PIP27_ARATH
ID PIP27_ARATH Reviewed; 280 AA.
AC P93004; O22332; O49616;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 174.
DE RecName: Full=Aquaporin PIP2-7 {ECO:0000303|PubMed:11806824};
DE AltName: Full=Plasma membrane intrinsic protein 2-7 {ECO:0000303|PubMed:11806824};
DE Short=AtPIP2;7 {ECO:0000303|PubMed:11806824};
DE AltName: Full=Plasma membrane intrinsic protein 3 {ECO:0000303|PubMed:9276952};
DE Short=At-PIP3 {ECO:0000303|PubMed:9276952};
DE AltName: Full=Salt stress-induced major intrinsic protein {ECO:0000303|PubMed:10102577};
GN Name=PIP2-7 {ECO:0000303|PubMed:11806824};
GN Synonyms=PIP3 {ECO:0000303|PubMed:9276952},
GN SIMIP {ECO:0000303|PubMed:10102577};
GN OrderedLocusNames=At4g35100 {ECO:0000312|Araport:AT4G35100};
GN ORFNames=M4E13.150 {ECO:0000312|EMBL:CAA17774.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9276952; DOI=10.1104/pp.114.4.1347;
RA Weig A.R., Deswarte C., Chrispeels M.J.;
RT "The major intrinsic protein family of Arabidopsis has 23 members that form
RT three distinct groups with functional aquaporins in each group.";
RL Plant Physiol. 114:1347-1357(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10102577;
RA Pih K.T., Kabilan V., Lim J.H., Kang S.G., Piao H.L., Jin J.B., Hwang I.;
RT "Characterization of two new channel protein genes in Arabidopsis.";
RL Mol. Cells 9:84-90(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10737809; DOI=10.1073/pnas.97.7.3718;
RA Cutler S.R., Ehrhardt D.W., Griffitts J.S., Somerville C.R.;
RT "Random GFP::cDNA fusions enable visualization of subcellular structures in
RT cells of Arabidopsis at a high frequency.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3718-3723(2000).
RN [8]
RP NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=11806824; DOI=10.1186/gb-2001-3-1-research0001;
RA Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
RT "From genome to function: the Arabidopsis aquaporins.";
RL Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-276, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-276 AND THR-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP INTERACTION WITH SYP61 AND SYP121, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=25082856; DOI=10.1105/tpc.114.127159;
RA Hachez C., Laloux T., Reinhardt H., Cavez D., Degand H., Grefen C.,
RA De Rycke R., Inze D., Blatt M.R., Russinova E., Chaumont F.;
RT "Arabidopsis SNAREs SYP61 and SYP121 coordinate the trafficking of plasma
RT membrane aquaporin PIP2;7 to modulate the cell membrane water
RT permeability.";
RL Plant Cell 26:3132-3147(2014).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane. May be involved in the osmoregulation in plants
CC under high osmotic stress such as under a high salt condition.
CC {ECO:0000269|PubMed:10102577, ECO:0000269|PubMed:9276952}.
CC -!- SUBUNIT: Interacts with SYP61 and SYP121 in trafficking vesicles and at
CC the plasma membrane. {ECO:0000269|PubMed:25082856}.
CC -!- INTERACTION:
CC P93004; Q8LAA6: PIP1-5; NbExp=3; IntAct=EBI-4434233, EBI-4440607;
CC P93004; Q39196: PIP1.4; NbExp=3; IntAct=EBI-4434233, EBI-4427223;
CC P93004; Q8VZ95: PVA11; NbExp=3; IntAct=EBI-4434233, EBI-2010972;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10737809,
CC ECO:0000269|PubMed:15060130, ECO:0000269|PubMed:25082856}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10737809}. Note=Trafficking from
CC the post-Golgi compartment to the plasma membrane is mediated by the
CC SNARE proteins SYP61 and SYP121. {ECO:0000269|PubMed:25082856}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers, expressed at low
CC levels in siliques, and at low level in leaves and roots
CC (PubMed:10102577, PubMed:11806824). Highly levels in elongating cells
CC in both roots and shoots (PubMed:25082856).
CC {ECO:0000269|PubMed:10102577, ECO:0000269|PubMed:11806824,
CC ECO:0000269|PubMed:25082856}.
CC -!- INDUCTION: By NaCl and abscisic acid (ABA) treatments.
CC {ECO:0000269|PubMed:10102577}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC
CC 1.A.8.11) subfamily. {ECO:0000305}.
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DR EMBL; U78297; AAB36949.1; -; mRNA.
DR EMBL; AF003728; AAB65787.1; -; mRNA.
DR EMBL; AL022023; CAA17774.1; -; Genomic_DNA.
DR EMBL; AL161586; CAB80227.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86464.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86465.1; -; Genomic_DNA.
DR EMBL; AF412110; AAL06563.1; -; mRNA.
DR EMBL; AY062803; AAL32881.1; -; mRNA.
DR EMBL; AY081580; AAM10142.1; -; mRNA.
DR EMBL; AY088485; AAM66021.1; -; mRNA.
DR PIR; T05780; T05780.
DR RefSeq; NP_001190920.1; NM_001203991.1.
DR RefSeq; NP_195236.1; NM_119676.4.
DR AlphaFoldDB; P93004; -.
DR SMR; P93004; -.
DR BioGRID; 14944; 49.
DR IntAct; P93004; 39.
DR STRING; 3702.AT4G35100.2; -.
DR iPTMnet; P93004; -.
DR SwissPalm; P93004; -.
DR PaxDb; P93004; -.
DR PRIDE; P93004; -.
DR ProteomicsDB; 234761; -.
DR EnsemblPlants; AT4G35100.1; AT4G35100.1; AT4G35100.
DR EnsemblPlants; AT4G35100.2; AT4G35100.2; AT4G35100.
DR GeneID; 829662; -.
DR Gramene; AT4G35100.1; AT4G35100.1; AT4G35100.
DR Gramene; AT4G35100.2; AT4G35100.2; AT4G35100.
DR KEGG; ath:AT4G35100; -.
DR Araport; AT4G35100; -.
DR TAIR; locus:2131601; AT4G35100.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; P93004; -.
DR OMA; WEERQEQ; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P93004; -.
DR PRO; PR:P93004; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P93004; baseline and differential.
DR Genevisible; P93004; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR45687; PTHR45687; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..280
FT /note="Aquaporin PIP2-7"
FT /id="PRO_0000064057"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..69
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 100..102
FT /note="NPA 1"
FT MOTIF 221..223
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 52
FT /note="Y -> I (in Ref. 1; AAB36949)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="G -> R (in Ref. 2; AAB65787)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="R -> G (in Ref. 1; AAB36949 and 2; AAB65787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 29743 MW; 844337FA87BB2400 CRC64;
MSKEVSEEGK THHGKDYVDP PPAPLLDMGE LKSWSFYRAL IAEFIATLLF LYVTVATVIG
HKKQTGPCDG VGLLGIAWAF GGMIFVLVYC TAGISGGHIN PAVTFGLFLA RKVSLVRALG
YMIAQCLGAI CGVGFVKAFM KTPYNTLGGG ANTVADGYSK GTALGAEIIG TFVLVYTVFS
ATDPKRSARD SHIPVLAPLP IGFAVFMVHL ATIPITGTGI NPARSFGAAV IYNNEKAWDD
QWIFWVGPFL GALAAAAYHQ YILRASAIKA LGSFRSNATN
