TIP12_ARATH
ID TIP12_ARATH Reviewed; 253 AA.
AC Q41963; O23117; O82446; Q9LRV6;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Aquaporin TIP1-2;
DE AltName: Full=Gamma-tonoplast intrinsic protein 2;
DE Short=Gamma-TIP2;
DE AltName: Full=Salt stress-induced tonoplast intrinsic protein;
DE AltName: Full=Tonoplast intrinsic protein 1-2;
DE Short=AtTIP1;2;
GN Name=TIP1-2; Synonyms=SITIP, TIP2; OrderedLocusNames=At3g26520;
GN ORFNames=MFE16.17;
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], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10102577;
RA Pih K.T., Kabilan V., Lim J.H., Kang S.G., Piao H.L., Jin J.B., Hwang I.;
RT "Characterization of two new channel protein genes in Arabidopsis.";
RL Mol. Cells 9:84-90(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Young L.W., Bonham-Smith P.C.;
RT "Molecular cloning and characterization of a new member of the Arabidopsis
RT thaliana tonoplast intrinsic protein (gTIP) family.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-122.
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
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 [9]
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 [10]
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 across cell membrane. May be involved in the osmoregulation in plants
CC under high osmotic stress such as under a high salt condition.
CC Transports urea in yeast cells in a pH-independent manner. Transports
CC H(2)O(2) in yeast cells. {ECO:0000269|PubMed:10102577,
CC ECO:0000269|PubMed:14576283, ECO:0000269|PubMed:17105724}.
CC -!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
CC {ECO:0000269|PubMed:17030879}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14576283};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14576283}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Widely expressed. Predominantly expressed in roots.
CC -!- DEVELOPMENTAL STAGE: Starts to be expressed in seedlings from 2 days
CC ays after germination. {ECO:0000269|PubMed:14576283}.
CC -!- INDUCTION: By NaCl and abscisic acid (ABA) treatments.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62692.1; Type=Miscellaneous discrepancy; Note=Duplication of 20 AA in position 80.; Evidence={ECO:0000305};
CC Sequence=CAA79103.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF004393; AAB62692.1; ALT_SEQ; mRNA.
DR EMBL; AF057137; AAC62397.1; -; mRNA.
DR EMBL; AB028611; BAB01832.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77174.1; -; Genomic_DNA.
DR EMBL; AF419613; AAL31945.1; -; mRNA.
DR EMBL; AF428341; AAL16271.1; -; mRNA.
DR EMBL; AY079114; AAL84998.1; -; mRNA.
DR EMBL; Z18111; CAA79103.1; ALT_FRAME; mRNA.
DR PIR; T51819; T51819.
DR RefSeq; NP_189283.1; NM_113559.4.
DR AlphaFoldDB; Q41963; -.
DR SMR; Q41963; -.
DR BioGRID; 7590; 2.
DR STRING; 3702.AT3G26520.1; -.
DR TCDB; 1.A.8.10.9; the major intrinsic protein (mip) family.
DR PaxDb; Q41963; -.
DR PRIDE; Q41963; -.
DR ProteomicsDB; 246427; -.
DR EnsemblPlants; AT3G26520.1; AT3G26520.1; AT3G26520.
DR GeneID; 822259; -.
DR Gramene; AT3G26520.1; AT3G26520.1; AT3G26520.
DR KEGG; ath:AT3G26520; -.
DR Araport; AT3G26520; -.
DR TAIR; locus:2088867; AT3G26520.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR OMA; IDENAHE; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q41963; -.
DR PRO; PR:Q41963; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q41963; baseline and differential.
DR Genevisible; Q41963; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0043674; C:columella; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; 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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; ISS:TAIR.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
DR GO; GO:0030104; P:water homeostasis; IDA:TAIR.
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 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..253
FT /note="Aquaporin TIP1-2"
FT /id="PRO_0000064009"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..57
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..144
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..219
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 86..88
FT /note="NPA 1"
FT MOTIF 200..202
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT CONFLICT 65
FT /note="A -> S (in Ref. 2; AAC62397)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="G -> R (in Ref. 2; AAC62397)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="G -> A (in Ref. 2; AAC62397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 25849 MW; 939282A6E7FC009E CRC64;
MPTRNIAIGG VQEEVYHPNA LRAALAEFIS TLIFVFAGSG SGIAFNKITD NGATTPSGLV
AAALAHAFGL FVAVSVGANI SGGHVNPAVT FGVLLGGNIT LLRGILYWIA QLLGSVAACF
LLSFATGGEP IPAFGLSAGV GSLNALVFEI VMTFGLVYTV YATAVDPKNG SLGTIAPIAI
GFIVGANILA GGAFSGASMN PAVAFGPAVV SWTWTNHWVY WAGPLIGGGL AGIIYDFVFI
DENAHEQLPT TDY
