ID Q17EW2_AEDAE Unreviewed; 1761 AA.
AC Q17EW2;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=AAEL003658-PA {ECO:0000313|EMBL:EAT44989.1};
GN ORFNames=AAEL003658 {ECO:0000313|EMBL:EAT44989.1};
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 {ECO:0000313|EMBL:EAT44989.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT44989.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT44989.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT44989.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT44989.1};
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 [3] {ECO:0000313|EMBL:EAT44989.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT44989.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; CH477279; EAT44989.1; -; Genomic_DNA.
DR RefSeq; XP_001657107.1; XM_001657057.1.
DR STRING; 7159.Q17EW2; -.
DR PaxDb; 7159-AAEL003658-PA; -.
DR VEuPathDB; VectorBase:AAEL003658; -.
DR eggNOG; KOG0994; Eukaryota.
DR HOGENOM; CLU_001560_1_0_1; -.
DR OMA; PCANSHP; -.
DR PhylomeDB; Q17EW2; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 11.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460}.
FT DOMAIN 23..259
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 260..322
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 323..385
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 386..445
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 446..496
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 535..755
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 761..808
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 809..854
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 855..904
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 964..1015
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1016..1066
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1067..1114
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1115..1161
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1233..1288
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1314..1377
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1419..1446
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1515..1608
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1721..1748
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 288..297
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 353..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 416..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 468..477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 480..494
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 761..773
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 763..780
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 782..791
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 809..821
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 811..828
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 830..839
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 874..883
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 988..997
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1039..1048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1067..1079
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1069..1086
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1088..1097
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1115..1127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1117..1134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1136..1145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1761 AA; 197696 MW; DA1489A096A41C75 CRC64;
MLNTNRRPPT TNKQPIHRVH PCEQSSCYPA TGNLLIGREN RLEASSTCGT VRPERYCIVS
HLEEKKCFLC DTRPETAHIP MKNHRVGQII YKNQPGTLEQ SWWQSENGKE NVTIQLDLEA
EFHFTHLIIV FATFRPAAML IERSYDFGKT WHVYRYFAHN CRSAFPDVPT IGKNITDVIC
DHRYSGVEPS KNGEVIYRVL PPMHIENPYA EHVQNMLKMT NLRINFTRLH TLGDTLLDDR
QEIQEKYYYA ISNMIVRGSC SCYGHASRCL PLEGVRNTID MVHGRCECTH NTKGLNCEEC
EDFFNDLPWK PALGKQTNAC KKCHCNNHAT SCHFDQAVYE HSGRVSGGVC DNCQHNTQGY
HCEECSPFFY RDPLEDIQSP YVCKPCDCDP RGSLDDGICD SIADEENGVE AGACHCKKNV
NGRRCDHCKE GFWNFDENNP DGCQTCSCNI LGTVDNAGCN VHTGECICKR LVTGRDCNQC
IPETYGLSDS PEGCTMCNCH PGGSLDNSCD VITGQCRCRP HMQGRDCSEP KQHYFIPTLH
QVLEAEFPGT VNCTHLSQNC SAVIREHPHG YPPTWTGPGF IRAFEGTELK FTVDDIPKTM
NYDVLVRYSP QIKGDWEDIR MTVIRPDEYD PDGPCANSHP EYERDFHTTL SEYETSAVAM
RDICLENGKT YKFIVTFQRH DPYRDNGAAQ ILIDSLVLVP RIEVTPIFHG NPQAEVRYTE
YQNLGCNQTY YDVNYDSEAR PECKDLLNMV SVYVFNGATP CECNPTGSTT KKCEEFGGYC
ACKTNVVGRQ CDKCAPGTYG FGPEGCKACD CNSIGSKDND CDLVTGQCNC HPNTYGRECD
QCQPGFWNFP NCQMCECNGH TPTCNSKTGE CSQCQDFTQG WKCDRCLDGY YGNPLLGSEI
GCRPCRCPDT IASGHSYANE CLLDPKANDV ICLCDQGYAG AKCDVCADNY FGNPDRPGGV
CQQCDCSNNV DLNQPGNCDP KSGQCLQCLY DTEGDHCEFC RDGFYGNALE QNCRPCDCNV
LGTNQTVQHC DRFTGQCPCL ANVRGQYCED CIENHWKIAS GEGCEACNCD PVGSMSEQCN
PYDGQCTCKQ GFGGRQCNQC ESNFWGNPNV HCHACDCNPY GSATYQCNRE TGQCICNPGI
GGYKCDQCAR GYLGEAPYCE PCGECFDNWD MILDGLKEET NRTIEEAKTI KTLGATGAYK
KEFDSMGKKI DIIKGLLTNT ISDREITTID DRIAEVRQHL KASLEELKES EKRLQDTDAT
INFANIEIDN LRKRTEEVKQ LADYLKDNAT KLQEGNIEGA LNLTRDAWNR VTLLGETNME
IQELNDNAER QCKRTEILLK KQQDHFDHLH DTNEASFLKY QNELDTLNAN IPDLNERICD
RRGDPCDEFC GGAGCDGKCG GLTCDKGALT RSEKALQYAK KTEQTIKEKE ELADDILRSM
SQAKTNASEA FKKAKRAHDK AKAHYDHTHS LIDQANVVVT ALTDIIDNNT ATPEKIKDLA
DQVMDYTLQL DPDQIQKLAE QIDEAVSHLE NVETIIRHTE HDLQRVQDLK DDTFATKDRA
EKVLDEAIEL VKALDDADDA QKKARQSIKR ANEDIQSAKI DLEEIDKETD DAYKRANATA
SKVDELKARL NKLHVSNVQN DQDAQEIIKQ AEAVKDSANN AHDLATQLKD NYKTANATLT
ARSNASESAR ERAQNLLNRA SKITVETTNQ LNKLHDLYKT YEQNQNELGS LETNIQGLTE
QINTYLNKIQ GDADRYRQCT T
//
