CLB10_ANOGA
ID CLB10_ANOGA Reviewed; 362 AA.
AC Q7QBP4;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=CLIP domain-containing serine protease B10 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000269|PubMed:33520733};
DE Contains:
DE RecName: Full=CLIP domain-containing serine protease B10 light chain {ECO:0000305};
DE Contains:
DE RecName: Full=CLIP domain-containing serine protease B10 heavy chain {ECO:0000305};
DE Flags: Precursor;
GN Name=CLIPB10 {ECO:0000303|PubMed:33520733};
GN Synonyms=1273735 {ECO:0000312|EnsemblMetazoa:AGAP029770-PA};
GN ORFNames=AgaP_AGAP003058 {ECO:0000312|EMBL:EAA08418.4};
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|Proteomes:UP000007062};
RN [1] {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).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH SRPN2,
RP PROTEOLYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=G3 {ECO:0000269|PubMed:33520733};
RX PubMed=33520733; DOI=10.3389/fcimb.2020.585986;
RA Zhang X., Li M., El Moussawi L., Saab S., Zhang S., Osta M.A., Michel K.;
RT "CLIPB10 is a Terminal Protease in the Regulatory Network That Controls
RT Melanization in the African Malaria Mosquito Anopheles gambiae.";
RL Front. Cell. Infect. Microbiol. 10:585986-585986(2020).
CC -!- FUNCTION: Serine protease which preferentially cleaves after arginine
CC residues (PubMed:33520733). Involved in the innate immune response
CC against parasite P.bergei infection by activating the melanization
CC cascade (PubMed:33520733). Probably in the hemolymph, cleaves and
CC activates prophenoloxidase (PPO), which functions in the formation of
CC pigments such as melanin and other polyphenolic compounds
CC (PubMed:33520733). In the susceptible strain G3, appears to be
CC dispensable for ookinete elimination which occurs by lysis
CC (PubMed:33520733). {ECO:0000269|PubMed:33520733}.
CC -!- ACTIVITY REGULATION: Inhibited by serpin SRPN2.
CC {ECO:0000269|PubMed:33520733}.
CC -!- SUBUNIT: Forms a covalent heterodimer with SRPN2; the interaction
CC inhibits CLIPB10 catalytic activity. {ECO:0000269|PubMed:33520733}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|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:0000255|PROSITE-ProRule:PRU01236}.
CC -!- PTM: Cleaved by an unknown protease into an active form.
CC {ECO:0000269|PubMed:33520733}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the susceptible strain
CC G3 infected with P.berghei does not affect the numbers of live oocysts
CC and melanized ookinetes in the midgut; however, severely reduces
CC ookinete melanization in a CTL4 RNAi-mediated knockdown background
CC (PubMed:33520733). Simultaneous RNAi-mediated knockdown of SRPN2 and
CC CLIPB10 in female, partially reduces the formation of abdominal
CC melanotic tumors caused by SRPN2 RNAi-mediated knockdown
CC (PubMed:33520733). {ECO:0000269|PubMed:33520733}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|RuleBase:RU366078}.
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DR EMBL; AAAB01008879; EAA08418.4; -; Genomic_DNA.
DR RefSeq; XP_312744.4; XM_312744.4.
DR MEROPS; S01.203; -.
DR EnsemblMetazoa; AGAP029770-RA; AGAP029770-PA; AGAP029770.
DR GeneID; 1273735; -.
DR KEGG; aga:AgaP_AGAP003058; -.
DR CTD; 1273735; -.
DR VEuPathDB; VectorBase:AGAP029770; -.
DR HOGENOM; CLU_006842_0_3_1; -.
DR InParanoid; Q7QBP4; -.
DR OMA; HENYRPR; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0140546; P:defense response to symbiont; IMP:UniProtKB.
DR GO; GO:0035008; P:positive regulation of melanization defense response; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:UniProtKB.
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; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..362
FT /note="CLIP domain-containing serine protease B10"
FT /evidence="ECO:0000255"
FT /id="PRO_5014588334"
FT CHAIN 20..109
FT /note="CLIP domain-containing serine protease B10 light
FT chain"
FT /evidence="ECO:0000250|UniProtKB:Q9XXV0"
FT /id="PRO_0000455767"
FT CHAIN 110..362
FT /note="CLIP domain-containing serine protease B10 heavy
FT chain"
FT /evidence="ECO:0000250|UniProtKB:Q9XXV0"
FT /id="PRO_0000455768"
FT DOMAIN 22..75
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 110..361
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT SITE 109..110
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9XXV0"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 23..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 33..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 39..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 140..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 285..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 310..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 362 AA; 40138 MW; BB77496E7621B81C CRC64;
MAKVVDCVLL LAFIAVVRGQ EACRTPDHRD GVCHPVQQCP SVRDEFFNSD RVLSEDEIDY
LRKLQCKTKD VTICCPDGVT TVDRNPTAVR DGLPNPKAFE CGLDTLADRI IGGNYTAIDE
FPWYALLEYQ SKKGERAFKC GGSLINGRYV LTAAHCLANK KLDEGERLVN VRLGEYNTAT
DTDCADGNPD DCADPPQNFG IEAQIVHPGY DKNGPYQHHD IALIRLDRDV TMNNFVSPVC
LPPDDFPPTS PGLNVTAVGF GHTGRQRHSG IKKKAQFPVF AQEECDKKWK NIEVIGEQLC
AGGVFGIDSC SGDSGGPLMV KRFYWIQEGV ISFGNQCALE GWPGVYTRVS SYLDWIRQNI
RR
