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AQPZ_BRUAB
ID   AQPZ_BRUAB              Reviewed;         228 AA.
AC   P0C112; Q57AQ4; Q9LA79;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Aquaporin Z;
DE   AltName: Full=Aquaporin X;
GN   Name=aqpZ; Synonyms=aqpX; OrderedLocusNames=BruAb1_1976;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX75280.1; -; Genomic_DNA.
DR   RefSeq; WP_002967012.1; NC_006932.1.
DR   AlphaFoldDB; P0C112; -.
DR   SMR; P0C112; -.
DR   EnsemblBacteria; AAX75280; AAX75280; BruAb1_1976.
DR   GeneID; 3788457; -.
DR   KEGG; bmb:BruAb1_1976; -.
DR   HOGENOM; CLU_020019_3_2_5; -.
DR   OMA; IFKALMY; -.
DR   Proteomes; UP000000540; 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_0000063983"
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
 
 
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