ID W5JHU4_ANODA Unreviewed; 426 AA.
AC W5JHU4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ETN63927.1};
GN ORFNames=AND_004346 {ECO:0000313|EMBL:ETN63927.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN63927.1};
RN [1] {ECO:0000313|EMBL:ETN63927.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN63927.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN63927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC004346-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR EMBL; ADMH02001148; ETN63927.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JHU4; -.
DR STRING; 43151.W5JHU4; -.
DR EnsemblMetazoa; ADAC004346-RA; ADAC004346-PA; ADAC004346.
DR VEuPathDB; VectorBase:ADAC004346; -.
DR VEuPathDB; VectorBase:ADAR2_011803; -.
DR eggNOG; KOG3627; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_036017_0_0_1; -.
DR OMA; GWRNGTN; -.
DR OrthoDB; 3473805at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF153; GH19262P-RELATED; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:ETN63927.1};
KW Protease {ECO:0000313|EMBL:ETN63927.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..426
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010155452"
FT DOMAIN 36..283
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 303..423
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
SQ SEQUENCE 426 AA; 47085 MW; ED49206CC1AB11ED CRC64;
MMLVCLCVLV LVNCSFLAVQ ATTQCGVRQF KVRRLLTNGY DTQPGDYPWH SAIFHLKPKR
EYVCGGTIIS PRAIVTSAHC VTLPNRNVVR DVDELLVKLG LYTLLEDTES VQEHSIARAT
MHNAFTHEAF QNDIALLITQ SQINFDSYVQ PACLPKRSLL RAAVPGIVLG WGYTEDMNVA
NVLRAASAPI VSHRECRESN SVAYGSLLDE TMFCAGWRNG TNPCNGDSGG GLFMQTDSGR
WILNGIVTVT AANRQNENAC STSDYTVFVD VAKYVTWIDQ QLQIRRAPTT KGCTCDSPKS
KRYVVHNNKP VTFFEAWRLC QHLGHGLATI TSKADSELIA AAINTSSSTT GPWWIGGTDL
GNEGIFTWIS TNKLVGHGTG YLDFSHHQPD NHSGKEHCLE IGRWGGVAWN DAPCEFKQNY
ICEYIS
//
