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Aquaporin PIP2-2 (Plasma membrane intrinsic protein 2-2) (AtPIP2;2) (Plasma membrane intrinsic protein 2b) (PIP2b) (TMP2b) [Cleaved into: Aquaporin PIP2-2, N-terminally processed]

 PIP22_ARATH             Reviewed;         285 AA.
P43287; Q8L5U5; Q9SKR8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
22-NOV-2017, entry version 146.
RecName: Full=Aquaporin PIP2-2;
AltName: Full=Plasma membrane intrinsic protein 2-2;
Short=AtPIP2;2;
AltName: Full=Plasma membrane intrinsic protein 2b;
Short=PIP2b;
AltName: Full=TMP2b;
Contains:
RecName: Full=Aquaporin PIP2-2, N-terminally processed;
Name=PIP2-2; Synonyms=PIP2B; OrderedLocusNames=At2g37170;
ORFNames=T2N18.7;
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. 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=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
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.
[5]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Root;
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).
[6]
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).
[7]
FUNCTION, AND MUTAGENESIS OF ARG-194; ASP-195; HIS-197 AND HIS-264.
PubMed=14508488; DOI=10.1038/nature01853;
Tournaire-Roux C., Sutka M., Javot H., Gout E., Gerbeau P., Luu D.-T.,
Bligny R., Maurel C.;
"Cytosolic pH regulates root water transport during anoxic stress
through gating of aquaporins.";
Nature 425:393-397(2003).
[8]
METHYLATION AT LYS-3, 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).
-!- FUNCTION: Water channel required to facilitate the transport of
water across cell membrane. Plays an predominant role in root
water uptake process in conditions of reduced transpiration, and
in osmotic fluid transport. Its function is impaired by Hg(2+).
Inhibited by cytosolic acidosis which occurs during anoxia in
roots. {ECO:0000269|PubMed:12566588, ECO:0000269|PubMed:14508488,
ECO:0000269|PubMed:7920711}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12566588};
Multi-pass membrane protein {ECO:0000269|PubMed:12566588}.
-!- TISSUE SPECIFICITY: Predominantly expressed in the root, with a
strong expression in the cortex, endodermis, and stele.
{ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:12566588}.
-!- 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; X75884; CAA53478.1; -; mRNA.
EMBL; AC006260; AAD18142.1; -; Genomic_DNA.
EMBL; CP002685; AEC09362.1; -; Genomic_DNA.
EMBL; AY086460; AAM63463.1; -; mRNA.
PIR; D84789; D84789.
PIR; S44085; S44085.
RefSeq; NP_181254.1; NM_129273.5.
UniGene; At.24327; -.
ProteinModelPortal; P43287; -.
SMR; P43287; -.
BioGrid; 3637; 10.
IntAct; P43287; 1.
STRING; 3702.AT2G37170.1; -.
iPTMnet; P43287; -.
PaxDb; P43287; -.
PRIDE; P43287; -.
EnsemblPlants; AT2G37170.1; AT2G37170.1; AT2G37170.
EnsemblPlants; AT2G37170.2; AT2G37170.2; AT2G37170.
GeneID; 818293; -.
Gramene; AT2G37170.1; AT2G37170.1; AT2G37170.
Gramene; AT2G37170.2; AT2G37170.2; AT2G37170.
KEGG; ath:AT2G37170; -.
Araport; AT2G37170; -.
TAIR; locus:2061773; AT2G37170.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; P43287; -.
KO; K09872; -.
OMA; IMSMSAN; -.
OrthoDB; EOG09360H78; -.
PhylomeDB; P43287; -.
PRO; PR:P43287; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; P43287; baseline and differential.
Genevisible; P43287; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0015250; F:water channel activity; 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.
CHAIN 1 285 Aquaporin PIP2-2.
/FTId=PRO_0000425767.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:Q41951}.
CHAIN 2 285 Aquaporin PIP2-2, N-terminally processed.
/FTId=PRO_0000064052.
TOPO_DOM 2 37 Cytoplasmic. {ECO:0000255}.
TRANSMEM 38 58 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 59 74 Extracellular. {ECO:0000255}.
TRANSMEM 75 95 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 96 123 Cytoplasmic. {ECO:0000255}.
TRANSMEM 124 144 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 145 165 Extracellular. {ECO:0000255}.
TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 187 199 Cytoplasmic. {ECO:0000255}.
TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 221 247 Extracellular. {ECO:0000255}.
TRANSMEM 248 268 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 269 285 Cytoplasmic. {ECO:0000255}.
MOTIF 105 107 NPA 1.
MOTIF 226 228 NPA 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P61837}.
MOD_RES 2 2 N-acetylalanine; in Aquaporin PIP2-2, N-
terminally processed.
{ECO:0000250|UniProtKB:Q41951}.
MOD_RES 3 3 N6,N6-dimethyllysine; partial.
{ECO:0000269|PubMed:16839310}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000250|UniProtKB:P43286}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000250|UniProtKB:P43286}.
MUTAGEN 194 194 R->A: Reduced sensitivity to cytosolic
acidification. Insensitive to cytosolic
acidification; when associated with A-
197. {ECO:0000269|PubMed:14508488}.
MUTAGEN 195 195 D->A: Reduced sensitivity to cytosolic
acidification. Insensitive to cytosolic
acidification; when associated with A-
197. {ECO:0000269|PubMed:14508488}.
MUTAGEN 197 197 H->A: Reduced water transport activity.
Reduced sensitivity to cytosolic
acidification. Insensitive to cytosolic
acidification; when associated with A-194
or A-195. {ECO:0000269|PubMed:14508488}.
MUTAGEN 197 197 H->D: Reduced water transport activity.
Insensitive to cytosolic acidification.
{ECO:0000269|PubMed:14508488}.
MUTAGEN 197 197 H->K: Very low water transport activity.
Insensitive to cytosolic acidification.
{ECO:0000269|PubMed:14508488}.
MUTAGEN 264 264 H->A: No effect.
{ECO:0000269|PubMed:14508488}.
CONFLICT 68 68 A -> V (in Ref. 4; AAM63463).
{ECO:0000305}.
CONFLICT 141 143 VKA -> RQS (in Ref. 1; CAA53478).
{ECO:0000305}.
CONFLICT 234 234 A -> S (in Ref. 1; CAA53478).
{ECO:0000305}.
SEQUENCE 285 AA; 30453 MW; 04364AFE7531EE10 CRC64;
MAKDVEGPEG FQTRDYEDPP PTPFFDADEL TKWSLYRAVI AEFVATLLFL YITVLTVIGY
KIQSDTKAGG VDCGGVGILG IAWAFGGMIF ILVYCTAGIS GGHINPAVTF GLFLARKVSL
IRAVLYMVAQ CLGAICGVGF VKAFQSSYYD RYGGGANSLA DGYNTGTGLA AEIIGTFVLV
YTVFSATDPK RNARDSHVPV LAPLPIGFAV FMVHLATIPI TGTGINPARS FGAAVIYNKS
KPWDDHWIFW VGPFIGAAIA AFYHQFVLRA SGSKSLGSFR SAANV


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