ID A0A673AAA8_9TELE Unreviewed; 338 AA.
AC A0A673AAA8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Cathepsin S {ECO:0000256|ARBA:ARBA00039679};
DE EC=3.4.22.27 {ECO:0000256|ARBA:ARBA00038916};
GN Name=LOC115435570 {ECO:0000313|Ensembl:ENSSORP00005025648.1};
OS Sphaeramia orbicularis (orbiculate cardinalfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005025648.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005025648.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to cathepsin L, but with much less activity on Z-Phe-
CC Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.;
CC EC=3.4.22.27; Evidence={ECO:0000256|ARBA:ARBA00035956};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome
CC {ECO:0000256|ARBA:ARBA00004262}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR AlphaFoldDB; A0A673AAA8; -.
DR Ensembl; ENSSORT00005026412.1; ENSSORP00005025648.1; ENSSORG00005012332.1.
DR InParanoid; A0A673AAA8; -.
DR OrthoDB; 5472948at2759; -.
DR Proteomes; UP000472271; Unplaced.
DR GO; GO:0045335; C:phagocytic vesicle; 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; 3.90.70.10; Cysteine proteinases; 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; 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:SF525; CATHEPSIN S; 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; 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 Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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:UP000472271};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..338
FT /note="Cathepsin S"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025461006"
FT DOMAIN 35..95
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 123..337
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 338 AA; 37227 MW; AF9477A6FB11EA08 CRC64;
MSPTQQGLVV LGGWLLVCWC VGVAAEFDGR LDWHWELWKK THEKKYHTEA EEVSRRELWE
KNVLLITTHN LEASLGLHSY TLSMNHMGDL TTEEILQSFA TLRPPTDLQR APSALTGTSG
ADIPDTVDWR QKGCVTSVKM QGSCGSCWAF SAAGALEGLL ARTTGKLVDL SPQNLVDCST
KYGNHGCNGG FMHKAFQYVI DNPGIDSDAS YPYRGVEQQC RYNPAYRAAN CSGYRWVPQG
NEDALKQALA SVGPVSVAID ATRTQFIFYS SGVYDDPGCS QRVNHGVLAV GYGTLNGQDY
WLVKNSWGQT FGEGGYIRMA RNKNDQCGIA LYAVYPVL
//
