ID B0VMJ8_ACIBS Unreviewed; 229 AA. AC B0VMJ8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146}; GN Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146, GN ECO:0000313|EMBL:CAP02612.1}; GN OrderedLocusNames=ABSDF3343 {ECO:0000313|EMBL:CAP02612.1}; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02612.1, ECO:0000313|Proteomes:UP000001741}; RN [1] {ECO:0000313|EMBL:CAP02612.1, ECO:0000313|Proteomes:UP000001741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF {ECO:0000313|EMBL:CAP02612.1, RC ECO:0000313|Proteomes:UP000001741}; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). 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:0000256|HAMAP-Rule:MF_01146}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01146}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01146}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01146}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01146}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass CC membrane protein {ECO:0000256|ARBA:ARBA00004141}. 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). {ECO:0000256|HAMAP-Rule:MF_01146}. CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. CC {ECO:0000256|HAMAP-Rule:MF_01146}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01146}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU468230; CAP02612.1; -; Genomic_DNA. DR AlphaFoldDB; B0VMJ8; -. DR KEGG; abm:ABSDF3343; -. DR HOGENOM; CLU_020019_3_2_6; -. DR Proteomes; UP000001741; Chromosome. 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; Glycerol uptake facilitator protein; 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 NCBIfam; TIGR00861; MIP; 1. DR PANTHER; PTHR19139:SF199; AQUAPORIN; 1. DR PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; Aquaporin-like; 1. DR PROSITE; PS00221; MIP; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP- KW Rule:MF_01146}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01146}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01146}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01146}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01146}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01146}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01146}. FT TRANSMEM 35..53 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT TRANSMEM 80..102 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT TRANSMEM 127..150 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT TRANSMEM 157..178 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT TRANSMEM 204..224 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT MOTIF 62..64 FT /note="NPA 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT MOTIF 184..186 FT /note="NPA 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT SITE 19 FT /note="Involved in tetramerization or stability of the FT tetramer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT SITE 42 FT /note="Selectivity filter" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT SITE 172 FT /note="Selectivity filter" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT SITE 181 FT /note="Selectivity filter" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" FT SITE 187 FT /note="Selectivity filter" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146" SQ SEQUENCE 229 AA; 23443 MW; E6CB05D97950F795 CRC64; MNKYFAEFLG TFWLVFGGCG SAVLAAAFPE LGIGFAGVAL AFGLTVLTGA YALGHISGGH FNPAVSVGLW VGGRFDVKDL IPYIVAQVVG ATAAAFVLYI IAQGQAGFSG VGGFAANGFG DLSPNKFGLG SAFIIEVVLT AFFLIIILGA TDRRAPAGFA PIAIGLGLTL IHLISIPVTN TSVNPARSTG VAFFAETAAL SQLWLFWVAP ILGAVIGAII YKVVAGDKD //