TIP11_ARATH
ID TIP11_ARATH Reviewed; 251 AA.
AC P25818; P21652; Q42075; Q8L5T8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Aquaporin TIP1-1;
DE AltName: Full=Aquaporin TIP;
DE AltName: Full=Gamma-tonoplast intrinsic protein;
DE Short=Gamma-TIP;
DE AltName: Full=Tonoplast intrinsic protein 1-1;
DE Short=AtTIP1;1;
DE AltName: Full=Tonoplast intrinsic protein, root-specific RB7;
GN Name=TIP1-1; Synonyms=AQP.1; OrderedLocusNames=At2g36830; ORFNames=T1J8.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=2129561; DOI=10.1093/nar/18.24.7449;
RA Yamamoto Y.T., Cheng C.-L., Conkling M.A.;
RT "Root-specific genes from tobacco and Arabidopsis homologous to an
RT evolutionarily conserved gene family of membrane channel proteins.";
RL Nucleic Acids Res. 18:7449-7449(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=16668923; DOI=10.1104/pp.99.2.561;
RA Hoefte H.R., Hubbard L., Reizer J., Ludevid D., Kerman E.M.,
RA Chrispeels M.J.;
RT "Vegetative and seed-specific forms of tonoplast intrinsic protein in the
RT vacuolar membrane of Arabidopsis thaliana.";
RL Plant Physiol. 99:561-570(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower bud;
RX PubMed=8155880; DOI=10.1007/bf00023557;
RA Phillips A.L., Huttly A.K.;
RT "Cloning of two gibberellin-regulated cDNAs from Arabidopsis thaliana by
RT subtractive hybridization: expression of the tonoplast water channel,
RT gamma-TIP, is increased by GA3.";
RL Plant Mol. Biol. 24:603-615(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116 AND 243-251.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-207.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [10]
RP FUNCTION.
RX PubMed=8508761; DOI=10.1002/j.1460-2075.1993.tb05877.x;
RA Maurel C., Reizer J., Schroeder J.I., Chrispeels M.J.;
RT "The vacuolar membrane protein gamma-TIP creates water specific channels in
RT Xenopus oocytes.";
RL EMBO J. 12:2241-2247(1993).
RN [11]
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-118.
RX PubMed=8624437; DOI=10.2307/3870337;
RA Daniels M.J., Chaumont F., Mirkov T.E., Chrispeels M.J.;
RT "Characterization of a new vacuolar membrane aquaporin sensitive to mercury
RT at a unique site.";
RL Plant Cell 8:587-599(1996).
RN [12]
RP NOMENCLATURE.
RX PubMed=11806824; DOI=10.1186/gb-2001-3-1-research0001;
RA Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
RT "From genome to function: the Arabidopsis aquaporins.";
RL Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
RN [13]
RP FUNCTION.
RX PubMed=14576283; DOI=10.1104/pp.103.027409;
RA Liu L.-H., Ludewig U., Gassert B., Frommer W.B., von Wiren N.;
RT "Urea transport by nitrogen-regulated tonoplast intrinsic proteins in
RT Arabidopsis.";
RL Plant Physiol. 133:1220-1228(2003).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=15584951; DOI=10.1111/j.1365-313x.2004.02265.x;
RA Ma S., Quist T.M., Ulanov A., Joly R., Bohnert H.J.;
RT "Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant death.";
RL Plant J. 40:845-859(2004).
RN [15]
RP INTERACTION WITH CMV PROTEIN 1A.
RX PubMed=17030879; DOI=10.1099/vir.0.82252-0;
RA Kim M.J., Kim H.R., Paek K.-H.;
RT "Arabidopsis tonoplast proteins TIP1 and TIP2 interact with the cucumber
RT mosaic virus 1a replication protein.";
RL J. Gen. Virol. 87:3425-3431(2006).
RN [16]
RP FUNCTION.
RX PubMed=17105724; DOI=10.1074/jbc.m603761200;
RA Bienert G.P., Moeller A.L.B., Kristiansen K.A., Schulz A., Moeller I.M.,
RA Schjoerring J.K., Jahn T.P.;
RT "Specific aquaporins facilitate the diffusion of hydrogen peroxide across
RT membranes.";
RL J. Biol. Chem. 282:1183-1192(2007).
