ID A0A182MQ48_9DIPT Unreviewed; 562 AA.
AC A0A182MQ48;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:ACUA023599-PA};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA023599-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA023599-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA023599-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR EMBL; AXCM01004414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182MQ48; -.
DR STRING; 139723.A0A182MQ48; -.
DR EnsemblMetazoa; ACUA023599-RA; ACUA023599-PA; ACUA023599.
DR VEuPathDB; VectorBase:ACUA023599; -.
DR OrthoDB; 3412813at2759; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF136; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS51888; CLIP; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..562
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034397051"
FT DOMAIN 246..294
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 338..556
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 562 AA; 63791 MW; 41706069AA212C2D CRC64;
MSSMYRCVLF GLLALMIVGA SESSNPQEYD GRSMLQDFRN RFMTYEHIEI DECPLKYLRT
VYSDFCHVAL IKKNASTCLG VLVNDYYILS TAECVPEDWK SLHVQLQNNF DLPIADRLVY
EDYKSLNVSS EKAPVLLRIN GTTEVQDVGY DSTLNYLIQN TTVCSASMQE VCLNKTFTQW
CERNPTGSLL QIRDLDKYSM HPMVVGLFCN EQQQLVPVSR YAHWIRDVIA RDRILFAIPD
AGLGEKCITK NDKEGVCLRI DACPKVLKQL KSVARHLTAL EQCGFDGDQP LNCCTPDDML
KSEDKREKLQ SITHEIEHCH ELYDVYRRTT KEQQFHSQLA LIRDAANRVE CVGTLISKQF
VLTAAQCVLR IKSKSSTVQL GITALHEKAV QTLNVVSTLI HPMFDHQTNH YNIAILTLEA
PVTITEYSVP ACMWPDKDRM PAKLITTGYD TVANAVTVST VNPLYYIDCR LKYYSNLTLT
EACILPDMDK VYCDEEPMAC AESGTGLYGT VYMSSDWRPV NYVVGIYSIG AQCAQSKPAI
YTRVSEYYPW IKAQLYLMAQ DL
//
