ID   AQPZ2_AGRFC             Reviewed;         228 AA.
AC   Q8UJW4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Aquaporin Z 2;
GN   Name=aqpZ2; OrderedLocusNames=Atu5361; ORFNames=AGR_pAT_521;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OG   Plasmid AT.
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].
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE007872; AAK90735.1; -; Genomic_DNA.
DR   PIR; AC3204; AC3204.
DR   RefSeq; NP_396294.1; NC_003064.2.
DR   RefSeq; WP_010974613.1; NC_003064.2.
DR   PDB; 3LLQ; X-ray; 2.01 A; A/B=1-228.
DR   PDBsum; 3LLQ; -.
DR   AlphaFoldDB; Q8UJW4; -.
DR   SMR; Q8UJW4; -.
DR   STRING; 176299.Atu5361; -.
DR   EnsemblBacteria; AAK90735; AAK90735; Atu5361.
DR   KEGG; atu:Atu5361; -.
DR   PATRIC; fig|176299.10.peg.5033; -.
DR   eggNOG; COG0580; Bacteria.
DR   HOGENOM; CLU_020019_3_2_5; -.
DR   OMA; IFKALMY; -.
DR   PhylomeDB; Q8UJW4; -.
DR   BioCyc; AGRO:ATU5361-MON; -.
DR   EvolutionaryTrace; Q8UJW4; -.
DR   Proteomes; UP000000813; Plasmid At.
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; PTHR19139; PTHR19139; 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   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane; Plasmid;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..228
FT                   /note="Aquaporin Z 2"
FT                   /id="PRO_0000063979"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..61
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"
FT   HELIX           2..26
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           35..58
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           64..72
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           81..103
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   TURN            112..115
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           129..151
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           160..179
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           185..195
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           197..202
FT                   /evidence="ECO:0007829|PDB:3LLQ"
FT   HELIX           205..224
FT                   /evidence="ECO:0007829|PDB:3LLQ"
SQ   SEQUENCE   228 AA;  23138 MW;  89E474EF895D50D3 CRC64;
     MGRKLLAEFF GTFWLVFGGC GSAVFAAAFP ELGIGFTGVA LAFGLTVLTM AYAVGGISGG
     HFNPAVSVGL TVAGRFPASS LVPYVIAQVA GAIVAAAALY VIATGKAGID LGGFASNGYG
     EHSPGGYSLV SALLIEIILT AFFLIVILGS THGRVPAGFA PIAIGLALTL IHLISIPVTN
     TSVNPARSTG QALFVGGWAL QQLWLFWLAP IVGGAAGAVI WKLFGEKD