ID M3YPZ3_MUSPF Unreviewed; 389 AA.
AC M3YPZ3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Gastricsin {ECO:0000256|ARBA:ARBA00023821};
DE EC=3.4.23.3 {ECO:0000256|ARBA:ARBA00023796};
GN Name=PGC {ECO:0000313|Ensembl:ENSMPUP00000013401.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000013401.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000013401.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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; AEYP01006181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004739990.1; XM_004739933.1.
DR AlphaFoldDB; M3YPZ3; -.
DR STRING; 9669.ENSMPUP00000013401; -.
DR MEROPS; A01.003; -.
DR Ensembl; ENSMPUT00000013616.1; ENSMPUP00000013401.1; ENSMPUG00000013503.1.
DR KEGG; mpuf:101693498; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000160626; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; M3YPZ3; -.
DR OMA; GFWTIDI; -.
DR OrthoDB; 1120702at2759; -.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0002803; P:positive regulation of antibacterial peptide production; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..389
FT /note="Gastricsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004045518"
FT DOMAIN 73..386
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 104..109
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 389 AA; 42268 MW; 5CA35D55166128B7 CRC64;
MEWMVVALVS FQLLEAAVIK VPLRKLEPVR ATMKEKGLLG EFLRTHKNDP AQKYHVGDLG
MVYEPLAYLD SLYLGEIAIG TPPQNFLVLF DTGSSSLWVP SVQCQSQACA THSRFNPNAS
STYSSHGQTF SVQYGSGSLR GVYGYDTLRV QSAQVPNQQF GLSEHEPSPY FLQFKFDGIM
GLAYPALAEG RSATALQGLL QAGLLSSPVF SFYLGRGMSS QNGAVLIFGG IDHSLHSGPI
YWAPVTQERY WQIGIEEFLI GGHATGWCSQ GCQAIVDTGT SPLTVPQQYL SALLQATGAQ
ADQYGQFTVD CNNIQNLPTL TFLISGVHFS LPYHSYVFTG NGVCTIAVQA TYLPSSSGQS
LWILGGVFLR SYYSIFDIGN NRVGFATAA
//