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Database: UniProt
Entry: F1RIE1_PIG
LinkDB: F1RIE1_PIG
Original site: F1RIE1_PIG 
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
//
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