AQPZ1_AGRFC
ID AQPZ1_AGRFC Reviewed; 241 AA.
AC Q8UI24;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Aquaporin Z 1;
GN Name=aqpZ1; OrderedLocusNames=Atu0476; ORFNames=AGR_C_841;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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:0000305}.
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DR EMBL; AE007869; AAK86288.1; -; Genomic_DNA.
DR PIR; AI2634; AI2634.
DR PIR; G97416; G97416.
DR RefSeq; NP_353503.1; NC_003062.2.
DR RefSeq; WP_006313332.1; NC_003062.2.
DR AlphaFoldDB; Q8UI24; -.
DR SMR; Q8UI24; -.
DR STRING; 176299.Atu0476; -.
DR EnsemblBacteria; AAK86288; AAK86288; Atu0476.
DR GeneID; 66220647; -.
DR KEGG; atu:Atu0476; -.
DR PATRIC; fig|176299.10.peg.475; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_3_2_5; -.
DR OMA; CRREDIM; -.
DR PhylomeDB; Q8UI24; -.
DR BioCyc; AGRO:ATU0476-MON; -.
DR Proteomes; UP000000813; Chromosome circular.
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 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..241
FT /note="Aquaporin Z 1"
FT /id="PRO_0000063978"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 63..65
FT /note="NPA 1"
FT MOTIF 184..186
FT /note="NPA 2"
FT SITE 20
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT /evidence="ECO:0000250"
FT SITE 43
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 187
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
SQ SEQUENCE 241 AA; 24544 MW; 49EF4E3D787D5172 CRC64;
MSRKFISEFL GTFWLVFGGC GSAVFAAAFP ELGIGFLGVA FAFGLTVLTM AYAVGGISGG
HFNPAVSVGL TVAGKFPAAN LVPYIVAQVL GAVVAAAALY VILTGKAGAE IGGFAANGYG
EHSPGGYSLL SALLIEIILT AFFLVVILGS THGRVPVGFA PVAIGLALTL IHLISIPVTN
TSVNPARSTG QALFVGGWAL QQLWLFWLAP ILGGAIGAVV WKIFGEEEKA GHAGSVQPAK
T
