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Protein

Aquaporin PIP1-1

Gene

PIP1-1

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. Its function is impaired by Hg2+.1 Publication

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 water deprivation Source: TAIR
  • water transport Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_284409. Erythrocytes take up oxygen and release carbon dioxide.
REACT_286112. Erythrocytes take up carbon dioxide and release oxygen.
REACT_314388. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_343424. Passive transport by Aquaporins.

Protein family/group databases

TCDBi1.A.8.11.3. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin PIP1-1
Short name:
AtPIP1;1
Alternative name(s):
Plasma membrane aquaporin-1
Plasma membrane intrinsic protein 1a
Short name:
PIP1a
Gene namesi
Name:PIP1-1
Synonyms:PIP1A
Ordered Locus Names:At3g61430
ORF Names:F2A19.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G61430.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5454CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei55 – 7521Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini76 – 9116ExtracellularSequence AnalysisAdd
BLAST
Transmembranei92 – 11221Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini113 – 13220CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei133 – 15321Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini154 – 17421ExtracellularSequence AnalysisAdd
BLAST
Transmembranei175 – 19521Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini196 – 20813CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei209 – 22921Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini230 – 25627ExtracellularSequence AnalysisAdd
BLAST
Transmembranei257 – 27721Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini278 – 2869CytoplasmicSequence Analysis

GO - Cellular componenti

  • chloroplast envelope Source: TAIR
  • integral component of plasma membrane Source: GO_Central
  • membrane Source: TAIR
  • mitochondrion 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 – 286286Aquaporin PIP1-1PRO_0000064045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei284 – 2841PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP61837.
PRIDEiP61837.

Expressioni

Tissue specificityi

Widely expressed. Expressed in roots, above ground and in flower buds.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi10630. 6 interactions.
IntActiP61837. 5 interactions.
STRINGi3702.AT3G61430.1.

Structurei

3D structure databases

ProteinModelPortaliP61837.
SMRiP61837. Positions 34-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi114 – 1163NPA 1
Motifi235 – 2373NPA 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

eggNOGiCOG0580.
HOGENOMiHOG000288286.
InParanoidiP61837.
KOiK09872.
OMAiNLGANKY.
PhylomeDBiP61837.

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.

P61837-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGKEEDVRV GANKFPERQP IGTSAQSDKD YKEPPPAPFF EPGELSSWSF
60 70 80 90 100
WRAGIAEFIA TFLFLYITVL TVMGVKRSPN MCASVGIQGI AWAFGGMIFA
110 120 130 140 150
LVYCTAGISG GHINPAVTFG LFLARKLSLT RALYYIVMQC LGAICGAGVV
160 170 180 190 200
KGFQPKQYQA LGGGANTVAH GYTKGSGLGA EIIGTFVLVY TVFSATDAKR
210 220 230 240 250
NARDSHVPIL APLPIGFAVF LVHLATIPIT GTGINPARSL GAAIIYNKDH
260 270 280
SWDDHWVFWV GPFIGAALAA LYHVVVIRAI PFKSRS
Length:286
Mass (Da):30,689
Last modified:June 7, 2004 - v1
Checksum:i5C0284F6BB5EA7B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151F → L in AAM65975 (Ref. 5) Curated
Sequence conflicti231 – 2311G → A in CAA53475 (PubMed:7920711).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75881 mRNA. Translation: CAA53475.1.
AL132962 Genomic DNA. Translation: CAB71073.1.
CP002686 Genomic DNA. Translation: AEE80201.1.
CP002686 Genomic DNA. Translation: AEE80202.1.
AY097398 mRNA. Translation: AAM19914.1.
AY058113 mRNA. Translation: AAL25530.1.
AK229222 mRNA. Translation: BAF01089.1.
AY088439 mRNA. Translation: AAM65975.1.
PIRiT47935.
RefSeqiNP_001078323.1. NM_001084854.1.
NP_191702.1. NM_116008.3.
UniGeneiAt.23835.

Genome annotation databases

EnsemblPlantsiAT3G61430.1; AT3G61430.1; AT3G61430.
AT3G61430.2; AT3G61430.2; AT3G61430.
GeneIDi825316.
KEGGiath:AT3G61430.

Cross-referencesi

Web resourcesi

Protein Spotlight

Liquid states - Issue 36 of July 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75881 mRNA. Translation: CAA53475.1.
AL132962 Genomic DNA. Translation: CAB71073.1.
CP002686 Genomic DNA. Translation: AEE80201.1.
CP002686 Genomic DNA. Translation: AEE80202.1.
AY097398 mRNA. Translation: AAM19914.1.
AY058113 mRNA. Translation: AAL25530.1.
AK229222 mRNA. Translation: BAF01089.1.
AY088439 mRNA. Translation: AAM65975.1.
PIRiT47935.
RefSeqiNP_001078323.1. NM_001084854.1.
NP_191702.1. NM_116008.3.
UniGeneiAt.23835.

3D structure databases

ProteinModelPortaliP61837.
SMRiP61837. Positions 34-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10630. 6 interactions.
IntActiP61837. 5 interactions.
STRINGi3702.AT3G61430.1.

Protein family/group databases

TCDBi1.A.8.11.3. the major intrinsic protein (mip) family.

Proteomic databases

PaxDbiP61837.
PRIDEiP61837.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G61430.1; AT3G61430.1; AT3G61430.
AT3G61430.2; AT3G61430.2; AT3G61430.
GeneIDi825316.
KEGGiath:AT3G61430.

Organism-specific databases

GeneFarmi4862. 182.
TAIRiAT3G61430.

Phylogenomic databases

eggNOGiCOG0580.
HOGENOMiHOG000288286.
InParanoidiP61837.
KOiK09872.
OMAiNLGANKY.
PhylomeDBiP61837.

Enzyme and pathway databases

ReactomeiREACT_284409. Erythrocytes take up oxygen and release carbon dioxide.
REACT_286112. Erythrocytes take up carbon dioxide and release oxygen.
REACT_314388. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_343424. Passive transport by Aquaporins.

Miscellaneous databases

PROiP61837.

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. "Water channels in the plant plasma membrane cloned by immunoselection from a mammalian expression system."
    Kammerloher W., Fischer U., Piechottka G.P., Schaeffner A.R.
    Plant J. 6:187-199(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.
    Tissue: Root.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    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.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    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. "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.
  8. Cited for: ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPIP11_ARATH
AccessioniPrimary (citable) accession number: P61837
Secondary accession number(s): P43285
, Q0WP60, Q8L9H0, Q9LDT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: June 24, 2015
This is version 105 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.