ID D5ER88_CORAD Unreviewed; 231 AA.
AC D5ER88;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146};
GN OrderedLocusNames=Caka_2919 {ECO:0000313|EMBL:ADE55932.1};
OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS KCTC 12865 / 04OKA010-24).
OC Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC Coraliomargaritaceae; Coraliomargarita.
OX NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE55932.1, ECO:0000313|Proteomes:UP000000925};
RN [1] {ECO:0000313|EMBL:ADE55932.1, ECO:0000313|Proteomes:UP000000925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC {ECO:0000313|Proteomes:UP000000925};
RX PubMed=21304713; DOI=10.4056/sigs.952166;
RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Coraliomargarita akajimensis type strain
RT (04OKA010-24).";
RL Stand. Genomic Sci. 2:290-299(2010).
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}.
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; CP001998; ADE55932.1; -; Genomic_DNA.
DR RefSeq; WP_013044650.1; NC_014008.1.
DR AlphaFoldDB; D5ER88; -.
DR STRING; 583355.Caka_2919; -.
DR KEGG; caa:Caka_2919; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_3_2_0; -.
DR OrthoDB; 9807293at2; -.
DR Proteomes; UP000000925; 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:UP000000925};
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..53
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT TRANSMEM 84..108
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 205..225
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; 23550 MW; EEB994BB2C9CF161 CRC64;
MQKYLAEFIG TFWLVLGGCG SAVLAAAFPE VGIGLLGVSF AFGLTVLTMA YAIGHISGCH
LNPAVSVGLF LGGRFEGKDL PGYIIAQVLG GVVGAGVLYL IASGQAGFDA AASGFASNGY
GEHSPGQYSM MAGFVCEVVM TMMFLIIILG ATDGRAPAGF APIAIGLGLT LIHLISIPIT
NTSVNPARST GVAVFQGGWA LGQLWLFWVA PIIGGALGAI VYKVIGCSKD D
//
