGASPA PPHRAADARA REAAYPELLG PSRFALEMYN RGRAAGTRAA
LRAVRGRVRR AGEGSLYSLK ATLEEPPCND PTVCQLPVSK KTLLCSFEVL DELGKHMLLR
RDCGPVDTKV TDDRNETLSS VLPLLNKDPL PQDFSVKMAS IFKEFVTTYN RTYGTQEEAQ
WRMSVFSNNM VRAQKIQALD RGTAQYGITK FSDLTEEEFR TIYLNPLLKE NRNKMMHLAK
SIGDHAPPEW DWRTKGAVTN VKNQGMCGSC WAFSVTGNVE GQWFLKQGDL LSLSEQELLD
CDKVDKACLG GLPSNAYLAI KNLGGLETED DYSYSGHLQT CSFSAKKAKV YINDSVELSQ
NEQKLAAWLA KKGPISVAIN AFGMQFYRRG ISHPLRPLCS PWLIDHAVLL VGYGNRSGIP
FWAIKNSWGT DWGEEGYYYL YRGSGACGVN AMASSAVVN
//