ID I0II39_PHYMF Unreviewed; 252 AA.
AC I0II39;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146,
GN ECO:0000313|EMBL:BAM04927.1};
GN OrderedLocusNames=PSMK_27680 {ECO:0000313|EMBL:BAM04927.1};
OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM04927.1, ECO:0000313|Proteomes:UP000007881};
RN [1] {ECO:0000313|EMBL:BAM04927.1, ECO:0000313|Proteomes:UP000007881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC {ECO:0000313|Proteomes:UP000007881};
RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL Submitted (FEB-2012) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01146}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01146}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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; AP012338; BAM04927.1; -; Genomic_DNA.
DR RefSeq; WP_014438137.1; NC_017080.1.
DR AlphaFoldDB; I0II39; -.
DR STRING; 1142394.PSMK_27680; -.
DR GeneID; 80848934; -.
DR KEGG; phm:PSMK_27680; -.
DR PATRIC; fig|1142394.8.peg.2864; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_3_2_0; -.
DR OrthoDB; 9807293at2; -.
DR Proteomes; UP000007881; Chromosome.
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, ECO:0000256|HAMAP-
KW Rule:MF_01146};
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:UP000007881};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 86..109
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT MOTIF 65..67
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 22
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT SITE 45
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 252 AA; 25428 MW; EF191E74864192D7 CRC64;
MGLLKKCSAE AVGTFWLVFG GCGSAVLAAG FPEVGIGLLG VSLAFGLTVL TMAFAIGHIS
GCHLNPAVTL GLVVAKRFPA AELGPYWLSQ LAGGIAAAAV LFVIASGQAD WSAAESGFAA
NGFGEHSPGG FTLVAALTAE FVLTAMFLLV ILGATDVRAP KGFAPIAIGL GLTLIHLISI
PVTNTSVNPA RSTGPALFVG GWAIMQLWLF WVAPLAGAAA GGLLHLGFFA QEAEEGEDAV
NAGKVVLPNT EA
//
