ID F1RIE1_PIG Unreviewed; 369 AA.
AC F1RIE1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=LOC100522849 {ECO:0000313|Ensembl:ENSSSCP00000013929.4};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000013929.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000013929.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000013929.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000013929.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR AlphaFoldDB; F1RIE1; -.
DR SMR; F1RIE1; -.
DR STRING; 9823.ENSSSCP00000013929; -.
DR Ensembl; ENSSSCT00000014315.4; ENSSSCP00000013929.4; ENSSSCG00000058512.1.
DR GeneTree; ENSGT00940000153747; -.
DR HOGENOM; CLU_013253_5_2_1; -.
DR InParanoid; F1RIE1; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000008227; Chromosome 2.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF49; PEPSIN A-5; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 57..366
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 75
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 88..93
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 248..252
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 290..325
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 369 AA; 41369 MW; 8FC4B70401C2FCAA CRC64;
MALLGFVQIP LTKVKSVRES LREKGLLKNF LKEHPYKMIQ NQKIACHPLR NYLDMAYVGN
ITIGTPPQQF SVVFDTGSAD LWVPSVYCKS KACVTHRSFN PSHSSTFRLP GKNFELKYGS
GKISGFLGYD TVWIGSLRTM NQVFGLSQLE TGEAFEHGVF DGLLGLGFPS LALKGTTPIF
DNLKKQGQIS EPVFAFYLST KEEGSAVIFG GVDRSFYKGE LKWVPLTKPN YWQIALDRIT
WRGQIFGCPR GCQAIVDTGT TYLLGPHAEV DKIHSLMNAV PLQEEYLVHC NARDTYPDII
FTINNVDYPV PAHAYIRKDA NDILCYSTFE AMADTLTKSQ TWILGDVFLK VYFTVFDRGQ
NRIGLARAA
//