AQPZ_CHRVO
ID AQPZ_CHRVO Reviewed; 229 AA.
AC Q7NU39;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=CV_2864;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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:0000255|HAMAP-Rule:MF_01146}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01146}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01146}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01146}.
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).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000255|HAMAP-Rule:MF_01146}.
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DR EMBL; AE016825; AAQ60532.1; -; Genomic_DNA.
DR RefSeq; WP_011136411.1; NC_005085.1.
DR AlphaFoldDB; Q7NU39; -.
DR SMR; Q7NU39; -.
DR STRING; 243365.CV_2864; -.
DR EnsemblBacteria; AAQ60532; AAQ60532; CV_2864.
DR KEGG; cvi:CV_2864; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_3_2_4; -.
DR OMA; IFKALMY; -.
DR OrthoDB; 1744995at2; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 PANTHER; PTHR45724; PTHR45724; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..229
FT /note="Aquaporin Z"
FT /id="PRO_0000063987"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT MOTIF 62..64
FT /note="NPA 1"
FT MOTIF 184..186
FT /note="NPA 2"
FT SITE 19
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 42
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 172
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 181
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT SITE 187
FT /note="Selectivity filter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ SEQUENCE 229 AA; 23228 MW; 7BAB722B2B6F197B CRC64;
MKSYGAEFLG TFWLVLGGCG SAVLAAGFPN LGIGFAGVAL AFGLTVVTMA YAIGHISGCH
LNPAVSIGLW AGGRFPAGQL APYIVAQVLG AIAAGAVLYV IASGGAGFDV AKGFASNGYA
EHSPGGYSLL AALVCEVVMT MFFLLVIMGA TDKRAPAGFA PLAIGLALTL IHLISIPVTN
TSVNPARSTG VALFVGGWAV QQLWLFWLAP IIGAVLGAKV YRLIAGESE
