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DEFA_AEDAE
ID   DEFA_AEDAE              Reviewed;          98 AA.
AC   P91793; O77250; P91794; P91795; P91796; Q17EE3; Q6ITZ2; Q963E9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Defensin-A;
DE   AltName: Full=AaDef;
DE   Flags: Precursor;
GN   Name=DEFA; ORFNames=AAEL003841;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Koashiung;
RX   PubMed=8814787; DOI=10.1016/0965-1748(95)00108-5;
RA   Cho W.-L., Fu Y.-C., Chen C.-C., Ho C.-M.;
RT   "Cloning and characterization of cDNAs encoding the antibacterial peptide,
RT   defensin A, from the mosquito, Aedes aegypti.";
RL   Insect Biochem. Mol. Biol. 26:395-402(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Liverpool; TISSUE=Fat body;
RX   PubMed=9927179; DOI=10.1046/j.1365-2583.1999.810107.x;
RA   Lowenberger C.A., Smartt C.T., Bulet P., Ferdig M.T., Severson D.W.,
RA   Hoffmann J.A., Christensen B.M.;
RT   "Insect immunity: molecular cloning, expression, and characterization of
RT   cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes
RT   aegypti.";
RL   Insect Mol. Biol. 8:107-118(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10469248; DOI=10.1046/j.1365-2583.1999.83119.x;
RA   Gao Y., Hernandez V.P., Fallon A.M.;
RT   "Immunity proteins from mosquito cell lines include three defensin A
RT   isoforms from Aedes aegypti and a defensin D from Aedes albopictus.";
RL   Insect Mol. Biol. 8:311-318(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Liverpool, Moyo-R, and Red-eye;
RA   Morlais I., Severson D.W.;
RT   "Defensin A protein from Aedes aegypti.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16907826; DOI=10.1111/j.1365-2583.2006.00635.x;
RA   Meredith J.M., Munks R.J., Grail W., Hurd H., Eggleston P., Lehane M.J.;
RT   "A novel association between clustered NF-kappaB and C/EBP binding sites is
RT   required for immune regulation of mosquito Defensin genes.";
RL   Insect Mol. Biol. 15:393-401(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
RN   [7]
RP   PROTEIN SEQUENCE OF 59-98, FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=Liverpool;
RX   PubMed=7633471; DOI=10.1016/0965-1748(95)00043-u;
RA   Lowenberger C., Bulet P., Charlet M., Hetru C., Hodgeman B.,
RA   Christensen B.M., Hoffmann J.A.;
RT   "Insect immunity: isolation of three novel inducible antibacterial
RT   defensins from the vector mosquito, Aedes aegypti.";
RL   Insect Biochem. Mol. Biol. 25:867-873(1995).
RN   [8]
RP   PROTEIN SEQUENCE OF 59-98, FUNCTION, AND INDUCTION.
RC   STRAIN=REFM;
RX   PubMed=7568275; DOI=10.1098/rspb.1995.0139;
RA   Chalk R., Albuquerque C.M., Ham P.J., Townson H.;
RT   "Full sequence and characterization of two insect defensins: immune
RT   peptides from the mosquito Aedes aegypti.";
RL   Proc. R. Soc. B 261:217-221(1995).
CC   -!- FUNCTION: Antibacterial peptide mostly active against Gram-positive
CC       bacteria. Has activity against the bacteria Gram-negative E.cloacae
CC       beta12. {ECO:0000255|PROSITE-ProRule:PRU00710,
CC       ECO:0000269|PubMed:7568275, ECO:0000269|PubMed:7633471,
CC       ECO:0000269|PubMed:8814787}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710,
CC       ECO:0000269|PubMed:7633471, ECO:0000269|PubMed:8814787}.
CC   -!- DEVELOPMENTAL STAGE: Expressed 75 minutes after bacterial infection.
