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Database: UniProt
Entry: A2ICG6_MUSDO
LinkDB: A2ICG6_MUSDO
Original site: A2ICG6_MUSDO 
ID   A2ICG6_MUSDO            Unreviewed;       390 AA.
AC   A2ICG6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Aspartic proteinase AspMD03 {ECO:0000313|EMBL:ABM69086.1};
DE   SubName: Full=Lysosomal aspartic protease-like precursor {ECO:0000313|RefSeq:NP_001273807.1};
GN   Name=101894200 {ECO:0000313|EnsemblMetazoa:MDOA014422-PD};
GN   Synonyms=LOC101894200 {ECO:0000313|RefSeq:NP_001273807.1};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EMBL:ABM69086.1};
RN   [1] {ECO:0000313|EMBL:ABM69086.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Padilha M.H.P., Pimentel A.C., Terra W.R.;
RT   "Molecular cloning and functional characterization of an aspartic
RT   proteinase from Musca domestica.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABM69086.1, ECO:0000313|RefSeq:NP_001273807.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19815068; DOI=10.1016/j.ibmb.2009.09.003;
RA   Padilha M.H., Pimentel A.C., Ribeiro A.F., Terra W.R.;
RT   "Sequence and function of lysosomal and digestive cathepsin D-like
RT   proteinases of Musca domestica midgut.";
RL   Insect Biochem. Mol. Biol. 39:782-791(2009).
RN   [3] {ECO:0000313|RefSeq:NP_001273807.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26156588;
RA   Li D., Liang Y., Wang X., Wang L., Qi M., Yu Y., Luan Y.;
RT   "Transcriptomic Analysis of Musca domestica to Reveal Key Genes of the
RT   Prophenoloxidase-Activating System.";
RL   G3 (Bethesda) 5:1827-1841(2015).
RN   [4] {ECO:0000313|EnsemblMetazoa:MDOA014422-PD}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA014422-PD};
RG   EnsemblMetazoa;
RL   Submitted (JAN-2021) to UniProtKB.
RN   [5] {ECO:0000313|RefSeq:NP_001273807.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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; EF193385; ABM69086.1; -; mRNA.
DR   RefSeq; NP_001273807.1; NM_001286878.1.
DR   STRING; 7370.A2ICG6; -.
DR   MEROPS; A01.009; -.
DR   EnsemblMetazoa; MDOA014422-RD; MDOA014422-PD; MDOA014422.
DR   GeneID; 101894200; -.
DR   KEGG; mde:101894200; -.
DR   VEuPathDB; VectorBase:MDOA014422; -.
DR   OrthoDB; 1120702at2759; -.
DR   BRENDA; 3.4.23.5; 3486.
DR   Proteomes; UP000095301; Unassembled WGS sequence.
DR   Proteomes; UP000694905; Unplaced.
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; 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,
KW   ECO:0000313|RefSeq:NP_001273807.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001273807.1}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..390
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001273807.1"
FT                   /id="PRO_5038206371"
FT   DOMAIN          71..387
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        102..109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        309..346
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   390 AA;  42426 MW;  6CCDA8BE89DE9CBF CRC64;
     MIKFVILLSL VSLLLPESFA EEKLIRVPIQ KIKSARKHFY EVGTELQQLR LTYGAGGVTP
     EPLSNYLDAQ YYGPISIGTP PQDFKVVFDT GSSNLWVPSK KCHLTNIACL MHNKYDATKS
     KTFKQNGTEF AIHYGSGSLS GYLSTDTVNI GGLDIKDQTF AEALSEPGLV FVAAKFDGIL
     GLGYSSISVD GVKPPFYAMY EQGLISQPIF SFYLNRDPKA PEGGEIIFGG SDPDHYTGDF
     TYLPVTRKAY WQIKMDSASM GDLKCAKGGC QVIADTGTSL IALPPSEATS INQAIGGTPI
     MGGQYMVACE DIPKLPVIKF VLGGKTFELE GKDYVLRIAQ MGKTICLSGF MGIDIPPPNG
     PLWILGDVFI GKYYTEFDMG NDRVGFAIAK
//
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