ID   AQP2_MILTA              Reviewed;         323 AA.
AC   G5CTF9;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Aquaporin-2 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-2 {ECO:0000303|PubMed:23761966};
GN   Name=AQP2 {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 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}.
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DR   EMBL; JN378737; AEP14556.2; -; mRNA.
DR   AlphaFoldDB; G5CTF9; -.
DR   SMR; G5CTF9; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; 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; Glycoprotein; Membrane; Repeat; Stress response;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..323
FT                   /note="Aquaporin-2"
FT                   /id="PRO_0000440203"
FT   TRANSMEM        32..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           85..87
FT                   /note="NPA 1"
FT   MOTIF           217..219
FT                   /note="NPA 2"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   323 AA;  35605 MW;  D7CFF26F8EF28670 CRC64;
     MCISEGKMDW RSWLRKKFQV RSQLLRGCMA EFLAVFVLMV FTEGCSASAI FTHRRNDLLF
     AAFGSGLAVT MAVYVAGGVT GAFLNPAIAV AFSVLGKLPW KNCFCYMIAQ YLGAFLASLA
     IYAQYYDALN IFDGGHRQVL GDNGTAQIWS TYPQAFLSPQ GAFVDQVFGT ALLIIVVLSM
     VDKKNWKPQN GYFPIAIGLL IVVLDISLAY NAGAALNPSR DLAPRLFTYV AGYGTETFSV
     KGYTWFFVPV VGSHAGAIVG AVIYQLFIGA QWPQDDLDDS NSVSSMSIHE KNFSLAKRKN
     TRNFNLDITR DFKERNGIST VLY