AQPZ_PSEAE
ID AQPZ_PSEAE Reviewed; 229 AA.
AC Q9HWZ3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=PA4034;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG07421.1; -; Genomic_DNA.
DR PIR; F83141; F83141.
DR RefSeq; NP_252723.1; NC_002516.2.
DR RefSeq; WP_003102790.1; NZ_QZGE01000013.1.
DR AlphaFoldDB; Q9HWZ3; -.
DR SMR; Q9HWZ3; -.
DR STRING; 287.DR97_3833; -.
DR PaxDb; Q9HWZ3; -.
DR EnsemblBacteria; AAG07421; AAG07421; PA4034.
DR GeneID; 879049; -.
DR KEGG; pae:PA4034; -.
DR PATRIC; fig|208964.12.peg.4225; -.
DR PseudoCAP; PA4034; -.
DR HOGENOM; CLU_020019_3_2_6; -.
DR InParanoid; Q9HWZ3; -.
DR OMA; IFKALMY; -.
DR PhylomeDB; Q9HWZ3; -.
DR BioCyc; PAER208964:G1FZ6-4107-MON; -.
DR Proteomes; UP000002438; 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; IBA:GO_Central.
DR GO; GO:0006833; P:water transport; IBA:GO_Central.
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..229
FT /note="Aquaporin Z"
FT /id="PRO_0000063994"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 203..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT MOTIF 62..64
FT /note="NPA 1"
FT MOTIF 184..186
FT /note="NPA 2"
FT SITE 19
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 42
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 172
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 181
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 187
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ SEQUENCE 229 AA; 23320 MW; 4EA322E937C06D48 CRC64;
MKQYGAEFFG TFWLVLGGCG SAVLAAGVPE LGIGYLGVAL AFGLSVLTMA YAIGPISGAH
LNPAVSVGLW VGGRFPASQL LPYVVAQVLG GLAAGGVLYL IASGKAGFDL AAGFASNGYG
EHSPGGYSLQ AALVSEVVLT GMFLLIILGA TSKRAPQGFA PIAIGLTLTL IHLISIPVTN
TSVNPARSTA VALYVGDWAV SQLWLFWVAP ILGAVLGALA YRLIGDKND
