ID A0A0M2WN23_9BURK Unreviewed; 229 AA.
AC A0A0M2WN23;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146,
GN ECO:0000313|EMBL:KKO62673.1};
GN ORFNames=VM94_03671 {ECO:0000313|EMBL:KKO62673.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO62673.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO62673.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO62673.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-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:KKO62673.1}.
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DR EMBL; LBCO01000029; KKO62673.1; -; Genomic_DNA.
DR RefSeq; WP_034758233.1; NZ_VCCE02000001.1.
DR AlphaFoldDB; A0A0M2WN23; -.
DR PATRIC; fig|1649647.5.peg.3762; -.
DR Proteomes; UP000034315; 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:UP000034315};
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..59
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 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 229 AA; 23463 MW; 7AC65B0B9D81478A CRC64;
MKQYGAEFLG TFWLVLGGCG SAVLAAAFPG LGIGFVGVAL AFGLTVLTMA YAIGHISGCH
LNPAVSIGLW AGGRFPASQL LPYIIAQVLG AIVAGGVLYV IASGQAGFDV SKGFASNGFG
AHSPGGYSML SALVIEIVLT MFFLIVILGA TDKRAPAGFA PLPIGLALTL IHLISIPVTN
TSVNPARSTG VALYVGDWAT SQLWLFWLAP IIGALLGALA YRLIAGEKE
//
