ID   AQPZ_BRADU              Reviewed;         240 AA.
AC   Q89EG9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN   Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=bll7116;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Channel that permits osmotically driven movement of water in
CC       both directions. It is involved in the osmoregulation and in the
CC       maintenance of cell turgor during volume expansion in rapidly growing
CC       cells. It mediates rapid entry or exit of water in response to abrupt
CC       changes in osmolarity. {ECO:0000255|HAMAP-Rule:MF_01146}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01146}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01146}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01146}.
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).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01146}.
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DR   EMBL; BA000040; BAC52381.1; -; Genomic_DNA.
DR   RefSeq; NP_773756.1; NC_004463.1.
DR   RefSeq; WP_011089853.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89EG9; -.
DR   SMR; Q89EG9; -.
DR   STRING; 224911.27355398; -.
DR   EnsemblBacteria; BAC52381; BAC52381; BAC52381.
DR   GeneID; 64026874; -.
DR   KEGG; bja:bll7116; -.
DR   PATRIC; fig|224911.44.peg.7175; -.
DR   eggNOG; COG0580; Bacteria.
DR   HOGENOM; CLU_020019_3_2_5; -.
DR   InParanoid; Q89EG9; -.
DR   OMA; IFKALMY; -.
DR   PhylomeDB; Q89EG9; -.
DR   Proteomes; UP000002526; Chromosome.
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:0015250; F:water channel activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   HAMAP; MF_01146; Aquaporin_Z; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR023743; Aquaporin_Z.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR45724; PTHR45724; 1.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..240
FT                   /note="Aquaporin Z"
FT                   /id="PRO_0000063982"
FT   TRANSMEM        13..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        39..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        129..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   MOTIF           64..66
FT                   /note="NPA 1"
FT   MOTIF           186..188
FT                   /note="NPA 2"
FT   SITE            21
FT                   /note="Involved in tetramerization or stability of the
FT                   tetramer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            44
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            174
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            183
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            189
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ   SEQUENCE   240 AA;  24527 MW;  2684D70E284D4FA6 CRC64;
     MDMKKYAAEA IGTFWLTFAG CGSAVIAAGF PQVGIGLVGV SLAFGLSVVT MAYAIGHISG
     CHLNPAVTVG LAAGGRFPAG QILPYVIAQV CGAIVAAELL YIIASGAPGF DVTKGFASNG
     YDAHSPGQYS MMACFLTEVV MTMMFLFIIM GATHGRAPAG FAPLAIGLAL VMIHLVSIPV
     TNTSVNPARS TGPALFVGGW AMAQLWLFWV APLIGGALGG VIYRWLSEEP TGVVAGAKAA