ID A0A673X172_SALTR Unreviewed; 281 AA.
AC A0A673X172;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Pro-cathepsin H {ECO:0000256|ARBA:ARBA00039372};
GN Name=LOC115203334 {ECO:0000313|Ensembl:ENSSTUP00000014697.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000014697.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000014697.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Important for the overall degradation of proteins in
CC lysosomes. {ECO:0000256|ARBA:ARBA00037522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC Evidence={ECO:0000256|ARBA:ARBA00036517};
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR AlphaFoldDB; A0A673X172; -.
DR Ensembl; ENSSTUT00000015510.1; ENSSTUP00000014697.1; ENSSTUG00000006567.1.
DR GeneTree; ENSGT00940000160227; -.
DR Proteomes; UP000472277; Unplaced.
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; 2.
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; 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; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF642; PRO-CATHEPSIN H; 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; PS00640; THIOL_PROTEASE_ASN; 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:UP000472277};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..281
FT /note="Pro-cathepsin H"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025408455"
FT DOMAIN 30..85
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 111..278
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 281 AA; 31934 MW; 794705E43EEF86DD CRC64;
MALYTVAFIL AFLHLANFTP LFLPEEEYHF KQWMLQYNKV YDLEEYYHRL DIFTRHKRRI
DYHNAGKHTF SMGLNQFSDM SFAEFRKTFL LTEPQNCSAT KGSHISSHGP YPGSVDWREK
GNYVSPVKYQ GHCGSCWTFS TTGCLESVTA IATGKLPLLS EQQLVDCAQD FNNHGCMGLY
DEKGMVDAVA RLNPVSFGYE VTDDFLHYKD GVYSSTTCKN TTDNVNHAVL AVGYGEKNST
PYWIVKNSWG TNWGMDGYFL IERGRNMCGL AACSSYPLPP V
//
