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Protein

Aquaporin NIP1-2

Gene

NIP1-2

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

Functioni

Water channel probably required to promote glycerol permeability and water transport across cell membranes.1 Publication

GO - Molecular functioni

GO - Biological processi

  • arsenite transport Source: TAIR
  • glycerol transport Source: GOC
  • hydrogen peroxide transmembrane transport Source: TAIR
  • response to arsenic-containing substance Source: TAIR
  • water transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Transport

Protein family/group databases

TCDBi1.A.8.12.7. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin NIP1-2
Alternative name(s):
NOD26-like intrinsic protein 1-2
Short name:
AtNIP1;2
Nodulin-26-like major intrinsic protein 2
Short name:
NodLikeMip2
Short name:
Protein NLM2
Cleaved into the following chain:
Gene namesi
Name:NIP1-2
Synonyms:NLM2
Ordered Locus Names:At4g18910
ORF Names:F13C5.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G18910.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei54 – 7421Helical; Name=1Sequence analysisAdd
BLAST
Transmembranei82 – 10221Helical; Name=2Sequence analysisAdd
BLAST
Transmembranei133 – 15321Helical; Name=3Sequence analysisAdd
BLAST
Transmembranei177 – 19721Helical; Name=4Sequence analysisAdd
BLAST
Transmembranei201 – 22121Helical; Name=5Sequence analysisAdd
BLAST
Transmembranei248 – 26821Helical; Name=6Sequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Aquaporin NIP1-2PRO_0000064063Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 294293Aquaporin NIP1-2, N-terminally processedPRO_0000425775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ8LFP7.
PRIDEiQ8LFP7.

PTM databases

iPTMnetiQ8LFP7.

Expressioni

Tissue specificityi

Expressed in developing seeds.1 Publication

Gene expression databases

GenevisibleiQ8LFP7. AT.

Interactioni

Protein-protein interaction databases

BioGridi12919. 1 interaction.
MINTiMINT-8070165.
STRINGi3702.AT4G18910.1.

Structurei

3D structure databases

ProteinModelPortaliQ8LFP7.
SMRiQ8LFP7. Positions 47-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi111 – 1133NPA 1
Motifi230 – 2323NPA 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 316Poly-Gln

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiQ8LFP7.
KOiK09874.
OMAiQQKEAIH.
PhylomeDBiQ8LFP7.

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.

Q8LFP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEISGNGGD ARDGAVVVNL KEEDEQQQQQ QAIHKPLKKQ DSLLSISVPF
60 70 80 90 100
LQKLMAEVLG TYFLIFAGCA AVAVNTQHDK AVTLPGIAIV WGLTVMVLVY
110 120 130 140 150
SLGHISGAHF NPAVTIAFAS CGRFPLKQVP AYVISQVIGS TLAAATLRLL
160 170 180 190 200
FGLDQDVCSG KHDVFVGTLP SGSNLQSFVI EFIITFYLMF VISGVATDNR
210 220 230 240 250
AIGELAGLAV GSTVLLNVII AGPVSGASMN PGRSLGPAMV YSCYRGLWIY
260 270 280 290
IVSPIVGAVS GAWVYNMVRY TDKPLREITK SGSFLKTVRN GSSR
Length:294
Mass (Da):31,269
Last modified:June 27, 2003 - v2
Checksum:iAF337613903285C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261Missing in AAM61294 (Ref. 5) Curated
Sequence conflicti85 – 851P → L in AAM61294 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250668 mRNA. Translation: CAC14597.1.
AL021711 Genomic DNA. Translation: CAA16748.1.
AL161549 Genomic DNA. Translation: CAB78893.1.
CP002687 Genomic DNA. Translation: AEE84106.1.
AY072380 mRNA. Translation: AAL62372.1.
BT000096 mRNA. Translation: AAN15415.1.
AY084720 mRNA. Translation: AAM61294.1.
PIRiT05028.
RefSeqiNP_193626.1. NM_118008.3.
UniGeneiAt.1953.

Genome annotation databases

EnsemblPlantsiAT4G18910.1; AT4G18910.1; AT4G18910.
GeneIDi827626.
GrameneiAT4G18910.1; AT4G18910.1; AT4G18910.
KEGGiath:AT4G18910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250668 mRNA. Translation: CAC14597.1.
AL021711 Genomic DNA. Translation: CAA16748.1.
AL161549 Genomic DNA. Translation: CAB78893.1.
CP002687 Genomic DNA. Translation: AEE84106.1.
AY072380 mRNA. Translation: AAL62372.1.
BT000096 mRNA. Translation: AAN15415.1.
AY084720 mRNA. Translation: AAM61294.1.
PIRiT05028.
RefSeqiNP_193626.1. NM_118008.3.
UniGeneiAt.1953.

3D structure databases

ProteinModelPortaliQ8LFP7.
SMRiQ8LFP7. Positions 47-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12919. 1 interaction.
MINTiMINT-8070165.
STRINGi3702.AT4G18910.1.

Protein family/group databases

TCDBi1.A.8.12.7. the major intrinsic protein (mip) family.

PTM databases

iPTMnetiQ8LFP7.

Proteomic databases

PaxDbiQ8LFP7.
PRIDEiQ8LFP7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G18910.1; AT4G18910.1; AT4G18910.
GeneIDi827626.
GrameneiAT4G18910.1; AT4G18910.1; AT4G18910.
KEGGiath:AT4G18910.

Organism-specific databases

TAIRiAT4G18910.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiQ8LFP7.
KOiK09874.
OMAiQQKEAIH.
PhylomeDBiQ8LFP7.

Miscellaneous databases

PROiQ8LFP7.

Gene expression databases

GenevisibleiQ8LFP7. 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. "Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae."
    Weig A.R., Jakob C.U.
    FEBS Lett. 481:293-298(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: cv. Columbia.
  2. "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.
  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. "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].
  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.

Entry informationi

Entry nameiNIP12_ARATH
AccessioniPrimary (citable) accession number: Q8LFP7
Secondary accession number(s): O49406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 27, 2003
Last modified: February 17, 2016
This is version 118 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.