Entry sw: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   18-JAN-2017, entry version 148.
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;
DE   Contains:
DE     RecName: Full=Aquaporin PIP2-1, N-terminally processed;
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   from 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.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   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
RT   structures in 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;
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   METHYLATION AT LYS-3, MUTAGENESIS OF LYS-3 AND GLU-6, AND
RP   IDENTIFICATION BY 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   [10]
RP   PHOSPHORYLATION AT SER-280 AND SER-283, SUBCELLULAR LOCATION,
RP   MUTAGENESIS OF SER-280 AND SER-283, AND IDENTIFICATION BY MASS
RP   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
RT   membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in
RT   response to salt stress.";
RL   Mol. Cell. Proteomics 7:1019-1030(2008).
RN   [11]
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
RT   ligase homolog, regulates aquaporin levels via ubiquitination in
RT   transgenic Arabidopsis plants.";
RL   Plant Cell 21:622-641(2009).
CC   -!- FUNCTION: Water channel required to facilitate the transport of
CC       water across cell membrane. Probably involved in root water
CC       uptake. Its function is impaired by Hg(2+).
CC       {ECO:0000269|PubMed:7920711}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10737809,
CC       ECO:0000269|PubMed:18234664}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:10737809, ECO:0000269|PubMed:18234664}. Note=A
CC       fuzzy intracellular localization is induced by salt (NaCl)
CC       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
CC       three membrane-spanning domains and a pore-forming loop with the
CC       signature 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
CC       of 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
CC       (TC 1.A.8.11) subfamily. {ECO:0000305}.
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   UniGene; At.47609; -.
DR   ProteinModelPortal; P43286; -.
DR   SMR; P43286; -.
DR   BioGrid; 9827; 12.
DR   MINT; MINT-6951259; -.
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   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   TAIR; AT3G53420; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   eggNOG; COG0580; LUCA.
DR   HOGENOM; HOG000288286; -.
DR   InParanoid; P43286; -.
DR   KO; K09872; -.
DR   OMA; NDSCAGV; -.
DR   OrthoDB; EOG09360H78; -.
DR   PhylomeDB; P43286; -.
DR   Reactome; R-ATH-432047; Passive transport by Aquaporins.
DR   PRO; PR:P43286; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   Genevisible; P43286; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0015254; F:glycerol channel activity; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA: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:0009992; P:cellular water homeostasis; IBA:GO_Central.
DR   GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; 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; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; PTHR19139; 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; Complete proteome; Membrane; Methylation;
KW   Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN         1    287       Aquaporin PIP2-1.
FT                                /FTId=PRO_0000064051.
FT   INIT_MET      1      1       Removed; alternate.
FT                                {ECO:0000250|UniProtKB:Q41951}.
FT   CHAIN         2    287       Aquaporin PIP2-1, N-terminally processed.
FT                                /FTId=PRO_0000425766.
FT   TOPO_DOM      1     39       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     40     60       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     61     83       Extracellular. {ECO:0000255}.
FT   TRANSMEM     84    104       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    105    125       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    126    146       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    147    167       Extracellular. {ECO:0000255}.
FT   TRANSMEM    168    188       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    189    201       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    202    222       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    223    249       Extracellular. {ECO:0000255}.
FT   TRANSMEM    250    270       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    271    287       Cytoplasmic. {ECO:0000255}.
FT   MOTIF       107    109       NPA 1.
FT   MOTIF       228    230       NPA 2.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:P61837}.
FT   MOD_RES       2      2       N-acetylalanine; in Aquaporin PIP2-1, N-
FT                                terminally processed.
FT                                {ECO:0000250|UniProtKB:Q41951}.
FT   MOD_RES       3      3       N6,N6-dimethyllysine; partial.
FT                                {ECO:0000269|PubMed:16839310}.
FT   MOD_RES     280    280       Phosphoserine.
FT                                {ECO:0000269|PubMed:18234664}.
FT   MOD_RES     283    283       Phosphoserine.
FT                                {ECO:0000269|PubMed:18234664}.
FT   MUTAGEN       3      3       K->A: 2-fold decrease in water transport
FT                                activity. {ECO:0000269|PubMed:16839310}.
FT   MUTAGEN       3      3       K->R: No effect.
FT                                {ECO:0000269|PubMed:16839310}.
FT   MUTAGEN       6      6       E->A: No effect.
FT                                {ECO:0000269|PubMed:16839310}.
FT   MUTAGEN     280    280       S->A: Normal subcellular localization.
FT                                {ECO:0000269|PubMed:18234664}.
FT   MUTAGEN     283    283       S->A: Intracellular reticulation pattern,
FT                                probably corresponding to the endoplasmic
FT                                reticulum. {ECO:0000269|PubMed:18234664}.
FT   MUTAGEN     283    283       S->D: Normal subcellular localization.
FT                                {ECO:0000269|PubMed:18234664}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       105    113       ipat:MIP [T]
FT   MYHIT        31    266       ipfam:MIP [T]
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
//