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Protein

Aquaporin TIP2-1

Gene

TIP2-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Hg2+. 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.3 Publications

GO - Molecular functioni

  • glycerol channel activity Source: GO_Central
  • methylammonium transmembrane transporter activity Source: TAIR
  • water channel activity Source: TAIR

GO - Biological processi

  • cellular water homeostasis Source: GO_Central
  • water transport Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-ATH-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-ATH-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-ATH-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-ATH-432047. Passive transport by Aquaporins.

Protein family/group databases

TCDBi1.A.8.10.10. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin TIP2-1
Alternative name(s):
Delta-tonoplast intrinsic protein
Short name:
Delta-TIP
Tonoplast intrinsic protein 2-1
Short name:
AtTIP2;1
Cleaved into the following chain:
Gene namesi
Name:TIP2-1
Ordered Locus Names:At3g16240
ORF Names:MYA6.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G16240.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 20CytoplasmicSequence analysisAdd BLAST20
Transmembranei21 – 41Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini42 – 54VacuolarSequence analysisAdd BLAST13
Transmembranei55 – 75Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini76 – 98CytoplasmicSequence analysisAdd BLAST23
Transmembranei99 – 119Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini120 – 141VacuolarSequence analysisAdd BLAST22
Transmembranei142 – 162Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini163 – 168CytoplasmicSequence analysis6
Transmembranei169 – 189Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini190 – 215VacuolarSequence analysisAdd BLAST26
Transmembranei216 – 236Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini237 – 250CytoplasmicSequence analysisAdd BLAST14

GO - Cellular componenti

  • cell wall Source: TAIR
  • central vacuole Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • Golgi apparatus Source: TAIR
  • integral component of plasma membrane Source: GO_Central
  • plant-type cell wall Source: TAIR
  • plant-type vacuole membrane Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • protein storage vacuole Source: TAIR
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi116C → S: Reduces the mercury-sensitivity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004257591 – 250Aquaporin TIP2-1Add BLAST250
Initiator methionineiRemoved; alternateCombined sources
ChainiPRO_00000640112 – 250Aquaporin TIP2-1, N-terminally processedAdd BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylalanine; in Aquaporin TIP2-1, N-terminally processedCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ41951.
PRIDEiQ41951.

Expressioni

Tissue specificityi

Strongly expressed in shoot, rosette, bolt and flowers. Also expressed in roots, flower buds and above ground.2 Publications

Developmental stagei

Starts to be expressed in seedlings from 2 days ays after germination.1 Publication

Inductioni

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.1 Publication

Gene expression databases

GenevisibleiQ41951. AT.

Interactioni

Subunit structurei

Interacts with cucumber mosaic virus (CMV) Protein 1a.1 Publication

Protein-protein interaction databases

BioGridi6204. 6 interactors.
DIPiDIP-61927N.
IntActiQ41951. 4 interactors.
STRINGi3702.AT3G16240.1.

Structurei

Secondary structure

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 12Combined sources4
Helixi15 – 46Combined sources32
Helixi53 – 74Combined sources22
Turni75 – 78Combined sources4
Helixi84 – 92Combined sources9
Helixi98 – 122Combined sources25
Helixi139 – 160Combined sources22
Helixi169 – 188Combined sources20
Turni189 – 192Combined sources4
Helixi198 – 208Combined sources11
Turni212 – 215Combined sources4
Helixi216 – 235Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5I32X-ray1.18A2-250[»]
ProteinModelPortaliQ41951.
SMRiQ41951.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi83 – 85NPA 13
Motifi197 – 199NPA 23

Domaini

Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiQ41951.
KOiK09873.
OMAiFMGSSEH.
OrthoDBiEOG09360J95.
PhylomeDBiQ41951.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q41951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVAFGSFD DSFSLASLRA YLAEFISTLL FVFAGVGSAI AYAKLTSDAA
60 70 80 90 100
LDTPGLVAIA VCHGFALFVA VAIGANISGG HVNPAVTFGL AVGGQITVIT
110 120 130 140 150
GVFYWIAQLL GSTAACFLLK YVTGGLAVPT HSVAAGLGSI EGVVMEIIIT
160 170 180 190 200
FALVYTVYAT AADPKKGSLG TIAPLAIGLI VGANILAAGP FSGGSMNPAR
210 220 230 240 250
SFGPAVAAGD FSGHWVYWVG PLIGGGLAGL IYGNVFMGSS EHVPLASADF
Length:250
Mass (Da):25,027
Last modified:June 27, 2003 - v2
Checksum:i4CBEF20B22CC40D9
GO

