ID   AQP_ENCCU               Reviewed;         250 AA.
AC   Q8SRK2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Aquaporin;
GN   Name=AQP; OrderedLocusNames=ECU07_0740;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   FUNCTION.
RX   PubMed=16197948; DOI=10.1016/j.ijpara.2005.08.013;
RA   Ghosh K., Cappiello C.D., McBride S.M., Occi J.L., Cali A., Takvorian P.M.,
RA   McDonald T.V., Weiss L.M.;
RT   "Functional characterization of a putative aquaporin from Encephalitozoon
RT   cuniculi, a microsporidia pathogenic to humans.";
RL   Int. J. Parasitol. 36:57-62(2006).
CC   -!- FUNCTION: Water channel required to facilitate the transport of water
CC       across membranes. Involved in osmotolerance.
CC       {ECO:0000269|PubMed:16197948}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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). In microsporidia, the second signature motif
CC       differs slightly and is Asn-Pro-Gly (NPG).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL590447; CAD25606.1; -; Genomic_DNA.
DR   RefSeq; NP_586002.1; NM_001041624.1.
DR   AlphaFoldDB; Q8SRK2; -.
DR   SMR; Q8SRK2; -.
DR   STRING; 284813.Q8SRK2; -.
DR   TCDB; 1.A.8.10.17; the major intrinsic protein (mip) family.
DR   PRIDE; Q8SRK2; -.
DR   GeneID; 859431; -.
DR   KEGG; ecu:ECU07_0740; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_0740; -.
DR   HOGENOM; CLU_020019_3_4_1; -.
DR   InParanoid; Q8SRK2; -.
DR   OMA; LCVGGHI; -.
DR   OrthoDB; 1152704at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
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; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; PTHR19139; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..250
FT                   /note="Aquaporin"
FT                   /id="PRO_0000385184"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..133
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..224
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           69..71
FT                   /note="NPA"
FT   MOTIF           206..208
FT                   /note="NPG"
SQ   SEQUENCE   250 AA;  26795 MW;  E309623243E19255 CRC64;
     MTRETLKTLQ STFGEMVASF VFGFAVYSAL LGSALTEQSA ARVIVGLTVG FSGICVIYSF
     CDVTVAHFNP AITLAAILTC KLGVLRGIGY IVAQYIGFIL AVCALLPCSP VGYKETLNII
     RPTPSPFGGD NLNVFFTEFF LTAILVHVAF ATAVNPYKPK TDTEGKFVDP DEEEPVDRRI
     TAPLCIGLTL GFLAFLGLAS SGGAFNPGLT LAPVIMSNTW NHFWAYFAGQ YLGGFVGGLL
     QVLVLYKLSF