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Aquaporin PIP2-7 (Plasma membrane intrinsic protein 2-7) (AtPIP2;7) (Plasma membrane intrinsic protein 3) (Salt stress-induced major intrinsic protein)

 PIP27_ARATH             Reviewed;         280 AA.
P93004; O22332; O49616;
27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
27-JUN-2003, sequence version 2.
07-NOV-2018, entry version 157.
RecName: Full=Aquaporin PIP2-7;
AltName: Full=Plasma membrane intrinsic protein 2-7;
Short=AtPIP2;7;
AltName: Full=Plasma membrane intrinsic protein 3;
AltName: Full=Salt stress-induced major intrinsic protein;
Name=PIP2-7; Synonyms=PIP3, SIMIP; OrderedLocusNames=At4g35100;
ORFNames=M4E13.150;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=cv. Columbia;
PubMed=9276952; DOI=10.1104/pp.114.4.1347;
Weig A.R., Deswarte C., Chrispeels M.J.;
"The major intrinsic protein family of Arabidopsis has 23 members that
form three distinct groups with functional aquaporins in each group.";
Plant Physiol. 114:1347-1357(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=cv. Columbia;
PubMed=10102577;
Pih K.T., Kabilan V., Lim J.H., Kang S.G., Piao H.L., Jin J.B.,
Hwang I.;
"Characterization of two new channel protein genes in Arabidopsis.";
Mol. Cells 9:84-90(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
SUBCELLULAR LOCATION.
PubMed=10737809; DOI=10.1073/pnas.97.7.3718;
Cutler S.R., Ehrhardt D.W., Griffitts J.S., Somerville C.R.;
"Random GFP::cDNA fusions enable visualization of subcellular
structures in cells of Arabidopsis at a high frequency.";
Proc. Natl. Acad. Sci. U.S.A. 97:3718-3723(2000).
[8]
NOMENCLATURE, AND TISSUE SPECIFICITY.
PubMed=11806824;
Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
"From genome to function: the Arabidopsis aquaporins.";
Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=15060130; DOI=10.1074/mcp.M400001-MCP200;
Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
Garin J., Barbier-Brygoo H., Ephritikhine G.;
"Identification of new intrinsic proteins in Arabidopsis plasma
membrane proteome.";
Mol. Cell. Proteomics 3:675-691(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-276, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-276 AND
THR-279, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10102577,
ECO:0000269|PubMed:9276952}.
-!- INTERACTION:
Q8LAA6:PIP1-5; NbExp=3; IntAct=EBI-4434233, EBI-4440607;
Q39196:PIP1.4; NbExp=3; IntAct=EBI-4434233, EBI-4427223;
Q8VZ95:PVA11; NbExp=3; IntAct=EBI-4434233, EBI-2010972;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10737809,
ECO:0000269|PubMed:15060130}; Multi-pass membrane protein
{ECO:0000269|PubMed:10737809}.
-!- TISSUE SPECIFICITY: Highly expressed in flowers, expressed at low
levels in siliques, and at low level in leaves and roots.
{ECO:0000269|PubMed:10102577, ECO:0000269|PubMed:11806824}.
-!- INDUCTION: By NaCl and abscisic acid (ABA) treatments.
{ECO:0000269|PubMed:10102577}.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA).
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP
(TC 1.A.8.11) subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U78297; AAB36949.1; -; mRNA.
EMBL; AF003728; AAB65787.1; -; mRNA.
EMBL; AL022023; CAA17774.1; -; Genomic_DNA.
EMBL; AL161586; CAB80227.1; -; Genomic_DNA.
EMBL; CP002687; AEE86464.1; -; Genomic_DNA.
EMBL; CP002687; AEE86465.1; -; Genomic_DNA.
EMBL; AF412110; AAL06563.1; -; mRNA.
EMBL; AY062803; AAL32881.1; -; mRNA.
EMBL; AY081580; AAM10142.1; -; mRNA.
EMBL; AY088485; AAM66021.1; -; mRNA.
PIR; T05780; T05780.
RefSeq; NP_001190920.1; NM_001203991.1.
RefSeq; NP_195236.1; NM_119676.4.
UniGene; At.20518; -.
UniGene; At.23067; -.
UniGene; At.24183; -.
ProteinModelPortal; P93004; -.
SMR; P93004; -.
BioGrid; 14944; 45.
IntAct; P93004; 39.
STRING; 3702.AT4G35100.1; -.
iPTMnet; P93004; -.
SwissPalm; P93004; -.
PaxDb; P93004; -.
PRIDE; P93004; -.
EnsemblPlants; AT4G35100.1; AT4G35100.1; AT4G35100.
EnsemblPlants; AT4G35100.2; AT4G35100.2; AT4G35100.
GeneID; 829662; -.
Gramene; AT4G35100.1; AT4G35100.1; AT4G35100.
Gramene; AT4G35100.2; AT4G35100.2; AT4G35100.
KEGG; ath:AT4G35100; -.
Araport; AT4G35100; -.
TAIR; locus:2131601; AT4G35100.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; P93004; -.
KO; K09872; -.
OMA; TSNWICC; -.
OrthoDB; EOG09360H78; -.
PhylomeDB; P93004; -.
Reactome; R-ATH-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-ATH-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-ATH-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-ATH-432047; Passive transport by Aquaporins.
PRO; PR:P93004; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P93004; baseline and differential.
Genevisible; P93004; AT.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0015250; F:water channel activity; IDA:TAIR.
GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
GO; GO:0009414; P:response to water deprivation; IBA:GO_Central.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Membrane; Methylation;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 280 Aquaporin PIP2-7.
/FTId=PRO_0000064057.
TOPO_DOM 1 38 Cytoplasmic. {ECO:0000255}.
TRANSMEM 39 59 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 60 69 Extracellular. {ECO:0000255}.
TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 91 118 Cytoplasmic. {ECO:0000255}.
TRANSMEM 119 139 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 140 160 Extracellular. {ECO:0000255}.
TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 182 192 Cytoplasmic. {ECO:0000255}.
TRANSMEM 193 213 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 214 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 263 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 264 280 Cytoplasmic. {ECO:0000255}.
MOTIF 100 102 NPA 1.
MOTIF 221 223 NPA 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P61837}.
MOD_RES 3 3 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P43286}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 279 279 Phosphothreonine.
{ECO:0000244|PubMed:19376835}.
CONFLICT 52 52 Y -> I (in Ref. 1; AAB36949).
{ECO:0000305}.
CONFLICT 106 106 G -> R (in Ref. 2; AAB65787).
{ECO:0000305}.
CONFLICT 111 111 R -> G (in Ref. 1; AAB36949 and 2;
AAB65787). {ECO:0000305}.
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


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