ID D3PHU2_LEPSM Unreviewed; 384 AA.
AC D3PHU2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Lysosomal aspartic protease {ECO:0000313|EMBL:ADD38128.1};
GN Name=ASPP {ECO:0000313|EMBL:ADD38128.1};
GN Synonyms=Dvir\GJ21122 {ECO:0000313|EMBL:CDW38642.1};
OS Lepeophtheirus salmonis (Salmon louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Hexanauplia; Copepoda; Siphonostomatoida; Caligidae; Lepeophtheirus.
OX NCBI_TaxID=72036 {ECO:0000313|EMBL:ADD38128.1};
RN [1] {ECO:0000313|EMBL:ADD38128.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Atlantic form {ECO:0000313|EMBL:ADD38128.1};
RC TISSUE=Mixed tissue {ECO:0000313|EMBL:ADD38128.1};
RA Yasuike M., von Schalburg K., Cooper G., Leong J., Nilsen F., Jones S.R.M.,
RA Koop B.F.;
RT "Atlantic Lepeophtheirus salmonis ESTs and full-length cDNAs.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW38642.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole organism {ECO:0000313|EMBL:CDW38642.1};
RA Chronopoulou M.;
RL Submitted (MAY-2014) 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; BT121198; ADD38128.1; -; mRNA.
DR EMBL; HACA01021281; CDW38642.1; -; Transcribed_RNA.
DR AlphaFoldDB; D3PHU2; -.
DR MEROPS; A01.009; -.
DR EnsemblMetazoa; EMLSAT00000011388; EMLSAP00000011388; EMLSAG00000011388.
DR OMA; HDEMCRV; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
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, ECO:0000313|EMBL:ADD38128.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..384
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013521885"
FT DOMAIN 65..381
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 96..103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 260..264
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 303..340
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 384 AA; 42094 MW; 4A4749ED65A04342 CRC64;
MKFALWGLLF LFGLSAGLVR VPVHKFQSAR KHFYEVGSSI QLIRKRWNTV GAHPEPLSNY
LDAQYYGPIT IGSPPQSFKV IFDTGSSNLW IPSKSCHITN IACLLHHKYD HSKSSTYVAN
GTEFAIQYGS GSLSGFLSSD SVSMGEVEIG SQTFGEAMSE PGMAFVAAKF DGILGMGYSN
IAVDGVVPPF YNMFKQGLIQ EPIFSFYLNR NPDAKVGGEI IFGGSDPDHY KGNITYIPVT
KKGYWQFKMD KMEVNSKSFC QNGCQAIADT GTSLIAGPSI EVNALNQLLG GTPIINGEYM
FNCEDIPNLP PITFTIGGEE FVLSGEDYVM QITQFGKTVC LSGFMGLDVP EPMGPIWILG
DVFIGRYYTV FDMGKDRVGF AQSK
//