CC -!- FUNCTION: Water channel required to facilitate the transport of water,
CC diffusion of amino acids and/or peptides from the vacuolar compartment
CC to the cytoplasm. Does not promote glycerol permeability. May play a
CC role in the control of cell turgor and cell expansion. Its function is
CC impaired by Hg(2+). May be involved in a vesicle-based metabolite
CC routing through or between pre-vacuolar compartments and the central
CC vacuole. Transports urea in yeast cells in a pH-independent manner.
CC Transports H(2)O(2) in yeast cells. {ECO:0000269|PubMed:14576283,
CC ECO:0000269|PubMed:15584951, ECO:0000269|PubMed:17105724,
CC ECO:0000269|PubMed:8508761}.
CC -!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
CC {ECO:0000269|PubMed:17030879}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15584951};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15584951}.
CC Note=Tonoplast. Specifically located in the tonoplast of lytic or
CC degradative vacuoles (LV) (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In all the vegetative organs, but not in seeds.
CC Preferentially expressed in roots. {ECO:0000269|PubMed:8624437}.
CC -!- INDUCTION: By gibberellins.
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 -!- DISRUPTION PHENOTYPE: Plants display lesion formation or plant death,
CC and low contents of glucose, fructose, inositol, and threonic,
CC succinic, fumaric, and malic acids. {ECO:0000269|PubMed:15584951}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP (TC
CC 1.A.8.10) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA38633.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X54854; CAA38633.1; ALT_FRAME; mRNA.
DR EMBL; X63552; CAA45115.1; -; Genomic_DNA.
DR EMBL; M84344; AAA32806.1; -; Genomic_DNA.
DR EMBL; X72581; CAA51171.1; -; mRNA.
DR EMBL; AC006922; AAD31569.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09303.1; -; Genomic_DNA.
DR EMBL; AF370172; AAK43987.1; -; mRNA.
DR EMBL; AY059134; AAL15240.1; -; mRNA.
DR EMBL; AY087558; AAM65100.1; -; mRNA.
DR EMBL; Z18124; CAA79107.1; -; mRNA.
DR EMBL; Z18771; CAA79247.1; -; mRNA.
DR EMBL; Z26215; CAA81194.1; -; mRNA.
DR PIR; S13718; S13718.
DR PIR; S22202; S22202.
DR RefSeq; NP_181221.1; NM_129238.4.
DR AlphaFoldDB; P25818; -.
DR SMR; P25818; -.
DR BioGRID; 3599; 12.
DR IntAct; P25818; 11.
DR STRING; 3702.AT2G36830.1; -.
DR TCDB; 1.A.8.10.3; the major intrinsic protein (mip) family.
DR PaxDb; P25818; -.
DR ProteomicsDB; 234358; -.
DR EnsemblPlants; AT2G36830.1; AT2G36830.1; AT2G36830.
DR GeneID; 818255; -.
DR Gramene; AT2G36830.1; AT2G36830.1; AT2G36830.
DR KEGG; ath:AT2G36830; -.
DR Araport; AT2G36830; -.
DR TAIR; locus:2057906; AT2G36830.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; P25818; -.
DR OMA; RPPYMSS; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P25818; -.
DR PRO; PR:P25818; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P25818; baseline and differential.
DR Genevisible; P25818; AT.
DR GO; GO:0042807; C:central vacuole; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0000326; C:protein storage vacuole; IDA:TAIR.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
DR GO; GO:0015840; P:urea transport; IGI:TAIR.
DR GO; GO:0006833; P:water transport; IDA:TAIR.
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 PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..251
FT /note="Aquaporin TIP1-1"
FT /id="PRO_0000064008"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..56
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..143
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..218
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 85..87
FT /note="NPA 1"
FT MOTIF 199..201
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MUTAGEN 118
FT /note="C->T: Strongly reduces the mercury-sensitivity."
FT /evidence="ECO:0000269|PubMed:8624437"
FT CONFLICT 8
FT /note="I -> V (in Ref. 3; CAA51171)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="V -> L (in Ref. 3; CAA51171 and 7; AAM65100)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="G -> W (in Ref. 9; CAA81194)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="P -> R (in Ref. 9; CAA81194)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="A -> P (in Ref. 1; CAA38633 and 9; CAA81194)"
FT /evidence="ECO:0000305"
SQ 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
