CLA30_ANOGA
ID CLA30_ANOGA Reviewed; 416 AA.
AC A0A1S4HE51;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Inactive CLIP domain-containing serine protease A30 {ECO:0000305};
DE AltName: Full=Inactive CLIP domain-containing serine protease SPCLIP1 {ECO:0000305};
DE Flags: Precursor;
GN Name=SPCLIP1 {ECO:0000303|PubMed:24039584}; Synonyms=CLIPA30 {ECO:0000305};
GN ORFNames=AGAP028725 {ECO:0000305};
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, INTERACTION WITH TEP1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=G3 {ECO:0000269|PubMed:24039584};
RX PubMed=24039584; DOI=10.1371/journal.ppat.1003623;
RA Povelones M., Bhagavatula L., Yassine H., Tan L.A., Upton L.M., Osta M.A.,
RA Christophides G.K.;
RT "The CLIP-domain serine protease homolog SPCLIP1 regulates complement
RT recruitment to microbial surfaces in the malaria mosquito Anopheles
RT gambiae.";
RL PLoS Pathog. 9:e1003623-e1003623(2013).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=G3 {ECO:0000269|PubMed:33045027};
RX PubMed=33045027; DOI=10.1371/journal.ppat.1008985;
RA Sousa G.L., Bishnoi R., Baxter R.H.G., Povelones M.;
RT "The CLIP-domain serine protease CLIPC9 regulates melanization downstream
RT of SPCLIP1, CLIPA8, and CLIPA28 in the malaria vector Anopheles gambiae.";
RL PLoS Pathog. 16:e1008985-e1008985(2020).
CC -!- FUNCTION: Probable inactive serine protease which plays an essential
CC role in the innate immune response against bacteria and protozoa
CC infection by activating the melanization cascade (PubMed:24039584,
CC PubMed:33045027). Binds to the surface of parasite P.berghei ookinetes
CC and bacterium E.coli where it promotes the accumulation of mature TEP1
CC which leads to the melanization of the microbe (PubMed:24039584,
CC PubMed:33045027). {ECO:0000269|PubMed:24039584,
CC ECO:0000269|PubMed:33045027}.
CC -!- SUBUNIT: Interacts with mature TEP1 and to a lesser extent with full-
CC length TEP1; the interaction is induced by microbial infection.
CC {ECO:0000269|PubMed:24039584}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24039584,
CC ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph.
CC {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}.
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:0000250|UniProtKB:P21902}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown increases the number of
CC P.berghei oocysts in the mosquito midgut (PubMed:24039584). In the
CC hemolymph, prevents the cleavage of TEP1 into its mature form thereby
CC preventing TEP1 binding to the surface of bacterium E.coli or parasite
CC P.berghei ookinetes (PubMed:24039584). In response to E.coli infection,
CC cleavage of CLIPA8, CLIPA28 and CLIPC9 in the hemolymph is impaired and
CC phenoloxidase (PO) activity is severely decreased (PubMed:24039584,
CC PubMed:33045027). Also reduces E.coli melanization (PubMed:33045027).
CC {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although it belongs to peptidase S1 family, the residues
CC corresponding to the serine protease catalytic triad (Asp-His-Ser) are
CC not conserved suggesting that SPCLIP1 lacks catalytic activity.
CC {ECO:0000305|PubMed:24039584}.
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DR EMBL; AAAB01008986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EnsemblMetazoa; AGAP028725-RA; AGAP028725-PA; AGAP028725.
DR VEuPathDB; VectorBase:AGAP028725; -.
DR OMA; SENICTT; -.
DR OrthoDB; 997013at2759; -.
DR Proteomes; UP000007062; Chromosome 3L.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0140367; P:antibacterial innate immune response; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0140546; P:defense response to symbiont; IMP:UniProtKB.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0035008; P:positive regulation of melanization defense response; IMP:UniProtKB.
DR GO; GO:0010954; P:positive regulation of protein processing; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR041515; PPAF-2_Clip.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF18322; CLIP_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Reference proteome; Secreted; Serine protease homolog; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..416
FT /note="Inactive CLIP domain-containing serine protease A30"
FT /evidence="ECO:0000255"
FT /id="PRO_5010387236"
FT DOMAIN 48..97
FT /note="Clip"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT DOMAIN 147..399
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 49..95
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT DISULFID 56..88
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT DISULFID 62..96
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT DISULFID 184..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 282..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 312..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 343..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 416 AA; 46590 MW; C37CD56AD9130320 CRC64;
MAFSLRIGIR TTDSKRCLVL LVLVVLLTVL ACLPPSVEGN FPVGKFRRCN NNKGICVSRE
QCLNGQINTV GHTQIEPRLL NDDDIDECDV YGMQCCNLPS TNVPADSDEE EQEEEEKEKK
GGTVTTTTTE EPDDPDWSRQ CGQRTDVTER ADQDGETNRF EFPWSVALFS KAQFFGKVRK
EFLCGGTLID DYLVLTAARC VNQKDRNTLV VQLGRWNLDA GKESRMQEIA VEELIIHRGY
VLSSHLHNVA LLVLANGAQL GRAANRVCLP DHSVQFGPDT LCYVVGWSNS PSPNTSNRQL
KLRSMVAPVQ ECTATIRRST GAWDFRLLSE NICTTYLDDT VPCERAPGSG FVCESPTLPG
QYFLVGIASY AVRQCHKYRA HDVFVHVPDY IEWVDGHVVN QSRQTSFYRP DPISFD
