ID   TIP22_MAIZE             Reviewed;         250 AA.
AC   Q9ATL8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Aquaporin TIP2-2;
DE   AltName: Full=Tonoplast intrinsic protein 2-2;
DE   AltName: Full=ZmTIP2-2;
DE   AltName: Full=ZmTIP2;2;
GN   Name=TIP2-2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. B73;
RX   PubMed=11244102; DOI=10.1104/pp.125.3.1206;
RA   Chaumont F., Barrieu F., Wojcik E., Chrispeels M.J., Jung R.;
RT   "Aquaporins constitute a large and highly divergent protein family in
RT   maize.";
RL   Plant Physiol. 125:1206-1215(2001).
CC   -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC       neutral solutes across cell membranes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=Tonoplast.
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. TIP (TC
CC       1.A.8.10) subfamily. {ECO:0000305}.
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DR   EMBL; AF326502; AAK26769.1; -; mRNA.
DR   RefSeq; NP_001105031.1; NM_001111561.1.
DR   AlphaFoldDB; Q9ATL8; -.
DR   SMR; Q9ATL8; -.
DR   STRING; 4577.GRMZM2G056908_P01; -.
DR   PaxDb; Q9ATL8; -.
DR   GeneID; 541895; -.
DR   KEGG; zma:541895; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_4_1; -.
DR   OMA; YILFPQS; -.
DR   OrthoDB; 1152704at2759; -.
DR   Proteomes; UP000007305; Chromosome 5.
DR   ExpressionAtlas; Q9ATL8; baseline and differential.
DR   Genevisible; Q9ATL8; ZM.
DR   GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0032586; C:protein storage vacuole membrane; TAS:AgBase.
DR   GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR   GO; GO:0006833; P:water transport; IBA:GO_Central.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR45665; PTHR45665; 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   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Vacuole.
FT   CHAIN           1..250
FT                   /note="Aquaporin TIP2-2"
FT                   /id="PRO_0000286004"
FT   TRANSMEM        22..42
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..119
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           83..85
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           197..199
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   250 AA;  25044 MW;  DA97D42821EEA5AF CRC64;
     MVKLAFGSVG DSFSVTSIKA YVAEFIATLL FVFAGVGSAI AFGQLTNGGA LDPAGLVAIA
     VAHALALFVG VSVAANTSGG HLNPAVTFGL AVGGHITVLT GLFYWVAQLL GASVACLLLR
     FVTHGKAIPT HGVSGGTTEL EGVVFEIVIT FALVYTVYAT AADPKKGSLG TIAPIAIGFI
     VGANILAAGP FSGGSMNPAR SFGPAVAAAD FAGNWVYWVG PLIGGGLAGL VYGDVFIGGS
     YQQVADQDYA