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Database: UniProt/TrEMBL
Entry: A7USI2_ANOGA
LinkDB: A7USI2_ANOGA
Original site: A7USI2_ANOGA 
ID   A7USI2_ANOGA            Unreviewed;       361 AA.
AC   A7USI2;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 89.
DE   SubName: Full=AGAP000315-PA {ECO:0000313|EMBL:EDO64345.2};
GN   Name=CLIPC6 {ECO:0000313|EMBL:EDO64345.2};
GN   Synonyms=5666762 {ECO:0000313|EnsemblMetazoa:AGAP000315-PA};
GN   ORFNames=AgaP_AGAP000315 {ECO:0000313|EMBL:EDO64345.2};
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:0000313|EMBL:EDO64345.2};
RN   [1] {ECO:0000313|EMBL:EDO64345.2, ECO:0000313|Proteomes:UP000007062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EDO64345.2,
RC   ECO:0000313|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:0000313|EMBL:EDO64345.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EDO64345.2};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EDO64345.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EDO64345.2};
RX   PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA   Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT   "The Anopheles gambiae genome: an update.";
RL   Trends Parasitol. 20:49-52(2004).
RN   [4] {ECO:0000313|EMBL:EDO64345.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EDO64345.2};
RX   PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA   Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA   Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT   "Update of the Anopheles gambiae PEST genome assembly.";
RL   Genome Biol. 8:R5.1-R5.13(2007).
RN   [5] {ECO:0000313|EMBL:EDO64345.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EDO64345.2};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EnsemblMetazoa:AGAP000315-PA}
RP   IDENTIFICATION.
RC   STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP000315-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195}.
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DR   EMBL; AAAB01008846; EDO64345.2; -; Genomic_DNA.
DR   RefSeq; XP_001687772.2; XM_001687720.2.
DR   AlphaFoldDB; A7USI2; -.
DR   STRING; 7165.A7USI2; -.
DR   PaxDb; 7165-AGAP000315-PA; -.
DR   EnsemblMetazoa; AGAP000315-RA; AGAP000315-PA; AGAP000315.
DR   GeneID; 5666762; -.
DR   KEGG; aga:AgaP_AGAP000315; -.
DR   CTD; 5666762; -.
DR   VEuPathDB; VectorBase:AGAP000315; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_0_3_1; -.
DR   InParanoid; A7USI2; -.
DR   OMA; AAHCIPT; -.
DR   OrthoDB; 3676963at2759; -.
DR   Proteomes; UP000007062; Chromosome X.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.30.1640.30; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24260; -; 1.
DR   PANTHER; PTHR24260:SF135; CLIP DOMAIN-CONTAINING SERINE PROTEASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007062};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..361
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014565975"
FT   DOMAIN          30..77
FT                   /note="Clip"
FT                   /evidence="ECO:0000259|PROSITE:PS51888"
FT   DOMAIN          107..360
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   361 AA;  39560 MW;  F42ED8EAAF68C687 CRC64;
     MLRHVASIGL LLLLVLTGGA LCQTLYEGDP CELRDGSAGV CTDATDCPWF LEVIVKNRRF
     ADRVSCGFDG LTEVICCKTN GTRPLGVRSR LACEQVPKYT SRLTFHIIDG EEASEGEFPF
     MAALGYPTDD ETQQNISYRC GASMISTDFL LTAAHCIPTN DRPTVAILGT NNLAPGNHGV
     LVGLKAFFPH PDYRTNRNYH DIALVQLERR IENEPDVNPI CLNDDLSDLP EDTVLTAEGY
     GIIDLDRNLR SNQLMKVNLT TVPWQKCNQT FADSNLLKNN RKLPQGIVAT QYCATGRENE
     EKKVVGDTCQ GDSGGPLQIM DDGKYKLVGV TSFGNGCGSN TPSVSTRVAA YIDWIESIVW
     A
//
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