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Protein

Aquaporin PIP2-7

Gene

PIP2-7

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

Functioni

Water channel required to facilitate the transport of water across cell membrane. May be involved in the osmoregulation in plants under high osmotic stress such as under a high salt condition.2 Publications

GO - Molecular functioni

  • glycerol channel activity Source: GO_Central
  • water channel activity Source: TAIR

GO - Biological processi

  • cellular water homeostasis Source: GO_Central
  • glycerol transport Source: GOC
  • ion transmembrane transport Source: GO_Central
  • response to abscisic acid Source: TAIR
  • water transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-ATH-432047. Passive transport by Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin PIP2-7
Alternative name(s):
Plasma membrane intrinsic protein 2-7
Short name:
AtPIP2;7
Plasma membrane intrinsic protein 3
Salt stress-induced major intrinsic protein
Cleaved into the following chain:
Gene namesi
Name:PIP2-7
Synonyms:PIP3, SIMIP
Ordered Locus Names:At4g35100
ORF Names:M4E13.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G35100.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838CytoplasmicSequence analysisAdd
BLAST
Transmembranei39 – 5921Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini60 – 6910ExtracellularSequence analysis
Transmembranei70 – 9021Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini91 – 11828CytoplasmicSequence analysisAdd
BLAST
Transmembranei119 – 13921Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini140 – 16021ExtracellularSequence analysisAdd
BLAST
Transmembranei161 – 18121Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini182 – 19211CytoplasmicSequence analysisAdd
BLAST
Transmembranei193 – 21321Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini214 – 24229ExtracellularSequence analysisAdd
BLAST
Transmembranei243 – 26321Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini264 – 28017CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • anchored component of plasma membrane Source: TAIR
  • integral component of plasma membrane Source: GO_Central
  • membrane Source: TAIR
  • nucleus Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280Aquaporin PIP2-7PRO_0000064057Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 280279Aquaporin PIP2-7, N-terminally processedPRO_0000434356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31N6,N6-dimethyllysineBy similarity
Modified residuei273 – 2731PhosphoserineCombined sources
Modified residuei276 – 2761PhosphoserineCombined sources
Modified residuei279 – 2791PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP93004.
PRIDEiP93004.

PTM databases

iPTMnetiP93004.
SwissPalmiP93004.

Expressioni

Tissue specificityi

Highly expressed in flowers, expressed at low levels in siliques, and at low level in leaves and roots.2 Publications

Inductioni

By NaCl and abscisic acid (ABA) treatments.1 Publication

Gene expression databases

ExpressionAtlasiP93004. baseline and differential.
GenevisibleiP93004. AT.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PVA11Q8VZ953EBI-4434233,EBI-2010972

Protein-protein interaction databases

BioGridi14944. 45 interactions.
IntActiP93004. 15 interactions.
STRINGi3702.AT4G35100.1.

Structurei

3D structure databases

ProteinModelPortaliP93004.
SMRiP93004. Positions 26-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi100 – 1023NPA 1
Motifi221 – 2233NPA 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.
InParanoidiP93004.
KOiK09872.
OMAiEEGKTHH.
PhylomeDBiP93004.

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.
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.

