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Aquaporin PIP2-1 (Plasma membrane intrinsic protein 2-1) (AtPIP2;1) (Plasma membrane intrinsic protein 2a) (PIP2a) [Cleaved into: Aquaporin PIP2-1, N-terminally processed]

 PIP21_ARATH             Reviewed;         287 AA.
P43286;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
18-JUL-2018, entry version 159.
RecName: Full=Aquaporin PIP2-1;
AltName: Full=Plasma membrane intrinsic protein 2-1;
Short=AtPIP2;1;
AltName: Full=Plasma membrane intrinsic protein 2a;
Short=PIP2a;
Name=PIP2-1; Synonyms=PIP2A; OrderedLocusNames=At3g53420;
ORFNames=F4P12.120;
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], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta; TISSUE=Root;
PubMed=7920711; DOI=10.1046/j.1365-313X.1994.6020187.x;
Kammerloher W., Fischer U., Piechottka G.P., Schaeffner A.R.;
"Water channels in the plant plasma membrane cloned by immunoselection
from a mammalian expression system.";
Plant J. 6:187-199(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
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).
[4]
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).
[5]
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.
[6]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12566588; DOI=10.1105/tpc.008888;
Javot H., Lauvergeat V., Santoni V., Martin-Laurent F., Gueclue J.,
Vinh J., Heyes J., Franck K.I., Schaeffner A.R., Bouchez D.,
Maurel C.;
"Role of a single aquaporin isoform in root water uptake.";
Plant Cell 15:509-522(2003).
[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]
METHYLATION AT LYS-3, MUTAGENESIS OF LYS-3 AND GLU-6, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16839310; DOI=10.1042/BJ20060569;
Santoni V., Verdoucq L., Sommerer N., Vinh J., Pflieger D., Maurel C.;
"Methylation of aquaporins in plant plasma membrane.";
Biochem. J. 400:189-197(2006).
[11]
PHOSPHORYLATION AT SER-280 AND SER-283, SUBCELLULAR LOCATION,
MUTAGENESIS OF SER-280 AND SER-283, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=cv. Columbia;
PubMed=18234664; DOI=10.1074/mcp.M700566-MCP200;
Prak S., Hem S., Boudet J., Viennois G., Sommerer N., Rossignol M.,
Maurel C., Santoni V.;
"Multiple phosphorylations in the C-terminal tail of plant plasma
membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in
response to salt stress.";
Mol. Cell. Proteomics 7:1019-1030(2008).
[12]
UBIQUITINATION BY RMA1.
PubMed=19234086; DOI=10.1105/tpc.108.061994;
Lee H.K., Cho S.K., Son O., Xu Z., Hwang I., Kim W.T.;
"Drought stress-induced Rma1H1, a RING membrane-anchor E3 ubiquitin
ligase homolog, regulates aquaporin levels via ubiquitination in
transgenic Arabidopsis plants.";
Plant Cell 21:622-641(2009).
-!- FUNCTION: Water channel required to facilitate the transport of
water across cell membrane. Probably involved in root water
uptake. Its function is impaired by Hg(2+).
{ECO:0000269|PubMed:7920711}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10737809,
ECO:0000269|PubMed:15060130, ECO:0000269|PubMed:18234664}; Multi-
pass membrane protein {ECO:0000269|PubMed:10737809,
ECO:0000269|PubMed:18234664}. Note=A fuzzy intracellular
localization is induced by salt (NaCl) treatment.
-!- TISSUE SPECIFICITY: Predominantly expressed in roots and green
siliques. Also expressed at lower level above ground and in flower
buds. {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:7920711}.
-!- 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).
-!- PTM: Ubiquitinated by RMA1, leading to proteasomal degradation.
{ECO:0000269|PubMed:19234086}.
-!- PTM: The phosphorylation at Ser-280 and Ser-283 is altered by salt
(NaCl) and hydrogen peroxide H(2)O(2) treatments. Phosphorylation
of Ser-283 is required for plasma membrane targeting.
{ECO:0000269|PubMed:18234664}.
-!- 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; X75883; CAA53477.1; -; mRNA.
EMBL; AL132966; CAB67649.1; -; Genomic_DNA.
EMBL; CP002686; AEE79083.1; -; Genomic_DNA.
EMBL; CP002686; AEE79084.1; -; Genomic_DNA.
EMBL; AY039579; AAK62634.1; -; mRNA.
