PIP21_ARATH
ID PIP21_ARATH Reviewed; 287 AA.
AC P43286;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 176.
DE RecName: Full=Aquaporin PIP2-1;
DE AltName: Full=Plasma membrane intrinsic protein 2-1;
DE Short=AtPIP2;1;
DE AltName: Full=Plasma membrane intrinsic protein 2a;
DE Short=PIP2a;
GN Name=PIP2-1; Synonyms=PIP2A; OrderedLocusNames=At3g53420;
GN ORFNames=F4P12.120;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Root;
RX PubMed=7920711; DOI=10.1046/j.1365-313x.1994.6020187.x;
RA Kammerloher W., Fischer U., Piechottka G.P., Schaeffner A.R.;
RT "Water channels in the plant plasma membrane cloned by immunoselection from
RT a mammalian expression system.";
RL Plant J. 6:187-199(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12566588; DOI=10.1105/tpc.008888;
RA Javot H., Lauvergeat V., Santoni V., Martin-Laurent F., Gueclue J.,
RA Vinh J., Heyes J., Franck K.I., Schaeffner A.R., Bouchez D., Maurel C.;
RT "Role of a single aquaporin isoform in root water uptake.";
RL Plant Cell 15:509-522(2003).
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 METHYLATION AT LYS-3, MUTAGENESIS OF LYS-3 AND GLU-6, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=16839310; DOI=10.1042/bj20060569;
RA Santoni V., Verdoucq L., Sommerer N., Vinh J., Pflieger D., Maurel C.;
RT "Methylation of aquaporins in plant plasma membrane.";
RL Biochem. J. 400:189-197(2006).
RN [11]
RP PHOSPHORYLATION AT SER-280 AND SER-283, SUBCELLULAR LOCATION, MUTAGENESIS
RP OF SER-280 AND SER-283, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=18234664; DOI=10.1074/mcp.m700566-mcp200;
RA Prak S., Hem S., Boudet J., Viennois G., Sommerer N., Rossignol M.,
RA Maurel C., Santoni V.;
RT "Multiple phosphorylations in the C-terminal tail of plant plasma membrane
RT aquaporins: role in subcellular trafficking of AtPIP2;1 in response to salt
RT stress.";
RL Mol. Cell. Proteomics 7:1019-1030(2008).
RN [12]
RP UBIQUITINATION BY RMA1.
RX PubMed=19234086; DOI=10.1105/tpc.108.061994;
RA Lee H.K., Cho S.K., Son O., Xu Z., Hwang I., Kim W.T.;
RT "Drought stress-induced Rma1H1, a RING membrane-anchor E3 ubiquitin ligase
RT homolog, regulates aquaporin levels via ubiquitination in transgenic
RT Arabidopsis plants.";
RL Plant Cell 21:622-641(2009).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane. Probably involved in root water uptake. Its
CC function is impaired by Hg(2+). {ECO:0000269|PubMed:7920711}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10737809,
CC ECO:0000269|PubMed:15060130, ECO:0000269|PubMed:18234664}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10737809,
CC ECO:0000269|PubMed:18234664}. Note=A fuzzy intracellular localization
CC is induced by salt (NaCl) treatment.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots and green
CC siliques. Also expressed at lower level above ground and in flower
CC buds. {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:7920711}.
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 -!- PTM: Ubiquitinated by RMA1, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:19234086}.
CC -!- PTM: The phosphorylation at Ser-280 and Ser-283 is altered by salt
CC (NaCl) and hydrogen peroxide H(2)O(2) treatments. Phosphorylation of
CC Ser-283 is required for plasma membrane targeting.
CC {ECO:0000269|PubMed:18234664}.
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; X75883; CAA53477.1; -; mRNA.
DR EMBL; AL132966; CAB67649.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79083.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79084.1; -; Genomic_DNA.
DR EMBL; AY039579; AAK62634.1; -; mRNA.
DR EMBL; AY044327; AAK73268.1; -; mRNA.
DR EMBL; AY056085; AAL06973.1; -; mRNA.
DR EMBL; AF428426; AAL16195.1; -; mRNA.
DR EMBL; AY072374; AAL62366.1; -; mRNA.
DR EMBL; AY087854; AAM65406.1; -; mRNA.
DR PIR; S44084; S44084.
DR RefSeq; NP_001030851.1; NM_001035774.1.
DR RefSeq; NP_190910.1; NM_115202.3.
DR AlphaFoldDB; P43286; -.
DR SMR; P43286; -.
DR BioGRID; 9827; 306.
DR IntAct; P43286; 4.
DR MINT; P43286; -.
DR STRING; 3702.AT3G53420.1; -.
DR TCDB; 1.A.8.11.4; the major intrinsic protein (mip) family.
DR iPTMnet; P43286; -.
DR PaxDb; P43286; -.
DR PRIDE; P43286; -.
DR ProteomicsDB; 234961; -.
DR EnsemblPlants; AT3G53420.1; AT3G53420.1; AT3G53420.
DR EnsemblPlants; AT3G53420.2; AT3G53420.2; AT3G53420.
DR GeneID; 824510; -.
DR Gramene; AT3G53420.1; AT3G53420.1; AT3G53420.
DR Gramene; AT3G53420.2; AT3G53420.2; AT3G53420.
DR KEGG; ath:AT3G53420; -.
DR Araport; AT3G53420; -.
DR TAIR; locus:2084031; AT3G53420.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; P43286; -.
DR OMA; FNNKKAW; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P43286; -.
DR PRO; PR:P43286; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P43286; baseline and differential.
DR Genevisible; P43286; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0006833; P:water transport; 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;
KW Ubl conjugation.
FT CHAIN 1..287
FT /note="Aquaporin PIP2-1"
FT /id="PRO_0000425766"
FT TOPO_DOM 2..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 107..109
FT /note="NPA 1"
FT MOTIF 228..230
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; partial"
FT /evidence="ECO:0000269|PubMed:16839310"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18234664"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18234664"
FT MUTAGEN 3
FT /note="K->A: 2-fold decrease in water transport activity."
FT /evidence="ECO:0000269|PubMed:16839310"
FT MUTAGEN 3
FT /note="K->R: No effect."
FT /evidence="ECO:0000269|PubMed:16839310"
FT MUTAGEN 6
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:16839310"
FT MUTAGEN 280
FT /note="S->A: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:18234664"
FT MUTAGEN 283
FT /note="S->A: Intracellular reticulation pattern, probably
FT corresponding to the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:18234664"
FT MUTAGEN 283
FT /note="S->D: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:18234664"
SQ 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
