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Protein

Probable aquaporin PIP1-4

Gene

PIP1.4

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

Functioni

Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.By similarity

GO - Molecular functioni

GO - Biological processi

  • 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

ReactomeiR-ATH-432047. Passive transport by Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable aquaporin PIP1-4
Alternative name(s):
Plasma membrane intrinsic protein 1-4
Short name:
AtPIP1;4
Transmembrane protein C
Short name:
TMP-C
Gene namesi
Name:PIP1.4
Synonyms:TMPC
Ordered Locus Names:At4g00430
ORF Names:A_IG005I10.2, F5I10.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G00430.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555CytoplasmicSequence analysisAdd
BLAST
Transmembranei56 – 7621Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini77 – 9216ExtracellularSequence analysisAdd
BLAST
Transmembranei93 – 11321Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini114 – 13320CytoplasmicSequence analysisAdd
BLAST
Transmembranei134 – 15421Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini155 – 17521ExtracellularSequence analysisAdd
BLAST
Transmembranei176 – 19621Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini197 – 20913CytoplasmicSequence analysisAdd
BLAST
Transmembranei210 – 23021Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini231 – 25727ExtracellularSequence analysisAdd
BLAST
Transmembranei258 – 27821Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini279 – 2879CytoplasmicSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: GO_Central
  • vacuole Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 287287Probable aquaporin PIP1-4PRO_0000064049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei285 – 2851PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ39196.
PRIDEiQ39196.

PTM databases

SwissPalmiQ39196.

Expressioni

Tissue specificityi

Predominantly expressed in roots and green siliques. Also expressed above ground and in flower buds.1 Publication

Gene expression databases

ExpressionAtlasiQ39196. baseline and differential.
GenevisibleiQ39196. AT.

Interactioni

Protein-protein interaction databases

BioGridi13247. 12 interactions.
IntActiQ39196. 5 interactions.
STRINGi3702.AT4G00430.1.

Structurei

3D structure databases

ProteinModelPortaliQ39196.
SMRiQ39196. Positions 44-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi115 – 1173NPA 1
Motifi236 – 2383NPA 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.
InParanoidiQ39196.
KOiK09872.
OMAiVKVGANK.
PhylomeDBiQ39196.

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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q39196-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGKEEDVRV GANKFPERQP IGTSAQSTDK DYKEPPPAPL FEPGELSSWS
60 70 80 90 100
FYRAGIAEFI ATFLFLYITV LTVMGVKRAP NMCASVGIQG IAWAFGGMIF
110 120 130 140 150
ALVYCTAGIS GGHINPAVTF GLFLARKLSL TRAVFYMIMQ CLGAICGAGV
160 170 180 190 200
VKGFQPTPYQ TLGGGANTVA HGYTKGSGLG AEIIGTFVLV YTVFSATDAK
210 220 230 240 250
RSARDSHVPI LAPLPIGFAV FLVHLATIPI TGTGINPARS LGAAIIYNKD
260 270 280
HSWDDHWIFW VGPFIGAALA ALYHQIVIRA IPFKSKS
Length:287
Mass (Da):30,693
Last modified:November 1, 1996 - v1
Checksum:i8CE76043F389B3B8
GO

Sequence cautioni

The sequence AAB62824.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAF02782.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB80801.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → V in BAA22097 (PubMed:8980528).Curated
Sequence conflicti39 – 391P → S in BAA22097 (PubMed:8980528).Curated
Sequence conflicti169 – 1691V → G in BAA22097 (PubMed:8980528).Curated
Sequence conflicti199 – 1991A → D in BAA22097 (PubMed:8980528).Curated
Sequence conflicti203 – 2031A → V in BAA22097 (PubMed:8980528).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26609 mRNA. Translation: BAA05654.1.
D85192 mRNA. Translation: BAA22097.1.
AF013293 Genomic DNA. Translation: AAB62824.1. Sequence problems.
AF195115 Genomic DNA. Translation: AAF02782.1. Sequence problems.
AL161471 Genomic DNA. Translation: CAB80801.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE81879.1.
AY099825 mRNA. Translation: AAM20676.1.
AY120785 mRNA. Translation: AAM53343.1.
BT000330 mRNA. Translation: AAN15649.1.
BT006313 mRNA. Translation: AAP13421.1.
PIRiT01528.
RefSeqiNP_567178.1. NM_116268.3. [Q39196-1]
UniGeneiAt.20518.
At.20892.

Genome annotation databases

EnsemblPlantsiAT4G00430.1; AT4G00430.1; AT4G00430. [Q39196-1]
GeneIDi827956.
KEGGiath:AT4G00430.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26609 mRNA. Translation: BAA05654.1.
D85192 mRNA. Translation: BAA22097.1.
AF013293 Genomic DNA. Translation: AAB62824.1. Sequence problems.
AF195115 Genomic DNA. Translation: AAF02782.1. Sequence problems.
AL161471 Genomic DNA. Translation: CAB80801.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE81879.1.
AY099825 mRNA. Translation: AAM20676.1.
AY120785 mRNA. Translation: AAM53343.1.
BT000330 mRNA. Translation: AAN15649.1.
BT006313 mRNA. Translation: AAP13421.1.
PIRiT01528.
RefSeqiNP_567178.1. NM_116268.3. [Q39196-1]
UniGeneiAt.20518.
At.20892.

3D structure databases

ProteinModelPortaliQ39196.
SMRiQ39196. Positions 44-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13247. 12 interactions.
IntActiQ39196. 5 interactions.
STRINGi3702.AT4G00430.1.

PTM databases

SwissPalmiQ39196.

Proteomic databases

PaxDbiQ39196.
PRIDEiQ39196.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G00430.1; AT4G00430.1; AT4G00430. [Q39196-1]
GeneIDi827956.
KEGGiath:AT4G00430.

Organism-specific databases

TAIRiAT4G00430.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiQ39196.
KOiK09872.
OMAiVKVGANK.
PhylomeDBiQ39196.

Enzyme and pathway databases

ReactomeiR-ATH-432047. Passive transport by Aquaporins.

Miscellaneous databases

PROiQ39196.

Gene expression databases

ExpressionAtlasiQ39196. baseline and differential.
GenevisibleiQ39196. 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. "Nucleotide sequence of a transmembrane protein (TMP-C) cDNA in Arabidopsis thaliana."
    Kinoshita T., Hara-Nishimura I., Shiraishi H., Okada K., Shimura Y., Nishimura M.
    Plant Physiol. 105:1441-1442(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Flower bud.
  2. "Isolation and characterization of cDNA clones corresponding to the genes expressed preferentially in floral organs of Arabidopsis thaliana."
    Utsugi S., Sakamoto W., Ogura Y., Murata M., Motoyoshi F.
    Plant Mol. Biol. 32:759-765(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Flower bud.
  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. "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.
  7. Cited for: ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPIP14_ARATH
AccessioniPrimary (citable) accession number: Q39196
Secondary accession number(s): O23059, O23829
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: November 1, 1996
Last modified: February 17, 2016
This is version 128 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.