ID   AQP4_MILTA              Reviewed;         349 AA.
AC   G5CTG1;
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-4 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-4 {ECO:0000303|PubMed:23761966};
GN   Name=AQP4 {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: Most abundant aquaporin in early embryonic state, adult
CC       active, and adult anhydrobiotic state (PubMed:23761966,
CC       PubMed:23029181). Expression is slightly up-regulated in early
CC       embryonic state (PubMed:23029181). {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; JN378739; AEP14558.2; -; mRNA.
DR   AlphaFoldDB; G5CTG1; -.
DR   SMR; G5CTG1; -.
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   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR023275; Aquaporin_3.
DR   InterPro; IPR000425; MIP.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02015; AQUAPORIN3.
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..349
FT                   /note="Aquaporin-4"
FT                   /id="PRO_0000440205"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           148..150
FT                   /note="NPA 1"
FT   MOTIF           281..283
FT                   /note="NPA 2"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   349 AA;  39088 MW;  EA1594B32A00A424 CRC64;
     MSKVPPTDPF SHMLNGNLQQ RIVKRDIDGE VPTERAVTDL ASEKAHAIAT HGEVVIQIQH
     SDTFGMDKEK NDWRSRAARM LYIESRLVRE GLSESLAMFF FMSLLLGCAA TARFTGNQND
     PMLAAFYHGF SIIFAIYVAG GISGGLLNPA ITFTIAFLGR LSWLRCLIYM SAQYFGAFIA
     SAVVYLIYYD SLQNFSGANK VDETGANGTA GIWSTFPRPY LSLRGAIFNQ IFCTMLLTIG
     FLSICDFRNS RPDKGMFPFA VGMLIMTVFL AFSYSAGAAM NPARDISPRL WTLIVGYGDE
     VFSYNNYKWF WIPWLFPYVG ALLGGVIYEI FIGIHWPKDY ANKHVTNRT