AQPZ_BRUSU
ID AQPZ_BRUSU Reviewed; 228 AA.
AC Q8FY85; G0K8M1;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Aquaporin Z;
GN Name=aqpZ; OrderedLocusNames=BR2001, BS1330_I1995;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- FUNCTION: Transport of water across the membrane. Possibly involved in
CC the adaptation to variation in intravacuolar pH or osmolarity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane 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).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AE014291; AAN30891.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19308.1; -; Genomic_DNA.
DR RefSeq; WP_006190978.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8FY85; -.
DR SMR; Q8FY85; -.
DR EnsemblBacteria; AEM19308; AEM19308; BS1330_I1995.
DR GeneID; 45052938; -.
DR KEGG; bms:BR2001; -.
DR KEGG; bsi:BS1330_I1995; -.
DR PATRIC; fig|204722.21.peg.3229; -.
DR HOGENOM; CLU_020019_3_2_5; -.
DR OMA; IFKALMY; -.
DR PhylomeDB; Q8FY85; -.
DR Proteomes; UP000007104; Chromosome I.
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; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..228
FT /note="Aquaporin Z"
FT /id="PRO_0000063986"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..56
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..103
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..126
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..176
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..202
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..225
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 63..65
FT /note="NPA 1"
FT MOTIF 184..186
FT /note="NPA 2"
FT SITE 20
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000250"
FT SITE 43
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 187
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 23150 MW; F00135E825CD2898 CRC64;
MLNKLSAEFF GTFWLVFGGC GSAILAAAFP ELGIGFLGVA LAFGLTVLTM AYAVGGISGG
HFNPAVSLSL TVAGRLPAKD LIPYWVAQVL GAIATAAILY VIASGKDGFS AGGLASNGYG
ELSPGGYSMM AGLLIEIILT AFFIIIILGS TSSLAPAGFA PIAIGFGLTL IHLVSIPVTN
TSVNPARSTG VALFADTAAL SQLWLFWVAP LVGAVIGAII WKGLLGRD
