ID F1RIC8_PIG Unreviewed; 386 AA.
AC F1RIC8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=LOC100524300 {ECO:0000313|Ensembl:ENSSSCP00000013932.3};
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:ENSSSCP00000013932.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000013932.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000013932.3,
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:ENSSSCP00000013932.3}
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; F1RIC8; -.
DR SMR; F1RIC8; -.
DR STRING; 9823.ENSSSCP00000013932; -.
DR MEROPS; A01.051; -.
DR PaxDb; 9823-ENSSSCP00000013932; -.
DR Ensembl; ENSSSCT00000014318.4; ENSSSCP00000013932.3; ENSSSCG00000013098.5.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000153747; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; F1RIC8; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000013098; Expressed in lymph node.
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 74..383
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 105..110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 266..270
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 308..342
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 386 AA; 44135 MW; D7AABF7C74402D17 CRC64;
RVWVIVFHLL KMIELRIPLM KVKSIRENLR EKGLLENFLE EHPYDMIQNQ GSQNSTFKRK
VIRHRLRNYF DMIYVGNITV GTPPQQFSVV FDTGSTDLWV PSVYCHSMAC VTHNIFDPFQ
SSTFRFSATP IRLEYGSGMV SGFLGYDTVR IGRLIIMGQG FCITSWEESK TFEHAPFDGM
LGLGYASLGI RGVTPVFDNI KRRGFLDQPV FAFYLSTKSE QGSVVIFGGV DHRYYRGDLR
WVPLSKPHYW QIALDRISWR GYVIACKAGC QAIVDTGTSL LRGPNADVRN IQKLIGAHYF
HREYVIRCSA PDTLPDIVFT INNVQYPVPA RAYIRKNTNG ICLSNFKGLI GHFNREAIWI
LGDVFLRLYF TVFDRGQNRI GLATAV
//