P93004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKEVSEEGK THHGKDYVDP PPAPLLDMGE LKSWSFYRAL IAEFIATLLF
60 70 80 90 100
LYVTVATVIG HKKQTGPCDG VGLLGIAWAF GGMIFVLVYC TAGISGGHIN
110 120 130 140 150
PAVTFGLFLA RKVSLVRALG YMIAQCLGAI CGVGFVKAFM KTPYNTLGGG
160 170 180 190 200
ANTVADGYSK GTALGAEIIG TFVLVYTVFS ATDPKRSARD SHIPVLAPLP
210 220 230 240 250
IGFAVFMVHL ATIPITGTGI NPARSFGAAV IYNNEKAWDD QWIFWVGPFL
260 270 280
GALAAAAYHQ YILRASAIKA LGSFRSNATN
Length:280
Mass (Da):29,743
Last modified:June 27, 2003 - v2
Checksum:i844337FA87BB2400
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521Y → I in AAB36949 (PubMed:9276952).Curated
Sequence conflicti106 – 1061G → R in AAB65787 (PubMed:10102577).Curated
Sequence conflicti111 – 1111R → G in AAB36949 (PubMed:9276952).Curated
Sequence conflicti111 – 1111R → G in AAB65787 (PubMed:10102577).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78297 mRNA. Translation: AAB36949.1.
AF003728 mRNA. Translation: AAB65787.1.
AL022023 Genomic DNA. Translation: CAA17774.1.
AL161586 Genomic DNA. Translation: CAB80227.1.
CP002687 Genomic DNA. Translation: AEE86464.1.
CP002687 Genomic DNA. Translation: AEE86465.1.
AF412110 mRNA. Translation: AAL06563.1.
AY062803 mRNA. Translation: AAL32881.1.
AY081580 mRNA. Translation: AAM10142.1.
AY088485 mRNA. Translation: AAM66021.1.
PIRiT05780.
RefSeqiNP_001190920.1. NM_001203991.1.
NP_195236.1. NM_119676.3.
UniGeneiAt.20518.
At.23067.
At.24183.

Genome annotation databases

EnsemblPlantsiAT4G35100.1; AT4G35100.1; AT4G35100.
AT4G35100.2; AT4G35100.2; AT4G35100.
GeneIDi829662.
GrameneiAT4G35100.1; AT4G35100.1; AT4G35100.
AT4G35100.2; AT4G35100.2; AT4G35100.
KEGGiath:AT4G35100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78297 mRNA. Translation: AAB36949.1.
AF003728 mRNA. Translation: AAB65787.1.
AL022023 Genomic DNA. Translation: CAA17774.1.
AL161586 Genomic DNA. Translation: CAB80227.1.
CP002687 Genomic DNA. Translation: AEE86464.1.
CP002687 Genomic DNA. Translation: AEE86465.1.
AF412110 mRNA. Translation: AAL06563.1.
AY062803 mRNA. Translation: AAL32881.1.
AY081580 mRNA. Translation: AAM10142.1.
AY088485 mRNA. Translation: AAM66021.1.
PIRiT05780.
RefSeqiNP_001190920.1. NM_001203991.1.
NP_195236.1. NM_119676.3.
UniGeneiAt.20518.
At.23067.
At.24183.

3D structure databases

ProteinModelPortaliP93004.
SMRiP93004. Positions 26-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14944. 45 interactions.
IntActiP93004. 15 interactions.
STRINGi3702.AT4G35100.1.

PTM databases

iPTMnetiP93004.
SwissPalmiP93004.

Proteomic databases

PaxDbiP93004.
PRIDEiP93004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G35100.1; AT4G35100.1; AT4G35100.
AT4G35100.2; AT4G35100.2; AT4G35100.
GeneIDi829662.
GrameneiAT4G35100.1; AT4G35100.1; AT4G35100.
AT4G35100.2; AT4G35100.2; AT4G35100.
KEGGiath:AT4G35100.

Organism-specific databases

TAIRiAT4G35100.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiP93004.
KOiK09872.
OMAiEEGKTHH.
PhylomeDBiP93004.

Enzyme and pathway databases

ReactomeiR-ATH-432047. Passive transport by Aquaporins.

Miscellaneous databases

PROiP93004.

Gene expression databases

ExpressionAtlasiP93004. baseline and differential.
GenevisibleiP93004. 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.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group."
    Weig A.R., Deswarte C., Chrispeels M.J.
    Plant Physiol. 114:1347-1357(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: cv. Columbia.
  2. "Characterization of two new channel protein genes in Arabidopsis."
    Pih K.T., Kabilan V., Lim J.H., Kang S.G., Piao H.L., Jin J.B., Hwang I.
    Mol. Cells 9:84-90(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency."
    Cutler S.R., Ehrhardt D.W., Griffitts J.S., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 97:3718-3723(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "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, TISSUE SPECIFICITY.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-276, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  10. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-276 AND THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPIP27_ARATH
AccessioniPrimary (citable) accession number: P93004
Secondary accession number(s): O22332, O49616
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 27, 2003
Last modified: June 8, 2016
This is version 141 of the entry and version 2 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.