TIP21_ARATH
ID TIP21_ARATH Reviewed; 250 AA.
AC Q41951; Q0WM76; Q42200; Q42201; Q43352; Q8VZ81;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Aquaporin TIP2-1;
DE AltName: Full=Delta-tonoplast intrinsic protein;
DE Short=Delta-TIP;
DE AltName: Full=Tonoplast intrinsic protein 2-1;
DE Short=AtTIP2;1;
DE Contains:
DE RecName: Full=Aquaporin TIP2-1, N-terminally processed;
GN Name=TIP2-1; OrderedLocusNames=At3g16240; ORFNames=MYA6.10;
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-116.
RC STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-106.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-250.
RC STRAIN=cv. Columbia; TISSUE=Shoot;
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=10737809; DOI=10.1073/pnas.97.7.3718;
RA Cutler S.R., Ehrhardt D.W., Griffitts J.S., Somerville C.R.;
RT "Random GFP::cDNA fusions enable visualization of subcellular structures in
RT cells of Arabidopsis at a high frequency.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3718-3723(2000).
RN [10]
RP NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [11]
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 [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=15665250; DOI=10.1104/pp.104.051268;
RA Loque D., Ludewig U., Yuan L., von Wiren N.;
RT "Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3
RT transport into the vacuole.";
RL Plant Physiol. 137:671-680(2005).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Aquaporin required to facilitate the transport of water from
CC the vacuolar compartment to the cytoplasm. Does not promote glycerol
CC permeability. Its function is impaired by Hg(2+). Transports urea in
CC yeast cells and Xenopus laevis oocytes in a pH-independent manner.
CC Transports methylammonium or ammonium in yeast cells and Xenopus laevis
CC oocytes, preferentially at high medium pH. May participate in vacuolar
CC compartmentation and detoxification of ammonium.
CC {ECO:0000269|PubMed:14576283, ECO:0000269|PubMed:15665250,
CC ECO:0000269|PubMed:8624437}.
CC -!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
CC {ECO:0000269|PubMed:17030879}.
CC -!- INTERACTION:
CC Q41951; Q41951: TIP2-1; NbExp=2; IntAct=EBI-4442669, EBI-4442669;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10737809,
CC ECO:0000269|PubMed:14576283, ECO:0000269|PubMed:17151019,
CC ECO:0000269|PubMed:8624437}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:10737809, ECO:0000269|PubMed:14576283,
CC ECO:0000269|PubMed:8624437}. Note=Tonoplast. It is specifically located
CC in the tonoplast of protein storage vacuoles (PSV) (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in shoot, rosette, bolt and
CC flowers. Also expressed in roots, flower buds and above ground.
CC {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:8624437}.
CC -!- DEVELOPMENTAL STAGE: Starts to be expressed in seedlings from 2 days
CC ays after germination. {ECO:0000269|PubMed:14576283}.
CC -!- INDUCTION: By ammonium nitrate in roots. Expressed in roots with a
CC circadian rhythm showing an increase after onset of light, a peak
CC approximately at midday and a decline to lowest levels before offset of
CC light. {ECO:0000269|PubMed:15665250}.
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 -!- CAUTION: Was originally assigned as At3g16230, which is now a
CC completely different protein not related to aquaporins. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA79093.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA82298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U39485; AAC49281.1; -; mRNA.
DR EMBL; U39486; AAC49992.1; -; Genomic_DNA.
DR EMBL; AB023046; BAB01264.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75789.1; -; Genomic_DNA.
DR EMBL; AY065181; AAL38357.1; -; mRNA.
DR EMBL; AY081622; AAM10184.1; -; mRNA.
DR EMBL; AK229954; BAF01780.1; -; mRNA.
DR EMBL; AY085921; AAM63133.1; -; mRNA.
DR EMBL; Z18064; CAA79093.1; ALT_INIT; mRNA.
DR EMBL; Z29043; CAA82298.1; ALT_INIT; mRNA.
DR EMBL; Z29044; CAA82299.1; -; mRNA.
DR RefSeq; NP_188245.1; NM_112495.4.
DR PDB; 5I32; X-ray; 1.18 A; A=2-250.
DR PDBsum; 5I32; -.
DR AlphaFoldDB; Q41951; -.
DR SMR; Q41951; -.
DR BioGRID; 6204; 6.
DR DIP; DIP-61927N; -.
DR IntAct; Q41951; 4.
DR STRING; 3702.AT3G16240.1; -.
DR TCDB; 1.A.8.10.10; the major intrinsic protein (mip) family.
DR iPTMnet; Q41951; -.
DR PaxDb; Q41951; -.
DR PRIDE; Q41951; -.
DR ProteomicsDB; 232426; -.
DR EnsemblPlants; AT3G16240.1; AT3G16240.1; AT3G16240.
DR GeneID; 820870; -.
DR Gramene; AT3G16240.1; AT3G16240.1; AT3G16240.
DR KEGG; ath:AT3G16240; -.
DR Araport; AT3G16240; -.
DR TAIR; locus:2094977; AT3G16240.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; Q41951; -.
DR OMA; IYPNVFM; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q41951; -.
DR PRO; PR:Q41951; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q41951; baseline and differential.
DR Genevisible; Q41951; AT.
DR GO; GO:0042807; C:central vacuole; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA: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:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0000326; C:protein storage vacuole; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015200; F:methylammonium transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA: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 TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..250
FT /note="Aquaporin TIP2-1"
FT /id="PRO_0000425759"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..250
FT /note="Aquaporin TIP2-1, N-terminally processed"
FT /id="PRO_0000064011"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..54
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..141
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..215
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 83..85
FT /note="NPA 1"
FT MOTIF 197..199
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 2
FT /note="N-acetylalanine; in Aquaporin TIP2-1, N-terminally
FT processed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 116
FT /note="C->S: Reduces the mercury-sensitivity."
FT /evidence="ECO:0000269|PubMed:8624437"
FT CONFLICT 40
FT /note="I -> Y (in Ref. 6; CAA79093)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="W -> L (in Ref. 6; CAA79093)"
FT /evidence="ECO:0000305"
FT CONFLICT 124..126
FT /note="GGL -> KTQ (in Ref. 8; CAA82298)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="G -> E (in Ref. 4; AAL38357/AAM10184)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 15..46
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 53..74
FT /evidence="ECO:0007829|PDB:5I32"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 98..122
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 139..160
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 169..188
FT /evidence="ECO:0007829|PDB:5I32"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:5I32"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:5I32"
FT HELIX 216..235
FT /evidence="ECO:0007829|PDB:5I32"
SQ SEQUENCE 250 AA; 25027 MW; 4CBEF20B22CC40D9 CRC64;
MAGVAFGSFD DSFSLASLRA YLAEFISTLL FVFAGVGSAI AYAKLTSDAA LDTPGLVAIA
VCHGFALFVA VAIGANISGG HVNPAVTFGL AVGGQITVIT GVFYWIAQLL GSTAACFLLK
YVTGGLAVPT HSVAAGLGSI EGVVMEIIIT FALVYTVYAT AADPKKGSLG TIAPLAIGLI
VGANILAAGP FSGGSMNPAR SFGPAVAAGD FSGHWVYWVG PLIGGGLAGL IYGNVFMGSS
EHVPLASADF
