ID   TIP12_MUSAC             Reviewed;         252 AA.
AC   P0DO54;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=Aquaporin TIP1-2 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:29778840};
DE   AltName: Full=Tonoplast intrinsic protein 1-2 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:29778840};
DE            Short=MaTIP1-2 {ECO:0000303|PubMed:26307965};
DE            Short=MaTIP1;2 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:29778840};
GN   Name=TIP1-2 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:29778840};
OS   Musa acuminata (Banana) (Musa cavendishii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=4641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY SALT, GENE
RP   FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Cavendish (AAA);
RX   PubMed=26307965; DOI=10.3390/ijms160819728;
RA   Hu W., Hou X., Huang C., Yan Y., Tie W., Ding Z., Wei Y., Liu J., Miao H.,
RA   Lu Z., Li M., Xu B., Jin Z.;
RT   "Genome-wide identification and expression analyses of aquaporin gene
RT   family during development and abiotic stress in banana.";
RL   Int. J. Mol. Sci. 16:19728-19751(2015).
RN   [2]
RP   TISSUE SPECIFICITY, INDUCTION BY DROUGHT AND SALT, AND BIOTECHNOLOGY.
RX   PubMed=29778840; DOI=10.1016/j.plaphy.2018.05.003;
RA   Song S., Xu Y., Huang D., Miao H., Liu J., Jia C., Hu W., Valarezo A.V.,
RA   Xu B., Jin Z.;
RT   "Identification of a novel promoter from banana aquaporin family gene
RT   (MaTIP1;2) which responses to drought and salt-stress in transgenic
RT   Arabidopsis thaliana.";
RL   Plant Physiol. Biochem. 128:163-169(2018).
CC   -!- FUNCTION: Water channel required to facilitate the transport of water
CC       from the vacuolar compartment to the cytoplasm.
CC       {ECO:0000250|UniProtKB:P26587}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P26587};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in fruits and leaves, and, to a
CC       lower extent, in roots, stems and flowers.
CC       {ECO:0000269|PubMed:26307965, ECO:0000269|PubMed:29778840}.
CC   -!- INDUCTION: Induced by salt (NaCl) (PubMed:26307965, PubMed:29778840).
CC       Triggered by drought (PubMed:29778840). {ECO:0000269|PubMed:26307965,
CC       ECO:0000269|PubMed:29778840}.
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:0000305}.
CC   -!- BIOTECHNOLOGY: May be used to improve drought and salt stresses
CC       resistance. {ECO:0000305|PubMed:29778840}.
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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PE   2: Evidence at transcript level;
KW   Membrane; Stress response; Transmembrane; Transmembrane helix; Transport;
KW   Vacuole.
FT   CHAIN           1..252
FT                   /note="Aquaporin TIP1-2"
FT                   /id="PRO_0000455810"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        24..44
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..55
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        56..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        104..124
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..143
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        144..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        173..193
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..219
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        220..240
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   MOTIF           85..87
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000255"
FT   MOTIF           199..201
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   252 AA;  25732 MW;  1EE2737529EEC309 CRC64;
     MPIGSIAIGA PGEASHPDTI KASLAEFIST LIFVFAGEGS GMAFNKLTND GSTTPAGLVA
     ASLAHGFALF VAVSVGANIS GGHVNPAVTF GAFLGGNISL IRGILYWIAQ LLGSVVACLL
     LKLATGGLET SAFSLSSDVS VWNAVVFEIV MTFGLVYTVY ATAVDPRKGD LGVIAPIAIG
     FIVGANILAG GAFDGASMNP AVSFGPAVVS WTWDNHWVYW VGPLIGAAIA ALVYDGVFIG
     QATHEQLPPS DY