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Aquaporin TIP2-1 (Delta-tonoplast intrinsic protein) (Delta-TIP) (Tonoplast intrinsic protein 2-1) (AtTIP2;1) [Cleaved into: Aquaporin TIP2-1, N-terminally processed]

 TIP21_ARATH             Reviewed;         250 AA.
Q41951; Q0WM76; Q42200; Q42201; Q43352; Q8VZ81;
27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
27-JUN-2003, sequence version 2.
25-OCT-2017, entry version 154.
RecName: Full=Aquaporin TIP2-1;
AltName: Full=Delta-tonoplast intrinsic protein;
Short=Delta-TIP;
AltName: Full=Tonoplast intrinsic protein 2-1;
Short=AtTIP2;1;
Contains:
RecName: Full=Aquaporin TIP2-1, N-terminally processed;
Name=TIP2-1; OrderedLocusNames=At3g16240; ORFNames=MYA6.10;
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-116.
STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10819329; DOI=10.1093/dnares/7.2.131;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
features of the regions of 4,504,864 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:131-135(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-106.
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-250.
STRAIN=cv. Columbia; TISSUE=Shoot;
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).
[9]
SUBCELLULAR LOCATION.
PubMed=10737809; DOI=10.1073/pnas.97.7.3718;
Cutler S.R., Ehrhardt D.W., Griffitts J.S., Somerville C.R.;
"Random GFP::cDNA fusions enable visualization of subcellular
structures in cells of Arabidopsis at a high frequency.";
Proc. Natl. Acad. Sci. U.S.A. 97:3718-3723(2000).
[10]
NOMENCLATURE, AND TISSUE SPECIFICITY.
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).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
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).
[12]
FUNCTION, AND INDUCTION.
PubMed=15665250; DOI=10.1104/pp.104.051268;
Loque D., Ludewig U., Yuan L., von Wiren N.;
"Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3
transport into the vacuole.";
Plant Physiol. 137:671-680(2005).
[13]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=17151019; DOI=10.1074/mcp.M600250-MCP200;
Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V.,
Bruley C., Garin J., Bourguignon J.;
"A proteomics dissection of Arabidopsis thaliana vacuoles isolated
from cell culture.";
Mol. Cell. Proteomics 6:394-412(2007).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Aquaporin required to facilitate the transport of water
from the vacuolar compartment to the cytoplasm. Does not promote
glycerol permability. Its function is impaired by Hg(2+).
Transports urea in yeast cells and Xenopus laevis oocytes in a pH-
independent manner. Transports methylammonium or ammonium in yeast
cells and Xenopus laevis oocytes, preferentially at high medium
pH. May participate in vacuolar compartmentation and
detoxification of ammonium. {ECO:0000269|PubMed:14576283,
ECO:0000269|PubMed:15665250, ECO:0000269|PubMed:8624437}.
-!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
{ECO:0000269|PubMed:17030879}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-4442669, EBI-4442669;
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:10737809, ECO:0000269|PubMed:14576283,
ECO:0000269|PubMed:17151019, ECO:0000269|PubMed:8624437}; Multi-
pass membrane protein {ECO:0000255, ECO:0000269|PubMed:10737809,
ECO:0000269|PubMed:14576283, ECO:0000269|PubMed:8624437}.
Note=Tonoplast. It is specifically located in the tonoplast of
protein storage vacuoles (PSV) (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Strongly expressed in shoot, rosette, bolt and
flowers. Also expressed in roots, flower buds and above ground.
{ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:8624437}.
-!- DEVELOPMENTAL STAGE: Starts to be expressed in seedlings from 2
days ays after germination. {ECO:0000269|PubMed:14576283}.
-!- INDUCTION: By ammonium nitrate in roots. Expressed in roots with a
circadian rhythm showing an increase after onset of light, a peak
approximately at midday and a decline to lowest levels before
offset of light. {ECO:0000269|PubMed:15665250}.
-!- 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).
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP
(TC 1.A.8.10) subfamily. {ECO:0000305}.
-!- CAUTION: Was originally assigned as At3g16230, which is now a
completely different protein not related to aquaporins.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA79093.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA82298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U39485; AAC49281.1; -; mRNA.
EMBL; U39486; AAC49992.1; -; Genomic_DNA.
EMBL; AB023046; BAB01264.1; -; Genomic_DNA.
EMBL; CP002686; AEE75789.1; -; Genomic_DNA.
