CLB15_ANOGA
ID CLB15_ANOGA Reviewed; 364 AA.
AC Q9NAS9; Q7Q1D1;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=CLIP domain-containing serine protease B15 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
DE Contains:
DE RecName: Full=CLIP domain-containing serine protease B15 light chain {ECO:0000305};
DE Contains:
DE RecName: Full=CLIP domain-containing serine protease B15 heavy chain {ECO:0000305};
DE Flags: Precursor;
GN Name=CLIPB15 {ECO:0000303|PubMed:16188883};
GN Synonyms=ser3 {ECO:0000312|EMBL:CAB90818.1};
GN ORFNames=AGAP009844 {ECO:0000312|EMBL:EAA14160.5};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000312|EMBL:CAB90818.1};
RN [1] {ECO:0000312|EMBL:CAB90818.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, GLYCOSYLATION, PROTEOLYTIC
RP CLEAVAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16188883; DOI=10.1074/jbc.m506191200;
RA Volz J., Osta M.A., Kafatos F.C., Mueller H.M.;
RT "The roles of two clip domain serine proteases in innate immune responses
RT of the malaria vector Anopheles gambiae.";
RL J. Biol. Chem. 280:40161-40168(2005).
RN [2] {ECO:0000312|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Serine protease (By similarity). Plays a role in innate
CC immunity against infections by parasite P.berghei and by Gram-negative
CC bacteria such as E.coli (PubMed:16188883). In response to P.berghei
CC infection, contributes to the clearing of parasite ookinetes
CC independent of melanization, an innate immune response which consists
CC in the deposition of melanin pigments on invading pathogens and
CC parasites (PubMed:16188883). {ECO:0000250|UniProtKB:A0A126GUP6,
CC ECO:0000269|PubMed:16188883}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16188883}.
CC Note=Secreted in the hemolymph. {ECO:0000269|PubMed:16188883}.
CC -!- TISSUE SPECIFICITY: Expressed by a subpopulation of hemocytes.
CC {ECO:0000269|PubMed:16188883}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult females and to a lesser extent
CC in the second and third larval, and pupal stages.
CC {ECO:0000269|PubMed:16188883}.
CC -!- INDUCTION: Induced by infection with E.coli or S.aureus bacteria.
CC Induced by infection with P.berghei parasite following ookinete
CC invasion of the midgut cells. {ECO:0000269|PubMed:16188883}.
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:0000255|PROSITE-ProRule:PRU01236}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16188883}.
CC -!- PTM: Proteolytically cleaved. {ECO:0000305|PubMed:16188883}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the G3 strain reduces
CC survival following infection by E.coli bacteria but not following
CC infection by S.aureus bacteria. Following P.berghei infection, the
CC number of parasite oocysts in the gut is increased in the susceptible
CC G3 strain due to a failure to kill or/and lyse ookinetes (the motile
CC parasite zygote that enters the gut to form an oocyst). RNAi-mediated
CC knockdown in the refractory L3-5 strain results in an increase in the
CC number of killed and melanized ookinetes following P.berghei infection.
CC Simultaneous knockdown of lectin CTL4 in the G3 strain (but not in L3-5
CC strain) causes an increase in the number of developing oocysts and a
CC decrease in melanized ookinetes. {ECO:0000269|PubMed:16188883}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236}.
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 EMBL; AJ276486; CAB90818.1; -; mRNA.
DR EMBL; AAAB01008980; EAA14160.5; -; Genomic_DNA.
DR RefSeq; XP_318957.5; XM_318957.5.
DR AlphaFoldDB; Q9NAS9; -.
DR SMR; Q9NAS9; -.
DR STRING; 7165.AGAP009844-PA; -.
DR MEROPS; S01.449; -.
DR PaxDb; Q9NAS9; -.
DR GeneID; 1279262; -.
DR KEGG; aga:AgaP_AGAP009844; -.
DR CTD; 1279262; -.
DR VEuPathDB; VectorBase:AGAP009844; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_3_1; -.
DR InParanoid; Q9NAS9; -.
DR OMA; SRPNDIC; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9NAS9; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0042832; P:defense response to protozoan; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.1640.30; -; 1.
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 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; SSF50494; 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Protease; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..364
FT /note="CLIP domain-containing serine protease B15"
FT /evidence="ECO:0000255"
FT /id="PRO_5013536761"
FT CHAIN 20..106
FT /note="CLIP domain-containing serine protease B15 light
FT chain"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT /id="PRO_0000455752"
FT CHAIN 107..364
FT /note="CLIP domain-containing serine protease B15 heavy
FT chain"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT /id="PRO_0000455753"
FT DOMAIN 30..89
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 107..359
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT SITE 106..107
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 41..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 47..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 137..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 279..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 306..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 364 AA; 40555 MW; 1FBF903BA5B61C89 CRC64;
MRWLVCLIVS WCSLVPLGAT VGQSLNSGDP CQTPSGTAGT CEPVKNCSYV RKILKSPDFS
HYDTTYLDTL KCGDLMVPMR KKPIPLLCCP KFSNSPTCGA QQLADRIYFG EETERGAHPW
AALLFYNVGR NRTVPKCGGA LISERYVITA AHCTVDKPNW KLLYVRFNEF NTSSADNCTT
ENDEVICRED YAVESIVPHP EYDMHNISRP NDICILRLAS DVTFNDYVRP ICLPFDPDVQ
QLPIVDEIFT VTGWGETEDR RPSDTQKHVE LPGLEHEACN SVYAVANVTL SDKQLCIGGL
NGSDSCRGDS GGPLMREVRG GWFLIGVVSF GARFCGTQNL PGVYTNVAKY LDWMETVMFV
ERYL
