ID A0A087Y1P3_POEFO Unreviewed; 405 AA.
AC A0A087Y1P3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Cathepsin E-like {ECO:0000313|Ensembl:ENSPFOP00000011946.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011946.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000011946.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; AYCK01016792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007575554.1; XM_007575492.2.
DR AlphaFoldDB; A0A087Y1P3; -.
DR STRING; 48698.ENSPFOP00000011946; -.
DR MEROPS; A01.045; -.
DR Ensembl; ENSPFOT00000011963.2; ENSPFOP00000011946.2; ENSPFOG00000011897.2.
DR GeneID; 103154275; -.
DR KEGG; pfor:103154275; -.
DR CTD; 114367; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000164590; -.
DR OMA; CRVHQKF; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF37; CATHEPSINE-A-LIKE PROTEIN; 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; 1.
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:UP000028760};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001833857"
FT DOMAIN 82..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 286
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 113..118
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 277..281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 405 AA; 45263 MW; EF80340AE19C2121 CRC64;
MLRLLLLLLS TWTGSAMVRV ALMRVPSIRS QLRTQGLLED FLKDHRPDMF NRRYAQCFPP
GTPSLRLRRS SEKIYNFMDA QYYGEISVGT PPQNFSVIFD TGSADLWVPS SYCVSQACAF
HRRFKAFESK TFHHDGRSFG IHYGSGHLLG VMGRDTVKIG DMTILNQQFG ESVYEPGSAF
VTAKFDGVLG LAYQSLAEIL GNPVFDNMLA QKIVDQPVFS FYLSRRTRTS NPQGELLLGG
IDEAMYNGSI NWLPVSAKRY WQVEMDSVVV QGGSSFCPIG CHAIIDTGTS LIGGPTRDVL
RLQQLIGATP TNNGEFVIDC TRLSSLPRIT FILGGKEYTL TSEQYVRKEP FGISDLCFSG
FQAFDIISPE GPMWILGDVF LTEYYSIFDR GLDRIGLAQA RHPIE
//
