ID   AQPZ_SHEON              Reviewed;         231 AA.
AC   Q8EHC1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN   Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=SO_1307;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(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; AE014299; AAN54372.2; -; Genomic_DNA.
DR   RefSeq; NP_716927.2; NC_004347.2.
DR   RefSeq; WP_011071520.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EHC1; -.
DR   SMR; Q8EHC1; -.
DR   STRING; 211586.SO_1307; -.
DR   PaxDb; Q8EHC1; -.
DR   KEGG; son:SO_1307; -.
DR   PATRIC; fig|211586.12.peg.1257; -.
DR   eggNOG; COG0580; Bacteria.
DR   HOGENOM; CLU_020019_3_2_6; -.
DR   OrthoDB; 1744995at2; -.
DR   PhylomeDB; Q8EHC1; -.
DR   BioCyc; SONE211586:G1GMP-1209-MON; -.
DR   Proteomes; UP000008186; 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; IBA:GO_Central.
DR   GO; GO:0006833; P:water transport; 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; 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..231
FT                   /note="Aquaporin Z"
FT                   /id="PRO_0000063999"
FT   TRANSMEM        9..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        35..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        83..105
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        164..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        206..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   MOTIF           65..67
FT                   /note="NPA 1"
FT   MOTIF           187..189
FT                   /note="NPA 2"
FT   SITE            22
FT                   /note="Involved in tetramerization or stability of the
FT                   tetramer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            45
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            175
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            184
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            190
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ   SEQUENCE   231 AA;  23855 MW;  749DB5DA214522F6 CRC64;
     MNMSQKMAAE FLGTLWLVLG GCGSAVLAAA FPEVGIGLLG VSLAFGLTVL TMAFAIGHIS
     GCHLNPAVSF GLWAGGRFPT SELLPYIIAQ VAGGIAGAGV LYLIASGQEG FSLAAGFASN
     GFGEHSPGGY SMISVMICEI VMTLFFLLVI LGSTDERAPK GFAPIAIGLC LTLIHLISIP
     ISNTSVNPAR STGPALFVGD WAVSQLWLFW AAPIIGAILA GVIYRYFNAA K