AQPZ_BORBR
ID AQPZ_BORBR Reviewed; 236 AA.
AC Q7WKG2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=BB2145;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(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; BX640443; CAE32641.1; -; Genomic_DNA.
DR RefSeq; WP_003812617.1; NC_002927.3.
DR AlphaFoldDB; Q7WKG2; -.
DR SMR; Q7WKG2; -.
DR STRING; 257310.BB2145; -.
DR EnsemblBacteria; CAE32641; CAE32641; BB2145.
DR GeneID; 56478320; -.
DR GeneID; 66438397; -.
DR KEGG; bbr:BB2145; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_3_2_4; -.
DR OMA; IFKALMY; -.
DR OrthoDB; 1744995at2; -.
DR Proteomes; UP000001027; 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; 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..236
FT /note="Aquaporin Z"
FT /id="PRO_0000063980"
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT MOTIF 66..68
FT /note="NPA 1"
FT MOTIF 189..191
FT /note="NPA 2"
FT SITE 23
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 46
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 177
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 186
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 192
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ SEQUENCE 236 AA; 24025 MW; D15BFCB1215BFE5D CRC64;
MQPLFKRCGA EFFGTFWLVL GGCGSAVLAA GVPQVGIGYA GVALAFGLTV LTMAYAVGHI
SGGHFNPAVT VGLAASGRFG WRDVPPYIVA QVVGAIVAAA TLASIAQGVA GFDLVASKFA
ANGYGDHSPG KYSMQAALIC EIVLSAGFVF VILGATDKRA PAGFAPIPIG LALTLIHLIS
IPVTNTSVNP ARSTGPALFV GGWALEQLWL FWLAPIAGAL VGALAYRLVG TPSAQR