EMBL; AY065181; AAL38357.1; -; mRNA.
EMBL; AY081622; AAM10184.1; -; mRNA.
EMBL; AK229954; BAF01780.1; -; mRNA.
EMBL; AY085921; AAM63133.1; -; mRNA.
EMBL; Z18064; CAA79093.1; ALT_INIT; mRNA.
EMBL; Z29043; CAA82298.1; ALT_INIT; mRNA.
EMBL; Z29044; CAA82299.1; -; mRNA.
RefSeq; NP_188245.1; NM_112495.4.
UniGene; At.23571; -.
UniGene; At.32719; -.
UniGene; At.6081; -.
UniGene; At.71329; -.
PDB; 5I32; X-ray; 1.18 A; A=2-250.
PDBsum; 5I32; -.
ProteinModelPortal; Q41951; -.
SMR; Q41951; -.
BioGrid; 6204; 6.
DIP; DIP-61927N; -.
IntAct; Q41951; 4.
STRING; 3702.AT3G16240.1; -.
TCDB; 1.A.8.10.10; the major intrinsic protein (mip) family.
iPTMnet; Q41951; -.
PaxDb; Q41951; -.
PRIDE; Q41951; -.
EnsemblPlants; AT3G16240.1; AT3G16240.1; AT3G16240.
GeneID; 820870; -.
Gramene; AT3G16240.1; AT3G16240.1; AT3G16240.
KEGG; ath:AT3G16240; -.
Araport; AT3G16240; -.
TAIR; locus:2094977; AT3G16240.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; Q41951; -.
KO; K09873; -.
OMA; IRNPVAN; -.
OrthoDB; EOG09360J95; -.
PhylomeDB; Q41951; -.
Reactome; R-ATH-432047; Passive transport by Aquaporins.
PRO; PR:Q41951; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q41951; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0042807; C:central vacuole; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; 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:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0015200; F:methylammonium transmembrane transporter activity; IDA:TAIR.
GO; GO:0015250; F:water channel activity; IDA: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.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Membrane;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Vacuole.
CHAIN 1 250 Aquaporin TIP2-1.
/FTId=PRO_0000425759.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:22223895}.
CHAIN 2 250 Aquaporin TIP2-1, N-terminally processed.
/FTId=PRO_0000064011.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 42 54 Vacuolar. {ECO:0000255}.
TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 76 98 Cytoplasmic. {ECO:0000255}.
TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 120 141 Vacuolar. {ECO:0000255}.
TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 163 168 Cytoplasmic. {ECO:0000255}.
TRANSMEM 169 189 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 190 215 Vacuolar. {ECO:0000255}.
TRANSMEM 216 236 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 237 250 Cytoplasmic. {ECO:0000255}.
MOTIF 83 85 NPA 1.
MOTIF 197 199 NPA 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P61837}.
MOD_RES 2 2 N-acetylalanine; in Aquaporin TIP2-1, N-
terminally processed.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 116 116 C->S: Reduces the mercury-sensitivity.
{ECO:0000269|PubMed:8624437}.
CONFLICT 40 40 I -> Y (in Ref. 6; CAA79093).
{ECO:0000305}.
CONFLICT 105 105 W -> L (in Ref. 6; CAA79093).
{ECO:0000305}.
CONFLICT 124 126 GGL -> KTQ (in Ref. 8; CAA82298).
{ECO:0000305}.
CONFLICT 226 226 G -> E (in Ref. 4; AAL38357/AAM10184).
{ECO:0000305}.
HELIX 9 12 {ECO:0000244|PDB:5I32}.
HELIX 15 46 {ECO:0000244|PDB:5I32}.
HELIX 53 74 {ECO:0000244|PDB:5I32}.
TURN 75 78 {ECO:0000244|PDB:5I32}.
HELIX 84 92 {ECO:0000244|PDB:5I32}.
HELIX 98 122 {ECO:0000244|PDB:5I32}.
HELIX 139 160 {ECO:0000244|PDB:5I32}.
HELIX 169 188 {ECO:0000244|PDB:5I32}.
TURN 189 192 {ECO:0000244|PDB:5I32}.
HELIX 198 208 {ECO:0000244|PDB:5I32}.
TURN 212 215 {ECO:0000244|PDB:5I32}.
HELIX 216 235 {ECO:0000244|PDB:5I32}.
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


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