ID A3F4M4_CAPHI Unreviewed; 381 AA.
AC A3F4M4;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 22-FEB-2023, entry version 61.
DE SubName: Full=Preprochymosin {ECO:0000313|EMBL:ABN13683.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|EMBL:ABN13683.1};
RN [1] {ECO:0000313|EMBL:ABN13683.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang X.Q., Yang B.J., Luo J., Tang G.F., Li W.G., Zhang L.J.;
RT "Cloning and sequence analyses of preprochymosin cDNA of Xinong Saanen
RT goat.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; EF199763; ABN13683.1; -; mRNA.
DR AlphaFoldDB; A3F4M4; -.
DR MEROPS; A01.006; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05478; pepsin_A; 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; IPR034162; Pepsin_A.
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:SF13; CHYMOSIN; 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 Digestion {ECO:0000256|ARBA:ARBA00022757};
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..381
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002652798"
FT DOMAIN 74..378
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 274
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 105..110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 265..269
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 308..341
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 381 AA; 42093 MW; F6558456C9482D19 CRC64;
MRCLVVLLAV FALSHGAEIT RIPLYKGKPL RKALKERGLL EDFLQKQQYG VSSEYSGFGE
VANVPLTNYL DSQYFGKIYL GTPPQEFTVL FDTGSSDFWV PSIYCKSNAC KNHQRFDPRK
SSTFQNLGKP LSIRYGTGSM QGILGYDTVT VSNIVDTQQT VGLSTQEPGD VFTYAEFDGI
LGMAYPSLAS EYSVPVFDNM MDRHLVAQDL FSVYMDRNGQ GSMLTLGAID PSYYTGSLHW
VPVTLQKYWQ FTVDSVTISG AVVACEGGCQ AILDTGTSKL VGPSSDILNI QQAIGATQNQ
YGEFDVDCDS LSSMPTVVFE INGKMYPLTP YAYTSQEEGF CTSGFQGENH SHQWILGDVF
IREYYSVFDR ANNLVGLAKA I
//
