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Database: UniProt
Entry: A0A1H6VDV3_9RHOB
LinkDB: A0A1H6VDV3_9RHOB
Original site: A0A1H6VDV3_9RHOB 
ID   A0A1H6VDV3_9RHOB        Unreviewed;       229 AA.
AC   A0A1H6VDV3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN   Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146};
GN   ORFNames=SAMN05444007_103162 {ECO:0000313|EMBL:SEJ02723.1};
OS   Cribrihabitans marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cribrihabitans.
OX   NCBI_TaxID=1227549 {ECO:0000313|EMBL:SEJ02723.1, ECO:0000313|Proteomes:UP000199379};
RN   [1] {ECO:0000313|EMBL:SEJ02723.1, ECO:0000313|Proteomes:UP000199379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29340 {ECO:0000313|EMBL:SEJ02723.1,
RC   ECO:0000313|Proteomes:UP000199379};
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; FNYD01000003; SEJ02723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6VDV3; -.
DR   STRING; 1227549.SAMN05444007_103162; -.
DR   OrthoDB; 9807293at2; -.
DR   Proteomes; UP000199379; 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:UP000199379};
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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        33..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        81..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   MOTIF           63..65
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   MOTIF           185..187
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            20
FT                   /note="Involved in tetramerization or stability of the
FT                   tetramer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            43
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            173
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            182
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            188
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
SQ   SEQUENCE   229 AA;  23274 MW;  EA38E76442AF1842 CRC64;
     MVQRLSAEFL GTFWLVFGGC GSAIFAASVA NVGIGWLGVS LAFGLTVLTM AYAVGHISGG
     HFNPAVSLGL MLAGKFEGKD LIPYWIAQVL GGIVAALVLY IMVSGGPEFE GVGGFASNGY
     GAASPGGYSM AAALVAEIVL TAFFIFIILG ATSRGAPPGF APIAIGLALT LIHLVSIPIT
     NTSVNPARST GMALFADAPA LAQLWLFWVA PLIGGALGGL LWKAVADDD
//
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