GenomeNet

Database: UniProt
Entry: Q17J64_AEDAE
LinkDB: Q17J64_AEDAE
Original site: Q17J64_AEDAE 
ID   Q17J64_AEDAE            Unreviewed;       493 AA.
AC   Q17J64;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN   Name=5573598 {ECO:0000313|EnsemblMetazoa:AAEL002124-PA};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL002124-PA, ECO:0000313|Proteomes:UP000008820};
RN   [1] {ECO:0000313|EnsemblMetazoa:AAEL002124-PA, ECO:0000313|Proteomes:UP000008820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL002124-PA,
RC   ECO:0000313|Proteomes:UP000008820};
RG   Aedes aegypti Genome Working Group (AGWG);
RA   Matthews B.J.;
RT   "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AAEL002124-PA}
RP   IDENTIFICATION.
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL002124-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036320};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU366078}.
CC   -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC       together usually by 3 conserved disulfide bonds forming a clip-like
CC       compact structure. {ECO:0000256|RuleBase:RU366078}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195, ECO:0000256|RuleBase:RU366078}.
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DR   RefSeq; XP_001654732.1; XM_001654682.2.
DR   AlphaFoldDB; Q17J64; -.
DR   MEROPS; S01.B33; -.
DR   PaxDb; 7159-AAEL002124-PA; -.
DR   EnsemblMetazoa; AAEL002124-RA; AAEL002124-PA; AAEL002124.
DR   GeneID; 5573598; -.
DR   KEGG; aag:5573598; -.
DR   VEuPathDB; VectorBase:AAEL002124; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_0_3_1; -.
DR   InParanoid; Q17J64; -.
DR   OMA; CIGPDNR; -.
DR   OrthoDB; 3026955at2759; -.
DR   Proteomes; UP000008820; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.30.1640.30; -; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR022700; CLIP.
DR   InterPro; IPR038565; CLIP_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF12032; CLIP; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00680; CLIP; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51888; CLIP; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366078};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366078}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU366078"
FT   CHAIN           24..493
FT                   /note="CLIP domain-containing serine protease"
FT                   /evidence="ECO:0000256|RuleBase:RU366078"
FT                   /id="PRO_5014308028"
SQ   SEQUENCE   493 AA;  53628 MW;  D4F7B7D48E9645B0 CRC64;
     MWILKLVIFT VLAVQSVYPQ ARSCYTPNGV IGVCQSLPNC PTLVRLYQYD RSRQTVNFLV
     ASQRNCGNRV SGGYPVLCCT DGVQYDPNPT TRSPFVEVPT TTTTTTTTTT TTTTPRPTTQ
     APTSLAPIRL ADCIGPDNKE GNCISLRACP SLLNEFLQRQ KDPEYVRFIQ QSNAICNYIQ
     PNVCCPLEAY TPAPPIPPPT VTPPAPPAPS TEGPTQPKNN ALTTLPTPAT GCGYSKVEHN
     RVVGGVPAAL HGWPWMALIG YKNALGEVSF KCGGSLITNR HVLTAAHCIR KDLSSVRLGE
     HDTSTDTETN HVDVAVVKME MHPSYDKKDG HSDLALLYLG EDVAFNDAVR PICMPISDPI
     RSRNFEGYTP FVAGWGRTQE GGKSANVLQE LQIPIIANGE CRNLYAKINK AFSDKQFDES
     VTCAGVLEGG KDSCQGDSGG PLMLPQRDGV DFYYYQIGVV SYGIGCARAE VPGVYTRVAK
     FVDWVKEKVN EPV
//
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