AQP_CICVR
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 25-MAY-2022, entry version 86.
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: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 PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 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
