ID B0WQE7_CULQU Unreviewed; 375 AA.
AC B0WQE7;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU363034};
GN Name=6041708 {ECO:0000313|EnsemblMetazoa:CPIJ009625-PA};
GN ORFNames=CpipJ_CPIJ009625 {ECO:0000313|EMBL:EDS32818.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS32818.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS32818.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ009625-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ009625-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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 EMBL; DS232039; EDS32818.1; -; Genomic_DNA.
DR RefSeq; XP_001850931.1; XM_001850879.1.
DR AlphaFoldDB; B0WQE7; -.
DR STRING; 7176.B0WQE7; -.
DR MEROPS; S01.201; -.
DR EnsemblMetazoa; CPIJ009625-RA; CPIJ009625-PA; CPIJ009625.
DR KEGG; cqu:CpipJ_CPIJ009625; -.
DR VEuPathDB; VectorBase:CPIJ009625; -.
DR VEuPathDB; VectorBase:CQUJHB010724; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_3_1; -.
DR InParanoid; B0WQE7; -.
DR OMA; NHPLVCC; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
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; -; 1.
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; PTHR24256:SF537; RE37738P-RELATED; 1.
DR PANTHER; PTHR24256; TRYPTASE-RELATED; 1.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51888; CLIP; 1.
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|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366078}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 26..375
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5011408367"
FT DOMAIN 28..83
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 112..374
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 375 AA; 40649 MW; 9D5D2705F4B004E7 CRC64;
MTSSRGSLWT SLGLLGVILV VVVQGQEVCN APDGKPGRCI LLRSCNSLFA LIKKKPLEQE
DRAFLSRSQC GWSRTENHPL VCCSDPLETP IRVGASLLPA VGVCGIQTSD RIIGGTNTKI
DEFPWLALLK YAKPNDLFGF HCGGVLINDR YVLTASHCVN GRDIPTTWNL VEVRLGEWDT
STEQDCEGLG VDADCSPDPI DVVIENKLPH PQYNPQSTEQ YNDIALLRLA SRVSYSDFIK
PICLPRSADL REKSIVGLKL QVAGWGRTAT ARYSAVKQKV GVDGVDLARC NQVYQKESVT
LLDGQLCAGG ISGKDSCQGD SGGPLMGVAT SGNVQFWYLA GLVSFGPTPC GQEGWPGVYT
KVAKYIDWVE NSLQP
//
