ID Q9DE45_SALFO Unreviewed; 383 AA.
AC Q9DE45;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Gastricsin {ECO:0000256|ARBA:ARBA00023821};
DE EC=3.4.23.3 {ECO:0000256|ARBA:ARBA00023796};
OS Salvelinus fontinalis (Brook trout) (Salmo fontinalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salvelinus.
OX NCBI_TaxID=8038 {ECO:0000313|EMBL:AAG35646.1};
RN [1] {ECO:0000313|EMBL:AAG35646.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11259249;
RA Bobe J., Goetz F.W.;
RT "An ovarian progastricsin is present in the trout coelomic fluid after
RT ovulation.";
RL Biol. Reprod. 64:1048-1055(2001).
CC -!- FUNCTION: Hydrolyzes a variety of proteins.
CC {ECO:0000256|ARBA:ARBA00023749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=More restricted specificity than pepsin A, but shows
CC preferential cleavage at Tyr-|-Xaa bonds. High activity on
CC hemoglobin.; EC=3.4.23.3; Evidence={ECO:0000256|ARBA:ARBA00023733};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; AF203473; AAG35646.1; -; mRNA.
DR AlphaFoldDB; Q9DE45; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05477; gastricsin; 1.
DR Gene3D; 6.10.140.60; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF72; GASTRICSIN; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:AAG35646.1};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..383
FT /note="Gastricsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004324727"
FT DOMAIN 69..380
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 271
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 100..105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 383 AA; 42159 MW; 02A7CB9752E464FC CRC64;
MKYLVIVLVC AVLAEGIHRI PLVKHKSIRE RMMEKGEHLP YQDPALKYFP DEFAGSTTMY
INNYADTTYY GAITIGTPPQ SFQVLFDTGS ANLWVDSVLC NTQACNTHTK FNPQQSSTYS
ANGETFYLPY GAGSLSGVFG YDTVNVGGII LTNQEIGLST DEPGQNFVVA QFDGILGLSY
PSISAGQETP VMDNMMSQNL LQANIFAFYM TRDGQQGSEL SFGEVDNTKY QGQIYWTPVT
SQTYWQIGIQ GFQINGQETG WCGQGCQAIV DTGTSMLTAP RQIMGTLMQS IGAQQDQYGQ
YTVNCNQINS LPTLTFTING INFPLPPSAY IQQNNQVCSV GITPTYLPSQ NGQPLWILGD
VFLMQYYSVY DRTSNQVGFA PAA
//
