AQPZ_SHIFL
ID AQPZ_SHIFL Reviewed; 231 AA.
AC O68874; P48838; P75827; Q47159;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; Synonyms=bniP;
GN OrderedLocusNames=SF0832, S0873;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Calamita G., Ludovico A., DeVito D., Rizzo G., Svelto M.;
RT "Cloning of the S. flexneri aquaporin-Z coding region.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AF055905; AAC12651.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN42465.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16338.1; -; Genomic_DNA.
DR RefSeq; NP_706758.2; NC_004337.2.
DR RefSeq; WP_001298299.1; NZ_WPGW01000337.1.
DR AlphaFoldDB; O68874; -.
DR SMR; O68874; -.
DR STRING; 198214.SF0832; -.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR EnsemblBacteria; AAN42465; AAN42465; SF0832.
DR EnsemblBacteria; AAP16338; AAP16338; S0873.
DR GeneID; 1023778; -.
DR GeneID; 58388674; -.
DR KEGG; sfl:SF0832; -.
DR KEGG; sfx:S0873; -.
DR PATRIC; fig|198214.7.peg.961; -.
DR HOGENOM; CLU_020019_3_2_6; -.
DR OMA; IFKALMY; -.
DR OrthoDB; 1744995at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; 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; PTHR19139; PTHR19139; 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_0000064000"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TOPO_DOM 30..33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TOPO_DOM 55..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TOPO_DOM 103..130
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TOPO_DOM 152..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TOPO_DOM 177..201
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TOPO_DOM 223..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 63..65
FT /note="NPA 1"
FT MOTIF 186..188
FT /note="NPA 2"
FT SITE 20
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT SITE 43
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 174
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 183
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 189
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT CONFLICT 43
FT /note="F -> I (in Ref. 1; AAC12651)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="L -> V (in Ref. 1; AAC12651)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="I -> M (in Ref. 1; AAC12651)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> V (in Ref. 1; AAC12651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 23703 MW; 3BDE1A932D45CF14 CRC64;
MFRKLAAECF GTFWLVFGGC GSAVLAAGFP ELGIGFAGVA LAFGLTVLTM AFAVGHISGG
HFNPAVTIGL WAGGRFPAKE VVGYVIAQVV GGIVAAALLY LIASGKTGFD AAASGFASNG
YGEHSPGGYS MLSALVVELV LSAGFLLVIH GATDKFAPAG FAPIAIGLAL TLIHLISIPV
TNTSVNPARS TAVAIFQGGW ALEQLWFFWV VPIVGGIIGG LIYRTLLEKR D