EMBL; AY044327; AAK73268.1; -; mRNA.
EMBL; AY056085; AAL06973.1; -; mRNA.
EMBL; AF428426; AAL16195.1; -; mRNA.
EMBL; AY072374; AAL62366.1; -; mRNA.
EMBL; AY087854; AAM65406.1; -; mRNA.
PIR; S44084; S44084.
RefSeq; NP_001030851.1; NM_001035774.1.
RefSeq; NP_190910.1; NM_115202.3.
UniGene; At.47609; -.
ProteinModelPortal; P43286; -.
SMR; P43286; -.
BioGrid; 9827; 12.
IntAct; P43286; 4.
MINT; P43286; -.
STRING; 3702.AT3G53420.1; -.
TCDB; 1.A.8.11.4; the major intrinsic protein (mip) family.
iPTMnet; P43286; -.
PaxDb; P43286; -.
PRIDE; P43286; -.
EnsemblPlants; AT3G53420.1; AT3G53420.1; AT3G53420.
EnsemblPlants; AT3G53420.2; AT3G53420.2; AT3G53420.
GeneID; 824510; -.
Gramene; AT3G53420.1; AT3G53420.1; AT3G53420.
Gramene; AT3G53420.2; AT3G53420.2; AT3G53420.
KEGG; ath:AT3G53420; -.
Araport; AT3G53420; -.
TAIR; locus:2084031; AT3G53420.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; P43286; -.
KO; K09872; -.
OMA; VANHWDF; -.
OrthoDB; EOG09360H78; -.
PhylomeDB; P43286; -.
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:P43286; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P43286; baseline and differential.
Genevisible; P43286; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; 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:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0015250; F:water channel activity; IDA:TAIR.
GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
GO; GO:0006833; P:water transport; IDA:TAIR.
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; Ubl conjugation.
CHAIN 1 287 Aquaporin PIP2-1.
/FTId=PRO_0000425766.
TOPO_DOM 2 39 Cytoplasmic. {ECO:0000255}.
TRANSMEM 40 60 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 61 83 Extracellular. {ECO:0000255}.
TRANSMEM 84 104 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 105 125 Cytoplasmic. {ECO:0000255}.
TRANSMEM 126 146 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 147 167 Extracellular. {ECO:0000255}.
TRANSMEM 168 188 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 189 201 Cytoplasmic. {ECO:0000255}.
TRANSMEM 202 222 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 223 249 Extracellular. {ECO:0000255}.
TRANSMEM 250 270 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 271 287 Cytoplasmic. {ECO:0000255}.
MOTIF 107 109 NPA 1.
MOTIF 228 230 NPA 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P61837}.
MOD_RES 3 3 N6,N6-dimethyllysine; partial.
{ECO:0000269|PubMed:16839310}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000269|PubMed:18234664}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000269|PubMed:18234664}.
MUTAGEN 3 3 K->A: 2-fold decrease in water transport
activity. {ECO:0000269|PubMed:16839310}.
MUTAGEN 3 3 K->R: No effect.
{ECO:0000269|PubMed:16839310}.
MUTAGEN 6 6 E->A: No effect.
{ECO:0000269|PubMed:16839310}.
MUTAGEN 280 280 S->A: Normal subcellular localization.
{ECO:0000269|PubMed:18234664}.
MUTAGEN 283 283 S->A: Intracellular reticulation pattern,
probably corresponding to the endoplasmic
reticulum. {ECO:0000269|PubMed:18234664}.
MUTAGEN 283 283 S->D: Normal subcellular localization.
{ECO:0000269|PubMed:18234664}.
SEQUENCE 287 AA; 30474 MW; D73D618324B9A903 CRC64;
MAKDVEAVPG EGFQTRDYQD PPPAPFIDGA ELKKWSFYRA VIAEFVATLL FLYITVLTVI
GYKIQSDTDA GGVDCGGVGI LGIAWAFGGM IFILVYCTAG ISGGHINPAV TFGLFLARKV
SLPRALLYII AQCLGAICGV GFVKAFQSSY YTRYGGGANS LADGYSTGTG LAAEIIGTFV
LVYTVFSATD PKRSARDSHV PVLAPLPIGF AVFMVHLATI PITGTGINPA RSFGAAVIYN
KSKPWDDHWI FWVGPFIGAA IAAFYHQFVL RASGSKSLGS FRSAANV


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Catalog number Product name Quantity
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