AQPZ_PSEPK
ID AQPZ_PSEPK Reviewed; 230 AA.
AC Q88F17;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=PP_4282;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN69862.1; -; Genomic_DNA.
DR RefSeq; NP_746398.1; NC_002947.4.
DR AlphaFoldDB; Q88F17; -.
DR SMR; Q88F17; -.
DR STRING; 160488.PP_4282; -.
DR EnsemblBacteria; AAN69862; AAN69862; PP_4282.
DR KEGG; ppu:PP_4282; -.
DR PATRIC; fig|160488.4.peg.4552; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_3_2_6; -.
DR OMA; IFKALMY; -.
DR PhylomeDB; Q88F17; -.
DR BioCyc; PPUT160488:G1G01-4560-MON; -.
DR Proteomes; UP000000556; 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; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..230
FT /note="Aquaporin Z"
FT /id="PRO_0000063995"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 159..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT MOTIF 64..66
FT /note="NPA 1"
FT MOTIF 186..188
FT /note="NPA 2"
FT SITE 22
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 44
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"
SQ SEQUENCE 230 AA; 23149 MW; 6658AF912A1F662E CRC64;
MSLGKRMGAE LIGTFWLVLG GCGSAVLAAS SPLGIGVLGV AFAFGLTVLT MAFAIGHISG
CHLNPAVSFG LVVGGRFPAK ELLPYVIAQV IGAILAAGVI YLIASGKAGF ELSAGLASNG
YADHSPGGYT LGAGFVSEVV MTAMFLVVIM GATDARAPAG FAPIAIGLAL TLIHLISIPV
TNTSVNPARS TGPALFVGGW ALQQLWLFWV APLIGAAIGG ALYRGLAKEP
