ID   AQP3_MILTA              Reviewed;         326 AA.
AC   G5CTG0;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Aquaporin-3 {ECO:0000303|PubMed:23761966};
DE            Short=AQP-3 {ECO:0000303|PubMed:23761966};
GN   Name=AQP3 {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 completely unaffected 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; JN378738; AEP14557.1; -; mRNA.
DR   AlphaFoldDB; G5CTG0; -.
DR   SMR; G5CTG0; -.
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:0015791; P:polyol transmembrane 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.
DR   TIGRFAMs; TIGR00861; MIP; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Repeat; Stress response;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..326
FT                   /note="Aquaporin-3"
FT                   /id="PRO_0000440204"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           88..90
FT                   /note="NPA 1"
FT   MOTIF           220..222
FT                   /note="NPA 2"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   326 AA;  35534 MW;  838B64F53482FB25 CRC64;
     MAISWRTWLK KTIHCDNSYV RTGLAEFLGT FLLVLLLNGM IITAHMSVRN ADGTMAHPLN
     TAHLAFGGGL AVMVAVLVSG GISGAHLNPA VTTTMLVMGR LSPLKSLVYI FMQYMGAFFA
     ASILYAVYFE SILAYDYGER QVLGANGTAG WFATYPQEHI SLVTQIFDAI LGTGLLVMGI
     FAIIDPNNMA VPKGQIPLYV GFLISSLIFS FSYNAGAALN PARDLAPRLF LWVIGYGAEA
     FTARGHLWWL VPVIGPHVGG LLGGVTYQMF IGAHYQSDRK LKPATIMDED DDTNATYNTI
     TTTTHQKVYN GRRNFDESVP LKTVHA