ID   AQP1_MILTA              Reviewed;         333 AA.
AC   G5CTF8;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Aquaporin-1 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-1 {ECO:0000303|PubMed:23761966};
GN   Name=AQP1 {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: Aquaglyceroporin that may modulate the water content and
CC       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 medium and expression is slightly
CC       down-regulated in the inactive stage (during anhydrobiois)
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; JN378736; AEP14555.1; -; mRNA.
DR   AlphaFoldDB; G5CTF8; -.
DR   SMR; G5CTF8; -.
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:0015250; F:water channel activity; ISS:UniProtKB.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR000425; MIP.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Repeat; Stress response; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..333
FT                   /note="Aquaporin-1"
FT                   /id="PRO_0000440202"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           137..139
FT                   /note="NPA 1"
FT   MOTIF           270..272
FT                   /note="NPA 2"
SQ   SEQUENCE   333 AA;  37729 MW;  1EC54F37D2257B2F CRC64;
     MQKMSEKPLY RAAENPTRNA DRRAGRFEEE ELISKTGRHP DMVIQFQDDA DDQHTSHYEG
     NWRHYFHKKL HIKNRLIRDW LSESLAMFLF MSLLLGGAAT AHFTGKQDDP MLTAVFHGFS
     AVFGIYVGAG VSGGIINPAL TFAVALLGRV SWRKCLVLVS AQYFGSFIAS AVVYLIYYES
     LQNYAKTADD NGEFLQKTAG IWSTFPKPYL SMTGAIFNQI FCTMLLSIGF LSISDHKNFR
     PTKGLFPFAV GLLIMTVFLA FSYSAGAAMN PARDLSPRLW SLIIGYGNEV FSHNDYKWFW
     IPWLFPYVGA LFGAVMYQIF VGVHWPDKQS TKR