Sequence cautioni

The sequence CAA79093 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA82298 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40I → Y in CAA79093 (Ref. 6) Curated1
Sequence conflicti105W → L in CAA79093 (Ref. 6) Curated1
Sequence conflicti124 – 126GGL → KTQ in CAA82298 (PubMed:8580968).Curated3
Sequence conflicti226G → E in AAL38357 (PubMed:14593172).Curated1
Sequence conflicti226G → E in AAM10184 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39485 mRNA. Translation: AAC49281.1.
U39486 Genomic DNA. Translation: AAC49992.1.
AB023046 Genomic DNA. Translation: BAB01264.1.
CP002686 Genomic DNA. Translation: AEE75789.1.
AY065181 mRNA. Translation: AAL38357.1.
AY081622 mRNA. Translation: AAM10184.1.
AK229954 mRNA. Translation: BAF01780.1.
AY085921 mRNA. Translation: AAM63133.1.
Z18064 mRNA. Translation: CAA79093.1. Different initiation.
Z29043 mRNA. Translation: CAA82298.1. Different initiation.
Z29044 mRNA. Translation: CAA82299.1.
RefSeqiNP_188245.1. NM_112495.4.
UniGeneiAt.23571.
At.32719.
At.6081.
At.71329.

Genome annotation databases

EnsemblPlantsiAT3G16240.1; AT3G16240.1; AT3G16240.
GeneIDi820870.
GrameneiAT3G16240.1; AT3G16240.1; AT3G16240.
KEGGiath:AT3G16240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39485 mRNA. Translation: AAC49281.1.
U39486 Genomic DNA. Translation: AAC49992.1.
AB023046 Genomic DNA. Translation: BAB01264.1.
CP002686 Genomic DNA. Translation: AEE75789.1.
AY065181 mRNA. Translation: AAL38357.1.
AY081622 mRNA. Translation: AAM10184.1.
AK229954 mRNA. Translation: BAF01780.1.
AY085921 mRNA. Translation: AAM63133.1.
Z18064 mRNA. Translation: CAA79093.1. Different initiation.
Z29043 mRNA. Translation: CAA82298.1. Different initiation.
Z29044 mRNA. Translation: CAA82299.1.
RefSeqiNP_188245.1. NM_112495.4.
UniGeneiAt.23571.
At.32719.
At.6081.
At.71329.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5I32X-ray1.18A2-250[»]
ProteinModelPortaliQ41951.
SMRiQ41951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi6204. 6 interactors.
DIPiDIP-61927N.
IntActiQ41951. 4 interactors.
STRINGi3702.AT3G16240.1.

Protein family/group databases

TCDBi1.A.8.10.10. the major intrinsic protein (mip) family.

Proteomic databases

PaxDbiQ41951.
PRIDEiQ41951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G16240.1; AT3G16240.1; AT3G16240.
GeneIDi820870.
GrameneiAT3G16240.1; AT3G16240.1; AT3G16240.
KEGGiath:AT3G16240.

Organism-specific databases

TAIRiAT3G16240.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiQ41951.
KOiK09873.
OMAiFMGSSEH.
OrthoDBiEOG09360J95.
PhylomeDBiQ41951.

Enzyme and pathway databases

ReactomeiR-ATH-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-ATH-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-ATH-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-ATH-432047. Passive transport by Aquaporins.

Miscellaneous databases

PROiQ41951.

Gene expression databases

GenevisibleiQ41951. AT.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTIP21_ARATH
AccessioniPrimary (citable) accession number: Q41951
Secondary accession number(s): Q0WM76
, Q42200, Q42201, Q43352, Q8VZ81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 27, 2003
Last modified: November 30, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Was originally assigned as At3g16230, which is now a completely different protein not related to aquaporins.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.