AQP_AEDAE
ID AQP_AEDAE Reviewed; 249 AA.
AC Q9NHW7; Q0IG28;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Aquaporin AQPAe.a;
GN ORFNames=AAEL003512;
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].
RC STRAIN=UTMB; TISSUE=Malpighian tubule;
RX PubMed=10971718; DOI=10.1046/j.1365-2583.2000.00201.x;
RA Pietrantonio P.V., Jagge C., Keeley L.L., Ross L.S.;
RT "Cloning of an aquaporin-like cDNA and in situ hybridization in adults of
RT the mosquito Aedes aegypti (Diptera: Culicidae).";
RL Insect Mol. Biol. 9:407-418(2000).
RN [2]
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).
CC -!- FUNCTION: Forms a water-specific channel. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Localized in tracheolar cells associated with the
CC Malpighian tubules.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT45185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF218314; AAF64037.1; -; mRNA.
DR EMBL; CH477274; EAT45185.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001656931.1; XM_001656881.1.
DR AlphaFoldDB; Q9NHW7; -.
DR SMR; Q9NHW7; -.
DR STRING; 7159.AAEL003512-PA; -.
DR TCDB; 1.A.8.8.30; the major intrinsic protein (mip) family.
DR VEuPathDB; VectorBase:AAEL024675; -.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_3_1; -.
DR InParanoid; Q9NHW7; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..249
FT /note="Aquaporin AQPAe.a"
FT /id="PRO_0000063974"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 82..84
FT /note="NPA 1"
FT MOTIF 198..200
FT /note="NPA 2"
FT CONFLICT 147
FT /note="I -> M (in Ref. 1; AAF64037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 26093 MW; 491D5D3385A56F54 CRC64;
MTESAGVKQL VGVADITENR NIWRMLVAEF LGTFFLVSIG IGSTMGWGGD YAPTMTQIAF
TFGLVVATLA QAFGHVSGCH INPAVTIGLM ITADISILKG AFYIVSQCVG AIAGAALIKA
ATPSDVIGGL GVTGIDPRLT AGQGVMIEAL ITFILVFVVH GVCDNRRSDI KGSAPLAIGL
SITAGHLSAI KYTGASMNPA RSFGPAVVMG NWTDQWVYWV GPIVGGILAG AVYRLFFKVR
KGDEESYDF
