ID   AQP_CICVR               Reviewed;         255 AA.
AC   Q23808; Q23816;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 89.
DE   RecName: Full=Aquaporin AQPcic;
GN   Name=AQP; Synonyms=CIC;
OS   Cicadella viridis (Green leafhopper).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Membracoidea;
OC   Cicadellidae; Cicadellinae; Cicadellini; Cicadella.
OX   NCBI_TaxID=36150;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 245-255.
RC   TISSUE=Filter chamber;
RX   PubMed=8944756; DOI=10.1111/j.1432-1033.1996.00707.x;
RA   Le Caherec F., Deschamps S., Delamarche C., Pellerin I., Bonnec G.,
RA   Guillam M.-T., Thomas D., Gouranton J., Hubert J.-F.;
RT   "Molecular cloning and characterization of an insect aquaporin. Functional
RT   comparison with aquaporin 1.";
RL   Eur. J. Biochem. 241:707-715(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 85-205.
RC   TISSUE=Filter chamber;
RX   PubMed=7542238; DOI=10.1074/jbc.270.29.17414;
RA   Beuron F., Le Caherec F., Guillam M.-T., Cavalier A., Garret A.,
RA   Tassan J.-P., Delamarche C., Schultz P., Mallouh V., Rolland J.-P.,
RA   Hubert J.-F., Gouranton J., Thomas D.;
RT   "Structural analysis of a MIP family protein from the digestive tract of
RT   Cicadella viridis.";
RL   J. Biol. Chem. 270:17414-17422(1995).
CC   -!- FUNCTION: Forms a water-specific channel. May be involved in the
CC       transfer of excess sap dietary water from the initial midgut to the
CC       terminal midgut and the proximal part of the malpighian tubules.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Filter chamber epithelium in the digestive tract.
CC       Absent from midgut.
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   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Liquid states - Issue 36 of
CC       July 2003;
CC       URL="https://web.expasy.org/spotlight/back_issues/036";
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DR   EMBL; X97159; CAA65799.1; -; mRNA.
DR   EMBL; X77957; CAA54921.1; -; mRNA.
DR   AlphaFoldDB; Q23808; -.
DR   SMR; Q23808; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   NCBIfam; TIGR00861; MIP; 1.
DR   PANTHER; PTHR19139:SF199; AQUAPORIN; 1.
DR   PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..255
FT                   /note="Aquaporin AQPcic"
FT                   /id="PRO_0000063975"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..60
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..215
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           85..87
FT                   /note="NPA 1"
FT   MOTIF           201..203
FT                   /note="NPA 2"
FT   CONFLICT        120..146
FT                   /note="ILKVITPAEFRGTLCMTSLAPGVTPPM -> PQGNNPCRVQGHSLYDESRPR
FT                   CDPAH (in Ref. 2; CAA54921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..174
FT                   /note="VCDDRRKNLG -> LRRPPQEPA (in Ref. 2; CAA54921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="A -> R (in Ref. 2; CAA54921)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   255 AA;  26885 MW;  66093CF3D1253B1D CRC64;
     MAADKSVDNT KKIIGIDDIT DTKTIWRCLA AELIGTLLLV LIGTGSCTGV QISEGDVVVR
     IALTFGFIIA TMVQCIGHVS GCHINPAVTC GLLVTGHISI LKAIFYIIVQ CVGAIAGSAI
     LKVITPAEFR GTLCMTSLAP GVTPPMGFLV EACITFVLIL LVQSVCDDRR KNLGNAAPVA
     VGLAITCCHL AAIKYTGSSM NPARSFGPAV NGDDNWANHW VYWAGPIVGG VVAGITYRAL
     FRARKPEEEA SSYDF
//