ID S4PGV2_9NEOP Unreviewed; 401 AA.
AC S4PGV2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=CathD {ECO:0000313|EMBL:JAA89073.1};
OS Pararge aegeria (speckled wood butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Parargina; Pararge.
OX NCBI_TaxID=116150 {ECO:0000313|EMBL:JAA89073.1};
RN [1] {ECO:0000313|EMBL:JAA89073.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA89073.1};
RX PubMed=23622113; DOI=10.1186/1471-2164-14-283;
RA Carter J.M., Baker S.C., Pink R., Carter D.R., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RT "Unscrambling butterfly oogenesis.";
RL BMC Genomics 14:283-283(2013).
RN [2] {ECO:0000313|EMBL:JAA89073.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA89073.1};
RA Carter J.-M., Baker S.C., Pink R., Carter D.R.F., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GAIX01003487; JAA89073.1; -; Transcribed_RNA.
DR AlphaFoldDB; S4PGV2; -.
DR MEROPS; A01.009; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1960; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}.
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..120
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 277..281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 320..357
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 401 AA; 42888 MW; C7275CFBE2623841 CRC64;
MFVNFAESGR DLQFAVKMKK TFVLLLALAT CAAGFSRVPL FRMKTVRKHL HEVGTELHMV
RIKYAASGPA PEPLSNYLDA QYYGPISIGS PPQTFKVVFD TGSSNLWVPS KKCHYTNIAC
LLHNKYDSSK SASYRKNDTD FAIHYGSGSL SGFLSTDDVA VGGLTVRAQT FAEAMSEPGL
AFVAAKFDGI LGMAFSSIAV DGVTPVFDNM LAQGLVPRPV FSFYLNRDPA AAQGGEIILG
GSDPAHFRGN FTRVPLTKDT YWQFTVDAVR VRGAAFCEGG CQAIADTGTS LIGGPAAEVA
RLNAALGATP IAFGQFAVDC SLVPALPPVR FSIAGRDFEL EGADYVLRVS QFGKTVCLSG
FMGLDVPPPN GPLWILGDVF IGKYYTEFDM GGRSIGFATA A
//
