ID   AQP5_MILTA              Reviewed;         277 AA.
AC   G5CTG2;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Aquaporin-5 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-5 {ECO:0000303|PubMed:23761966};
GN   Name=AQP5 {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 water-specific aquaporin that may modulate the water
CC       content and osmolytes during anhydrobiosis (PubMed:23761966).
CC       {ECO:0000305|PubMed:23761966}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Transcript abundance is high and expression levels are not
CC       significantly affected 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}.
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DR   EMBL; JN378740; AEP14559.1; -; mRNA.
DR   AlphaFoldDB; G5CTG2; -.
DR   SMR; G5CTG2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Cell membrane; Membrane; Repeat; Stress response; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..277
FT                   /note="Aquaporin-5"
FT                   /id="PRO_0000440206"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           80..82
FT                   /note="NPA 1"
FT   MOTIF           202..204
FT                   /note="NPA 2"
SQ   SEQUENCE   277 AA;  29316 MW;  96EFF18181E535AA CRC64;
     MWCFNPRSSI EDLAKIQFWK ALGAEFIGTA VLVYIGCGAA VTSTPDANRD AFVTRVSLAF
     GLTVATMVWA ICGVSGGHIN PAVSLGFLVT RRISLVRFLL YVAFQCSGAV AGAALLYAST
     FDSVKRGGFG TNSMATENGQ YLISPAQGIL IEAIITFVLV FTVFATCDAK RSDLKGSGPL
     AIGIAVLISH LVAIPLTGTS MNPARSLGPA VLIGFWTDHW VFWVGPMLGG AVAGLLYDMA
     FAADASLRKF GECAVADDYD PDADDRTIDT KRVNARV