AQPZ_BRUA2
ID AQPZ_BRUA2 Reviewed; 228 AA.
AC Q2YR68; Q57AQ4; Q9LA79;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Aquaporin Z;
DE AltName: Full=Aquaporin X;
GN Name=aqpZ; Synonyms=aqpX; OrderedLocusNames=BAB1_2001;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11101683; DOI=10.1099/00221287-146-12-3251;
RA Rodriguez M.C., Froger A., Rolland J.-P., Thomas D., Aguero J.,
RA Delamarche C., Garcia-Lobo J.M.;
RT "A functional water channel protein in the pathogenic bacterium Brucella
RT abortus.";
RL Microbiology 146:3251-3257(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- FUNCTION: Transport of water across the membrane. Possibly involved in
CC the adaptation to variation in intravacuolar pH or osmolarity.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF148066; AAF73105.1; -; Genomic_DNA.
DR EMBL; AM040264; CAJ11957.1; -; Genomic_DNA.
DR RefSeq; WP_002967012.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YR68; -.
DR SMR; Q2YR68; -.
DR STRING; 359391.BAB1_2001; -.
DR EnsemblBacteria; CAJ11957; CAJ11957; BAB1_2001.
DR GeneID; 3788457; -.
DR KEGG; bmf:BAB1_2001; -.
DR PATRIC; fig|359391.11.peg.1238; -.
DR HOGENOM; CLU_020019_3_2_5; -.
DR OMA; IFKALMY; -.
DR PhylomeDB; Q2YR68; -.
DR Proteomes; UP000002719; 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; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..228
FT /note="Aquaporin Z"
FT /id="PRO_0000063984"
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; 23145 MW; 23C64C39E4DD444A CRC64;
MLNKLSAEFF GTFWLVFGGC GSAILAAAFP ELGIGFLGVA LAFGLTVLTM AYAVGGISGG
HFNPAVSLGL TVAGRLPAKD LIPYWVAQVL GAIAAAAILY VIASGKDGFS AGGLASNGYG
ELSPGGYSMM AGLLIEIILT AFFIIIILGS TSSLAPAGFA PIAIGFGLTL IHLVSIPVTN
TSVNPARSTG VALFADRAAL SQLWLFWVAP LVGAVIGAII WKGLLGRD
