AQPZ_BRUME
ID AQPZ_BRUME Reviewed; 228 AA.
AC Q9L772;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Aquaporin Z;
GN Name=aqpZ; OrderedLocusNames=BMEI0070;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=133;
RA Hernandez-Castro R., Verdugo-Rodriguez A., Gutierrez-Pabello J.A.,
RA Suarez-Guemes F.;
RT "Cloning and nucleotide sequence of aquaporin gene of Brucella
RT melitensis.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AF226624; AAF36396.1; -; Genomic_DNA.
DR EMBL; AE008917; AAL51252.1; -; Genomic_DNA.
DR PIR; AI3260; AI3260.
DR RefSeq; WP_004684491.1; NZ_GG703778.1.
DR AlphaFoldDB; Q9L772; -.
DR SMR; Q9L772; -.
DR STRING; 224914.BMEI0070; -.
DR EnsemblBacteria; AAL51252; AAL51252; BMEI0070.
DR GeneID; 29594900; -.
DR KEGG; bme:BMEI0070; -.
DR PATRIC; fig|224914.52.peg.1440; -.
DR eggNOG; COG0580; Bacteria.
DR OMA; IFKALMY; -.
DR PhylomeDB; Q9L772; -.
DR Proteomes; UP000000419; 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_0000063985"
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; 23189 MW; 64282C39E4DD4109 CRC64;
MLNKLSAEFF GTFWLVFGGC GSAILAAAFP ELGIGFLGVA LAFGLTVLTM AYAVGGISGG
HFNPAVSLGL TVAGRLPAKD LIPYWVAQVL GAIAAAAILY VIASGKDGFS AGGLASNGYG
ELSPGGYSMM AGLLIEIILT AFFIIIILGS TSSLAPAGFA PIAIGFGLTL IHLVSIPVTN
TWVNPARSTG VALFADTAAL SQLWLFWVAP LVGAVIGAII WKGLLGRD
