ID A0A1H7ENB1_9BURK Unreviewed; 235 AA.
AC A0A1H7ENB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146};
GN ORFNames=SAMN05518853_117104 {ECO:0000313|EMBL:SEK15399.1};
OS Variovorax sp. OK202.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEK15399.1, ECO:0000313|Proteomes:UP000199192};
RN [1] {ECO:0000313|EMBL:SEK15399.1, ECO:0000313|Proteomes:UP000199192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK202 {ECO:0000313|EMBL:SEK15399.1,
RC ECO:0000313|Proteomes:UP000199192};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000256|HAMAP-Rule:MF_01146};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01146}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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}.
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DR EMBL; FNZJ01000017; SEK15399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7ENB1; -.
DR Proteomes; UP000199192; Unassembled WGS sequence.
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; PTHR45724:SF13; AQUAPORIN NIP1-1-RELATED; 1.
DR PANTHER; PTHR45724; AQUAPORIN NIP2-1; 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};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 131..152
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 208..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT MOTIF 67..69
FT /note="NPA 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT MOTIF 188..190
FT /note="NPA 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT SITE 24
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT SITE 47
FT /note="Selectivity filter"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT SITE 176
FT /note="Selectivity filter"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT SITE 185
FT /note="Selectivity filter"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT SITE 191
FT /note="Selectivity filter"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
SQ SEQUENCE 235 AA; 23598 MW; E63C1AFB1B836D9A CRC64;
MEHSTYKKWS AEFIGTFWLT LGGCGSAVLA AAFPGTGIGF LGVALAFGLT VVTGAYALGP
ISGGHFNPAV SIGLAAAGRF KASQLAGYIV AQVLGAIAAA GVLYLIATGK PGADIGGFAT
NGYGEHSPGK YGLTAALLCE VVMTAVFLIV ILGSTAKRAA GGFAGLAIGL CLTLIHLISI
PVTNTSVNPA RSTGPALFGP SHAMSELWLF WVAPIAGALI GAAIYRALLS NSNDD
//
