ID A0A5J5CAD2_9PERO Unreviewed; 213 AA.
AC A0A5J5CAD2;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, 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 ORFNames=FQN60_009257 {ECO:0000313|EMBL:KAA8578438.1};
OS Etheostoma spectabile (orangethroat darter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Etheostomatinae; Etheostoma.
OX NCBI_TaxID=54343 {ECO:0000313|EMBL:KAA8578438.1, ECO:0000313|Proteomes:UP000327493};
RN [1] {ECO:0000313|EMBL:KAA8578438.1, ECO:0000313|Proteomes:UP000327493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EspeVRDwgs_2016 {ECO:0000313|EMBL:KAA8578438.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA8578438.1};
RA Moran R.L., Catchen J.M., Fuller R.C.;
RT "A chromosome-level genome assembly, high-density linkage maps, and genome
RT scans reveal the genomic architecture of hybrid incompatibilities
RT underlying speciation via character displacement in darters (Percidae:
RT Etheostominae).";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:KAA8578438.1}.
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DR EMBL; VOFY01000669; KAA8578438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5CAD2; -.
DR Proteomes; UP000327493; Unassembled WGS sequence.
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 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; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
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 SMART; SM00848; Inhibitor_I29; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 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:UP000327493};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 77..149
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
SQ SEQUENCE 213 AA; 24079 MW; 7D7BE49265071EFC CRC64;
MRCDAAFCFL RGRKCNSSCD TFIINRPINQ ENTIRGFKHT AAMTSPTDQR AMFASLLLVS
LCVGAAAMID SRLDDHWELW KKTHAKKYRN EYLTLCTLTV RLEVEEVRRR ELWEKNLMLI
TLHNLEASMG LHTYDLGMNH MGDLTQEEIL QSYATLSVPA DMQRAPSAFV GTSGTDVPDT
MDWRQKGCVT RVKMQGSCGS CWAFSAAGPW RAS
//
