ID   Q66GQ8_ARATH            Unreviewed;       426 AA.
AC   Q66GQ8;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=At5g22850 {ECO:0000313|EMBL:AAU05467.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:AAU05467.1};
RN   [1] {ECO:0000313|EMBL:AAU05467.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAV59285.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; BT015344; AAU05467.1; -; mRNA.
DR   EMBL; BT020219; AAV59285.1; -; mRNA.
DR   AlphaFoldDB; Q66GQ8; -.
DR   MEROPS; A01.A56; -.
DR   ExpressionAtlas; Q66GQ8; baseline and differential.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05476; pepsin_A_like_plant; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034161; Pepsin-like_plant.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR   PANTHER; PTHR13683:SF375; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022750};
KW   Protease {ECO:0000256|ARBA:ARBA00022750}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..426
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010141281"
FT   DOMAIN          81..426
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   426 AA;  45326 MW;  FE368DCAE9D91564 CRC64;
     MAAIRFAAAI LICCLLPAAV LSYGFPAALK LERVIPANHE MELSQLKARD EARHGRLLQS
     LGGVIDFPVD GTFDPFVVGL YYTKLRLGTP PRDFYVQVDT GSDVLWVSCA SCNGCPQTSG
     LQIQLNFFDP GSSVTASPIS CSDQRCSWGI QSSDSGCSVQ NNLCAYTFQY GDGSGTSGFY
     VSDVLQFDMI VGSSLVPNST APVVFGCSTS QTGDLVKSDR AVDGIFGFGQ QGMSVISQLA
     SQGIAPRVFS HCLKGENGGG GILVLGEIVE PNMVFTPLVP SQPHYNVNLL SISVNGQALP
     INPSVFSTSN GQGTIIDTGT TLAYLSEAAY VPFVEAITNA VSQSVRPVVS KGNQCYVITT
     SVGDIFPPVS LNFAGGASMF LNPQDYLIQQ NNVASALCFL GRYCSVVHRF SKDTESRDND
     PWRFGS
//