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Aquaporin TIP1-1 (Aquaporin TIP) (Gamma-tonoplast intrinsic protein) (Gamma-TIP) (Tonoplast intrinsic protein 1-1) (AtTIP1;1) (Tonoplast intrinsic protein, root-specific RB7)

 TIP11_ARATH             Reviewed;         251 AA.
P25818; P21652; Q42075; Q8L5T8;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
30-AUG-2017, entry version 167.
RecName: Full=Aquaporin TIP1-1;
AltName: Full=Aquaporin TIP;
AltName: Full=Gamma-tonoplast intrinsic protein;
Short=Gamma-TIP;
AltName: Full=Tonoplast intrinsic protein 1-1;
Short=AtTIP1;1;
AltName: Full=Tonoplast intrinsic protein, root-specific RB7;
Name=TIP1-1; Synonyms=AQP.1; OrderedLocusNames=At2g36830;
ORFNames=T1J8.1;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Root;
PubMed=2129561; DOI=10.1093/nar/18.24.7449;
Yamamoto Y.T., Cheng C.-L., Conkling M.A.;
"Root-specific genes from tobacco and Arabidopsis homologous to an
evolutionarily conserved gene family of membrane channel proteins.";
Nucleic Acids Res. 18:7449-7449(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=16668923; DOI=10.1104/pp.99.2.561;
Hoefte H.R., Hubbard L., Reizer J., Ludevid D., Kerman E.M.,
Chrispeels M.J.;
"Vegetative and seed-specific forms of tonoplast intrinsic protein in
the vacuolar membrane of Arabidopsis thaliana.";
Plant Physiol. 99:561-570(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Landsberg erecta; TISSUE=Flower bud;
PubMed=8155880; DOI=10.1007/BF00023557;
Phillips A.L., Huttly A.K.;
"Cloning of two gibberellin-regulated cDNAs from Arabidopsis thaliana
by subtractive hybridization: expression of the tonoplast water
channel, gamma-TIP, is increased by GA3.";
Plant Mol. Biol. 24:603-615(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116 AND 243-251.
STRAIN=cv. Columbia; TISSUE=Seedling;
PubMed=8281187; DOI=10.1046/j.1365-313X.1993.04061051.x;
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
Bardet C., Tremousaygue D., Lescure B.;
"An inventory of 1152 expressed sequence tags obtained by partial
sequencing of cDNAs from Arabidopsis thaliana.";
Plant J. 4:1051-1061(1993).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-207.
STRAIN=cv. Columbia; TISSUE=Seedling;
PubMed=8580968; DOI=10.1046/j.1365-313X.1996.09010101.x;
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y.,
Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C.,
Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F.,
Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H.,
Hoefte H.;
"Further progress towards a catalogue of all Arabidopsis genes:
analysis of a set of 5000 non-redundant ESTs.";
Plant J. 9:101-124(1996).
[10]
FUNCTION.
PubMed=8508761;
Maurel C., Reizer J., Schroeder J.I., Chrispeels M.J.;
"The vacuolar membrane protein gamma-TIP creates water specific
channels in Xenopus oocytes.";
EMBO J. 12:2241-2247(1993).
[11]
TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-118.
PubMed=8624437; DOI=10.1105/tpc.8.4.587;
Daniels M.J., Chaumont F., Mirkov T.E., Chrispeels M.J.;
"Characterization of a new vacuolar membrane aquaporin sensitive to
mercury at a unique site.";
Plant Cell 8:587-599(1996).
[12]
NOMENCLATURE.
PubMed=11806824;
Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
"From genome to function: the Arabidopsis aquaporins.";
Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
[13]
FUNCTION.
PubMed=14576283; DOI=10.1104/pp.103.027409;
Liu L.-H., Ludewig U., Gassert B., Frommer W.B., von Wiren N.;
"Urea transport by nitrogen-regulated tonoplast intrinsic proteins in
Arabidopsis.";
Plant Physiol. 133:1220-1228(2003).
[14]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=15584951; DOI=10.1111/j.1365-313X.2004.02265.x;
Ma S., Quist T.M., Ulanov A., Joly R., Bohnert H.J.;
"Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant
death.";
Plant J. 40:845-859(2004).
[15]
INTERACTION WITH CMV PROTEIN 1A.
PubMed=17030879; DOI=10.1099/vir.0.82252-0;
Kim M.J., Kim H.R., Paek K.-H.;
"Arabidopsis tonoplast proteins TIP1 and TIP2 interact with the
cucumber mosaic virus 1a replication protein.";
J. Gen. Virol. 87:3425-3431(2006).
[16]
FUNCTION.
PubMed=17105724; DOI=10.1074/jbc.M603761200;
Bienert G.P., Moeller A.L.B., Kristiansen K.A., Schulz A.,
Moeller I.M., Schjoerring J.K., Jahn T.P.;
"Specific aquaporins facilitate the diffusion of hydrogen peroxide
across membranes.";
J. Biol. Chem. 282:1183-1192(2007).
-!- FUNCTION: Water channel required to facilitate the transport of
water, diffusion of amino acids and/or peptides from the vacuolar
compartment to the cytoplasm. Does not promote glycerol
permeability. May play a role in the control of cell turgor and
cell expansion. Its function is impaired by Hg(2+). May be
involved in a vesicle-based metabolite routing through or between
pre-vacuolar compartments and the central vacuole. Transports urea
in yeast cells in a pH-independent manner. Transports H(2)O(2) in
yeast cells. {ECO:0000269|PubMed:14576283,
ECO:0000269|PubMed:15584951, ECO:0000269|PubMed:17105724,
ECO:0000269|PubMed:8508761}.
