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Database: UniProt
Entry: M3YPZ3_MUSPF
LinkDB: M3YPZ3_MUSPF
Original site: M3YPZ3_MUSPF 
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
//
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