ID A0A1M5YBM0_9GAMM Unreviewed; 231 AA.
AC A0A1M5YBM0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146};
GN ORFNames=SAMN02745129_4040 {ECO:0000313|EMBL:SHI09319.1};
OS Ferrimonas marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=299255 {ECO:0000313|EMBL:SHI09319.1, ECO:0000313|Proteomes:UP000184268};
RN [1] {ECO:0000313|EMBL:SHI09319.1, ECO:0000313|Proteomes:UP000184268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16917 {ECO:0000313|EMBL:SHI09319.1,
RC ECO:0000313|Proteomes:UP000184268};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01146}.
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DR EMBL; FQXG01000007; SHI09319.1; -; Genomic_DNA.
DR RefSeq; WP_067663743.1; NZ_FQXG01000007.1.
DR AlphaFoldDB; A0A1M5YBM0; -.
DR STRING; 299255.SAMN02745129_4040; -.
DR OrthoDB; 9807293at2; -.
DR Proteomes; UP000184268; 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:UP000184268};
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 128..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 199..222
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 185..187
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 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 231 AA; 23302 MW; E7FD14596E393607 CRC64;
MQKYLAECIG TFWLVLGGCG SAVLAAAFPE VGIGLVGVSF AFGLTVLTMA FAIGHISGCH
LNPAVSVGLW AGGRFPANQL LPYIVAQVVG AVIAGAVLYV IASGQAGFDA AASGFASNGY
GEHSPGGYGF TAALVCEVVM TAMFLVVILG ATDSRAPAGF APIAIGLCLT LIHLISIPVT
NTSVNPARST GVALFVGDWA VAQLWLFWLA PIVGAVIGAV LYKAIGSGGD E
//