-!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
{ECO:0000269|PubMed:17030879}.
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:15584951}; Multi-pass membrane protein
{ECO:0000269|PubMed:15584951}. Note=Tonoplast. Specifically
located in the tonoplast of lytic or degradative vacuoles (LV) (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: In all the vegetative organs, but not in
seeds. Preferentially expressed in roots.
{ECO:0000269|PubMed:8624437}.
-!- INDUCTION: By gibberellins.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA).
-!- DISRUPTION PHENOTYPE: Plants display lesion formation or plant
death, and low contents of glucose, fructose, inositol, and
threonic, succinic, fumaric, and malic acids.
{ECO:0000269|PubMed:15584951}.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP
(TC 1.A.8.10) subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA38633.1; Type=Frameshift; Positions=244; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X54854; CAA38633.1; ALT_FRAME; mRNA.
EMBL; X63552; CAA45115.1; -; Genomic_DNA.
EMBL; M84344; AAA32806.1; -; Genomic_DNA.
EMBL; X72581; CAA51171.1; -; mRNA.
EMBL; AC006922; AAD31569.1; -; Genomic_DNA.
EMBL; CP002685; AEC09303.1; -; Genomic_DNA.
EMBL; AF370172; AAK43987.1; -; mRNA.
EMBL; AY059134; AAL15240.1; -; mRNA.
EMBL; AY087558; AAM65100.1; -; mRNA.
EMBL; Z18124; CAA79107.1; -; mRNA.
EMBL; Z18771; CAA79247.1; -; mRNA.
EMBL; Z26215; CAA81194.1; -; mRNA.
PIR; S13718; S13718.
PIR; S22202; S22202.
RefSeq; NP_181221.1; NM_129238.4.
UniGene; At.25221; -.
UniGene; At.43252; -.
UniGene; At.67051; -.
ProteinModelPortal; P25818; -.
SMR; P25818; -.
BioGrid; 3599; 12.
IntAct; P25818; 1.
STRING; 3702.AT2G36830.1; -.
TCDB; 1.A.8.10.3; the major intrinsic protein (mip) family.
PaxDb; P25818; -.
PRIDE; P25818; -.
EnsemblPlants; AT2G36830.1; AT2G36830.1; AT2G36830.
GeneID; 818255; -.
Gramene; AT2G36830.1; AT2G36830.1; AT2G36830.
KEGG; ath:AT2G36830; -.
Araport; AT2G36830; -.
TAIR; locus:2057906; AT2G36830.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; P25818; -.
KO; K09873; -.
OMA; INQTHEP; -.
OrthoDB; EOG09360J95; -.
PhylomeDB; P25818; -.
Reactome; R-ATH-432047; Passive transport by Aquaporins.
PRO; PR:P25818; -.
Proteomes; UP000006548; Chromosome 2.
Genevisible; P25818; AT.
GO; GO:0042807; C:central vacuole; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
GO; GO:0000326; C:protein storage vacuole; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0015204; F:urea transmembrane transporter activity; IGI:TAIR.
GO; GO:0015250; F:water channel activity; IDA:TAIR.
GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0015840; P:urea transport; IGI:TAIR.
GO; GO:0006833; P:water transport; IDA:TAIR.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Membrane; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport; Vacuole.
CHAIN 1 251 Aquaporin TIP1-1.
/FTId=PRO_0000064008.
TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.
TRANSMEM 24 44 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 45 56 Vacuolar. {ECO:0000255}.
TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 78 103 Cytoplasmic. {ECO:0000255}.
TRANSMEM 104 124 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 125 143 Vacuolar. {ECO:0000255}.
TRANSMEM 144 164 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 165 172 Cytoplasmic. {ECO:0000255}.
TRANSMEM 173 193 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 194 218 Vacuolar. {ECO:0000255}.
TRANSMEM 219 239 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 240 251 Cytoplasmic. {ECO:0000255}.
MOTIF 85 87 NPA 1.
MOTIF 199 201 NPA 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P61837}.
MUTAGEN 118 118 C->T: Strongly reduces the mercury-
sensitivity.
{ECO:0000269|PubMed:8624437}.
CONFLICT 8 8 I -> V (in Ref. 3; CAA51171).
{ECO:0000305}.
CONFLICT 63 63 V -> L (in Ref. 3; CAA51171 and 7;
AAM65100). {ECO:0000305}.
CONFLICT 96 96 G -> W (in Ref. 9; CAA81194).
{ECO:0000305}.
CONFLICT 131 131 P -> R (in Ref. 9; CAA81194).
{ECO:0000305}.
CONFLICT 132 132 A -> P (in Ref. 1; CAA38633 and 9;
CAA81194). {ECO:0000305}.
SEQUENCE 251 AA; 25620 MW; CECC6BAF42F23302 CRC64;
MPIRNIAIGR PDEATRPDAL KAALAEFIST LIFVVAGSGS GMAFNKLTEN GATTPSGLVA
AAVAHAFGLF VAVSVGANIS GGHVNPAVTF GAFIGGNITL LRGILYWIAQ LLGSVVACLI
LKFATGGLAV PAFGLSAGVG VLNAFVFEIV MTFGLVYTVY ATAIDPKNGS LGTIAPIAIG
FIVGANILAG GAFSGASMNP AVAFGPAVVS WTWTNHWVYW AGPLVGGGIA GLIYEVFFIN
TTHEQLPTTD Y


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