ID A0A182RQF3_ANOFN Unreviewed; 403 AA.
AC A0A182RQF3; A0A4Y0BIB2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=CLIP domain-containing serine protease {ECO:0000256|RuleBase:RU366078};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU366078};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN018674-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|EnsemblMetazoa:AFUN018674-PA, ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN018674-PA,
RC ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN018674-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN018674-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A182RQF3; -.
DR STRING; 62324.A0A4Y0BIB2; -.
DR EnsemblMetazoa; AFUN018674-RA; AFUN018674-PA; AFUN018674.
DR VEuPathDB; VectorBase:AFUN008495; -.
DR VEuPathDB; VectorBase:AFUN018674; -.
DR VEuPathDB; VectorBase:AFUN2_002434; -.
DR Proteomes; UP000075900; 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 PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF148; SERINE PROTEASE GRASS; 1.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU366078};
KW Protease {ECO:0000256|RuleBase:RU366078};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366078};
KW Serine protease {ECO:0000256|RuleBase:RU366078};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366078}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT CHAIN 22..403
FT /note="CLIP domain-containing serine protease"
FT /evidence="ECO:0000256|RuleBase:RU366078"
FT /id="PRO_5039734388"
FT DOMAIN 144..402
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 403 AA; 44293 MW; FA6011CABC6A1A1D CRC64;
MGFQRVLVAC LLITTFSGVI SQEDPKCETP TKSDGFCVSI ERCRNIHSIV TSPTPPPRGV
QNYINRAACT QPGVERSVCC QPLEIIPKPV TTTTTTTRAP PVNIPVQTGT GLVMTVGVEP
DSSTTLDWSL LPTTNCGTIT INRIAHGNAT RVFEYPWMVL LRYLSNGNLQ DGCGGSLINN
RYVLTAAHCI KTSSRLQLAK VRLGEHDKRQ HEDCHVYNDG EIECADPAID VDIESTVVHK
NYNRPIKFRH DIGLIRMAQE VEFTDSIKPI CLPVNEAVRR KVLTKYIITG WGTTEEQSLS
DVLLQAIVNH VEVPECQQKM TENFLYVTLA EEWQMCAAGE GLVDSCQGDS GGPLGFSVDV
SGARFVQFGI VSAGVRSCGK ENVPGIYTRV SSYMDWIVAN MKP
//
