AQP_ENCHE
ID AQP_ENCHE Reviewed; 251 AA.
AC Q1M1A0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Aquaporin;
GN Name=AQP;
OS Encephalitozoon hellem (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=27973;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wasson K., Barry P.A.;
RT "Role for aquaporins in encephalitozoonosis.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across membranes. Involved in osmotolerance (By similarity).
CC {ECO:0000250}.
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}.
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DR EMBL; AY325888; AAQ91842.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1M1A0; -.
DR SMR; Q1M1A0; -.
DR VEuPathDB; MicrosporidiaDB:EHEL_070710; -.
DR VEuPathDB; MicrosporidiaDB:KMI_08g12930; -.
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; 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; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..251
FT /note="Aquaporin"
FT /id="PRO_0000385185"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..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..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 69..71
FT /note="NPA"
FT MOTIF 206..208
FT /note="NPG"
SQ SEQUENCE 251 AA; 26695 MW; 28C0FA54E789C853 CRC64;
MAGETLRKIQ SLLGEMVASF IFGFAVYSAI LGSTIAQQPA AKVIIGLTVG FSAIGIIYSF
SDVTIAHFNP AITLAAILTG KMGILCGLGY MLAQCVGFIL AVCALLVCSP VGYKETLNVI
RPAPAPFGAD NLNVFFTEFF LTAILVHIAF AVAVNPYRPK VDTDGKFVDP DEKEPVDRRI
TAPLCIGLTL GFLAFMGLVT SGGAFNPGLT LAPVIMSNTW QHFWLYLGAQ YLGGLVGGLL
QVFVLYKLSS N