ID   AQP9_MILTA              Reviewed;         281 AA.
AC   G5CTG6;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Aquaporin-9 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-9 {ECO:0000303|PubMed:23761966};
GN   Name=AQP9 {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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX   PubMed=23029181; DOI=10.1371/journal.pone.0045682;
RA   Schokraie E., Warnken U., Hotz-Wagenblatt A., Grohme M.A., Hengherr S.,
RA   Foerster F., Schill R.O., Frohme M., Dandekar T., Schnoelzer M.;
RT   "Comparative proteome analysis of Milnesium tardigradum in early embryonic
RT   state versus adults in active and anhydrobiotic state.";
RL   PLoS ONE 7:E45682-E45682(2012).
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: Expressed in early embryonic state, adult active, and adult
CC       anhydrobiotic state (PubMed:23029181). Transcript abundance is low but
CC       expression is slightly up-regulated in the inactive stage (during
CC       anhydrobiois) (PubMed:23761966). {ECO:0000269|PubMed:23029181,
CC       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; JN378744; AEP14563.1; -; mRNA.
DR   AlphaFoldDB; G5CTG6; -.
DR   SMR; G5CTG6; -.
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   GO; GO:0015166; F:polyol transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005350; F:pyrimidine nucleobase transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015204; F:urea transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015837; P:amine transport; ISS:UniProtKB.
DR   GO; GO:0015791; P:polyol transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006863; P:purine nucleobase transport; ISS:UniProtKB.
DR   GO; GO:0015855; P:pyrimidine nucleobase transport; 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   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Repeat; Stress response;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..281
FT                   /note="Aquaporin-9"
FT                   /id="PRO_0000440210"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           76..78
FT                   /note="NPA 1"
FT   MOTIF           213..215
FT                   /note="NPA 2"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   281 AA;  31066 MW;  BA952C50A3651034 CRC64;
     MGAFVNTKVY IENKNIRDWL SEALSMFMYM SLLLGSAATG HFSGREDDAL FGVIFQGFSI
     TFGIYIGGAM SGAIINPALT LAVALLGKIS WRKCIVLQSA QYIGSFIASA VVYLIYNDSL
     DAFGAGANFT ATEPGVFRKD VAGIWSTFPK TYLKERGAIF NQIFCSMLLT FGFLAISDYK
     NFRPSKGLFP IAVGLLVMTV FLAFSYSTGA AMNPARDFSP RLWSLIIGYG IEVFSYNQYE
     WFWIPWLMPY VGAMLGALIY QLLIGAQWSK GQKGESKHKD P