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Protein

Aquaporin TIP1-3

Gene

TIP1-3

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

Functioni

Potential aquaporin, which may facilitate the transport of water and small neutral solutes across cell membranes.By similarity

GO - Molecular functioni

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

GO - Biological processi

  • glycerol transport Source: GOC
  • ion transmembrane transport Source: GO_Central
  • urea transmembrane transport Source: GOC
  • urea transport Source: TAIR
  • water transport Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Stress response, 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.8.10.6. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin TIP1-3
Alternative name(s):
Gamma-tonoplast intrinsic protein 3
Short name:
Gamma-TIP3
Tonoplast intrinsic protein 1-3
Short name:
AtTIP1;3
Cleaved into the following chain:
Gene namesi
Name:TIP1-3
Ordered Locus Names:At4g01470
ORF Names:F11O4.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G01470.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence analysisAdd
BLAST
Transmembranei23 – 4321Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini44 – 5512VacuolarSequence analysisAdd
BLAST
Transmembranei56 – 7621Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini77 – 11438CytoplasmicSequence analysisAdd
BLAST
Transmembranei115 – 13521Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini136 – 1438VacuolarSequence analysis
Transmembranei144 – 16421Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini165 – 1706CytoplasmicSequence analysis
Transmembranei171 – 19121Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini192 – 21928VacuolarSequence analysisAdd
BLAST
Transmembranei220 – 24021Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini241 – 25212CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Aquaporin TIP1-3PRO_0000064010Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 252251Aquaporin TIP1-3, N-terminally processedPRO_0000425758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO82598.
PRIDEiO82598.

Expressioni

Inductioni

By dehydration. Not affected by water stress.

Gene expression databases

GenevisibleiO82598. AT.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi13342. 1 interaction.
STRINGi3702.AT4G01470.1.

Structurei

3D structure databases

ProteinModelPortaliO82598.
SMRiO82598. Positions 21-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi85 – 873NPA 1
Motifi199 – 2013NPA 2

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.
InParanoidiO82598.
KOiK09873.
OMAiMAYGKLT.
PhylomeDBiO82598.

Family and domain databases

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.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O82598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPINRIAIGT PGEASRPDAI RAAFAEFFSM VIFVFAGQGS GMAYGKLTGD
60 70 80 90 100
GPATPAGLVA ASLSHAFALF VAVSVGANVS GGHVNPAVTF GAFIGGNITL
110 120 130 140 150
LRAILYWIAQ LLGAVVACLL LKVSTGGMET AAFSLSYGVT PWNAVVFEIV
160 170 180 190 200
MTFGLVYTVY ATAVDPKKGD IGIIAPLAIG LIVGANILVG GAFDGASMNP
210 220 230 240 250
AVSFGPAVVS WIWTNHWVYW VGPFIGAAIA AIVYDTIFIG SNGHEPLPSN

DF
Length:252
Mass (Da):25,914
Last modified:November 1, 1998 - v1
Checksum:iF2FCC1D9DA44A76A
GO

Sequence cautioni

The sequence ABK28617.1 differs from that shown. Reason: Erroneous termination at position 253. Translated as stop.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF096370 Genomic DNA. Translation: AAC62778.1.
AL161492 Genomic DNA. Translation: CAB77717.1.
CP002687 Genomic DNA. Translation: AEE82031.1.
DQ446793 mRNA. Translation: ABE66039.1.
DQ653172 mRNA. Translation: ABK28617.1. Sequence problems.
PIRiT01947.
RefSeqiNP_192056.1. NM_116377.1.
UniGeneiAt.65315.

Genome annotation databases

EnsemblPlantsiAT4G01470.1; AT4G01470.1; AT4G01470.
GeneIDi828051.
GrameneiAT4G01470.1; AT4G01470.1; AT4G01470.
KEGGiath:AT4G01470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF096370 Genomic DNA. Translation: AAC62778.1.
AL161492 Genomic DNA. Translation: CAB77717.1.
CP002687 Genomic DNA. Translation: AEE82031.1.
DQ446793 mRNA. Translation: ABE66039.1.
DQ653172 mRNA. Translation: ABK28617.1. Sequence problems.
PIRiT01947.
RefSeqiNP_192056.1. NM_116377.1.
UniGeneiAt.65315.

3D structure databases

ProteinModelPortaliO82598.
SMRiO82598. Positions 21-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13342. 1 interaction.
STRINGi3702.AT4G01470.1.

Protein family/group databases

TCDBi1.A.8.10.6. the major intrinsic protein (mip) family.

Proteomic databases

PaxDbiO82598.
PRIDEiO82598.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G01470.1; AT4G01470.1; AT4G01470.
GeneIDi828051.
GrameneiAT4G01470.1; AT4G01470.1; AT4G01470.
KEGGiath:AT4G01470.

Organism-specific databases

TAIRiAT4G01470.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiO82598.
KOiK09873.
OMAiMAYGKLT.
PhylomeDBiO82598.

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

PROiO82598.

Gene expression databases

GenevisibleiO82598. AT.

Family and domain databases

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.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
    Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
    Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "From genome to function: the Arabidopsis aquaporins."
    Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.
    Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  5. "Arabidopsis tonoplast proteins TIP1 and TIP2 interact with the cucumber mosaic virus 1a replication protein."
    Kim M.J., Kim H.R., Paek K.-H.
    J. Gen. Virol. 87:3425-3431(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CMV PROTEIN 1A.

Entry informationi

Entry nameiTIP13_ARATH
AccessioniPrimary (citable) accession number: O82598
Secondary accession number(s): A0MF47, Q1PEC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: November 1, 1998
Last modified: February 17, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.