ID   AQP11_MILTA             Reviewed;         270 AA.
AC   G5CTG8;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Aquaporin-11 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-11 {ECO:0000303|PubMed:23761966};
GN   Name=AQP11 {ECO:0000303|PubMed:23761966};
OS   Milnesium tardigradum (Water bear) (Tardigrade).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Apochela;
OC   Milnesiidae; Milnesium.
OX   NCBI_TaxID=46460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, AND INDUCTION.
RX   PubMed=23761966; DOI=10.4137/bbi.s11497;
RA   Grohme M.A., Mali B., Welnicz W., Michel S., Schill R.O., Frohme M.;
RT   "The aquaporin channel repertoire of the tardigrade Milnesium
RT   tardigradum.";
RL   Bioinf. Biol. Insights 7:153-165(2013).
CC   -!- FUNCTION: Probable intracellular unorthodox aquaporin that may modulate
CC       the water content and osmolytes during anhydrobiosis (PubMed:23761966).
CC       {ECO:0000305|PubMed:23761966}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Transcript abundance is low and expression levels are
CC       completely unaffected by desiccation or rehydratation
CC       (PubMed:23761966). {ECO:0000269|PubMed:23761966}.
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). {ECO:0000305|PubMed:23761966}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JN378746; AEP14565.2; -; mRNA.
DR   AlphaFoldDB; G5CTG8; -.
DR   SMR; G5CTG8; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR016697; Aquaporin_11/12.
DR   PIRSF; PIRSF017529; Aquaporin_11/12; 1.
DR   SUPFAM; SSF81338; SSF81338; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Repeat; Stress response; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..270
FT                   /note="Aquaporin-11"
FT                   /id="PRO_0000440212"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           94..96
FT                   /note="NPA 1"
FT   MOTIF           207..209
FT                   /note="NPA 2"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   270 AA;  30369 MW;  4D615D4EB8C356B9 CRC64;
     MYTQIMTMYP LLISILHILF IISICQLCRY VSNVLVKHSL ARIAIEEFIC AVQLCATNFE
     LGVITQIYGF SAYALGLFFC SFTYTFTFQD GTCDPSECYE KFCKREMSAR EAVLRATFSI
     MGAAVSYRFA KIFWSFGLMA THMDFYKNES CDASLQVPVL IGLGFETFET IVNRLLQNMR
     HYNMLISAIS DVCITFFGLF VSGGYFNPTL SFAMEYGCQG LSGPSFFLVY WFGPILGSSI
     SLKIAKPLLR IIEGSDEAKV EVVDAKAHSD