ID   AQP10_MILTA             Reviewed;         409 AA.
AC   G5CTG7;
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-10 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-10 {ECO:0000303|PubMed:23761966};
GN   Name=AQP10 {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 high and
CC       expression levels are not significantly affected by desiccation or
CC       rehydratation (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; JN378745; AEP14564.1; -; mRNA.
DR   AlphaFoldDB; G5CTG7; -.
DR   SMR; G5CTG7; -.
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; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
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   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Repeat; Stress response;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..409
FT                   /note="Aquaporin-10"
FT                   /id="PRO_0000440211"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           164..166
FT                   /note="NPA 1"
FT   MOTIF           297..299
FT                   /note="NPA 2"
FT   COMPBIAS        47..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   409 AA;  44699 MW;  3F8833EB87477618 CRC64;
     MADAPTYIRQ STTGTATTAP TTMPVHPDTT YYKTTTTTVS DAPRAIADVN DDNHDNYDET
     TGLRSGEKKT RPLVTSTTAP IDAGRMTLGQ KISRWTRIGS DLAREALAEF LGSFILIVFG
     NGVVAQVVLS RGAHGNFLSI NIGYGLAVAF GVYIAGGISG GHLNPAVSLA FAALGKLPWR
     KLPVYMFAQY AGCICASAIV HAIYYDALNN YDGGNRTRGD TWQSTAGIHA SYPQEFLYWQ
     TGLADQIFAT SFLMIGILAL TDNRNTGPPG GVVPILVGCL VMAIGLAYGF NCGYPINPAR
     DMGPRLFTLM AGWGSRTFSN YNPYIFNDYY QRIPYWFWIP VVGPHLGALL GAAIYFFFIG
     NHWPTLHRNV LELQVGHRDN SDDIELLAAK SRRPIEVVTT TETTRERRT