CC       Increased dramatically after 6 hours, continued to increase through to
CC       24 hours and is maintained at high levels until at least 30 hours after
CC       bacterial infection. {ECO:0000269|PubMed:8814787,
CC       ECO:0000269|PubMed:9927179}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:7568275,
CC       ECO:0000269|PubMed:7633471, ECO:0000269|PubMed:8814787}.
CC   -!- MASS SPECTROMETRY: Mass=4072.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:7633471};
CC   -!- POLYMORPHISM: There are five defensin A forms, A1 (shown here) A2, A3,
CC       A4 and A5.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   EMBL; S82860; AAB46807.1; -; mRNA.
DR   EMBL; S82861; AAB46808.2; -; mRNA.
DR   EMBL; S82862; AAB46809.2; -; mRNA.
DR   EMBL; S82863; AAB46810.2; -; mRNA.
DR   EMBL; AF156088; AAD40112.1; ALT_SEQ; mRNA.
DR   EMBL; AF156089; AAD40113.1; -; mRNA.
DR   EMBL; AF095259; AAC64181.1; -; mRNA.
DR   EMBL; AF387487; AAK73080.1; -; mRNA.
DR   EMBL; AF392802; AAL11701.1; -; Genomic_DNA.
DR   EMBL; AF392803; AAL11702.1; -; Genomic_DNA.
DR   EMBL; AF392804; AAL11703.1; -; Genomic_DNA.
DR   EMBL; AY625500; AAT41586.1; -; Genomic_DNA.
DR   EMBL; AY625501; AAT41587.1; -; Genomic_DNA.
DR   EMBL; CH477283; EAT44833.1; -; Genomic_DNA.
DR   EMBL; CH477283; EAT44837.1; -; Genomic_DNA.
DR   RefSeq; XP_001657289.1; XM_001657239.2.
DR   RefSeq; XP_001657293.1; XM_001657243.2.
DR   AlphaFoldDB; P91793; -.
DR   STRING; 7159.AAEL003841-PA; -.
DR   GeneID; 5579095; -.
DR   GeneID; 5579099; -.
DR   KEGG; aag:5579095; -.
DR   KEGG; aag:5579099; -.
DR   VEuPathDB; VectorBase:AAEL003841; -.
DR   VEuPathDB; VectorBase:AAEL027792; -.
DR   eggNOG; ENOG502SD3P; Eukaryota.
DR   HOGENOM; CLU_174272_0_0_1; -.
DR   InParanoid; P91793; -.
DR   OrthoDB; 1600872at2759; -.
DR   PhylomeDB; P91793; -.
DR   Proteomes; UP000008820; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..58
FT                   /evidence="ECO:0000269|PubMed:7568275,
FT                   ECO:0000269|PubMed:7633471"
FT                   /id="PRO_0000006734"
FT   CHAIN           59..98
FT                   /note="Defensin-A"
FT                   /id="PRO_0000006735"
FT   DISULFID        61..88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT   DISULFID        74..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT   DISULFID        78..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT   VARIANT         2
FT                   /note="K -> Q (in forms A3, A4, A5 and A2 from strain
FT                   Liverpool)"
FT   VARIANT         3
FT                   /note="S -> P (in form A4)"
FT   VARIANT         4
FT                   /note="I -> L (in forms A2, A3, A4 and A2 from strain
FT                   Liverpool)"
FT   VARIANT         15
FT                   /note="V -> G (in forms A2, A3, A4, A5, B2, A1 from strain
FT                   Liverpool and A2 from strain Liverpool)"
FT   VARIANT         16
FT                   /note="A -> S (in form B2, A1 from strain Liverpool)"
FT   VARIANT         24
FT                   /note="E -> D (in form A1 from strain Liverpool)"
SQ   SEQUENCE   98 AA;  10583 MW;  95F9457B90E66856 CRC64;
     MKSITVICFL ALCTVAITSA YPQEPVLADE ARPFANSLFD ELPEETYQAA VENFRLKRAT
     CDLLSGFGVG DSACAAHCIA RGNRGGYCNS KKVCVCRN
 
 
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