ID   AQPZ_SYNY3              Reviewed;         247 AA.
AC   P73809;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN   Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=slr2057;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17863.1; -; Genomic_DNA.
DR   PIR; S74902; S74902.
DR   AlphaFoldDB; P73809; -.
DR   SMR; P73809; -.
DR   IntAct; P73809; 1.
DR   STRING; 1148.1652945; -.
DR   PaxDb; P73809; -.
DR   EnsemblBacteria; BAA17863; BAA17863; BAA17863.
DR   KEGG; syn:slr2057; -.
DR   eggNOG; COG0580; Bacteria.
DR   InParanoid; P73809; -.
DR   OMA; IFKALMY; -.
DR   PhylomeDB; P73809; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015250; F:water channel activity; IBA:GO_Central.
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; PTHR45687; PTHR45687; 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..247
FT                   /note="Aquaporin Z"
FT                   /id="PRO_0000064001"
FT   TRANSMEM        7..29
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        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        138..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        167..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        209..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   MOTIF           70..72
FT                   /note="NPA 1"
FT   MOTIF           194..196
FT                   /note="NPA 2"
FT   SITE            19
FT                   /note="Involved in tetramerization or stability of the
FT                   tetramer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            50
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            182
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            191
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            197
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ   SEQUENCE   247 AA;  25547 MW;  ED546D1A76D948FB CRC64;
     MKKYIAEFIG TFWLVLGGCG SAVFAAFIAA PGGGNTNEFG LGYLGVALAF GLTVFTGAYA
     LGHISGGHFN PAVSFGLWMG KRFPGSQLAP YIGAQVLGAI VASLFIFIVA QGGPNFSLDG
     SNPLATNGFG DHSPQGYGFL AALLIEFVLT FIFLIVILGV TDKTAPAGFA PAAIGLALTL
     IHLISIPITN TSVNPARSTG VALFCGNPAL IGQLWLFWLA PIAGALLAGF VYHNVLEDLG
     RPEPEAE