ID A0A0Q6W9G4_9BURK Unreviewed; 230 AA.
AC A0A0Q6W9G4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146};
GN ORFNames=ASD15_30475 {ECO:0000313|EMBL:KQV85359.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV85359.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV85359.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV85359.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV85359.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV85359.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01146}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQV85359.1}.
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DR EMBL; LMDJ01000010; KQV85359.1; -; Genomic_DNA.
DR RefSeq; WP_057155351.1; NZ_LMDJ01000010.1.
DR AlphaFoldDB; A0A0Q6W9G4; -.
DR OrthoDB; 9807293at2; -.
DR Proteomes; UP000051876; 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; 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};
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 Reference proteome {ECO:0000313|Proteomes:UP000051876};
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 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 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 203..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 230 AA; 23298 MW; 8383EC91A1FD7C9C CRC64;
MKAYGAEFVG TFWLVLGGCG SAVLAAAFPG VGIGLLGVSL AFGLTVLTMA YAIGHISGCH
LNPAVSIGLW AGGRFPASKL LPYIVAQVLG AIAAGGVLYL IASGKAGFSL AGGLASNGYG
EHSPGGYSLT AALVTEVVMT MMFLIVILGA TDRRAPAGFA PLPIGLALTL IHLISIPVTN
TSVNPARSTG VGVYVGDWAV SQLWLFWLAP IAGAVLGALV YRLIADEAKN
//
