PIP22_ARATH
ID PIP22_ARATH Reviewed; 285 AA.
AC P43287; Q8L5U5; Q9SKR8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 170.
DE RecName: Full=Aquaporin PIP2-2;
DE AltName: Full=Plasma membrane intrinsic protein 2-2;
DE Short=AtPIP2;2;
DE AltName: Full=Plasma membrane intrinsic protein 2b;
DE Short=PIP2b;
DE AltName: Full=TMP2b;
GN Name=PIP2-2; Synonyms=PIP2B; OrderedLocusNames=At2g37170; ORFNames=T2N18.7;
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], AND FUNCTION.
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Root;
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 [6]
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 [7]
RP FUNCTION, AND MUTAGENESIS OF ARG-194; ASP-195; HIS-197 AND HIS-264.
RX PubMed=14508488; DOI=10.1038/nature01853;
RA Tournaire-Roux C., Sutka M., Javot H., Gout E., Gerbeau P., Luu D.-T.,
RA Bligny R., Maurel C.;
RT "Cytosolic pH regulates root water transport during anoxic stress through
RT gating of aquaporins.";
RL Nature 425:393-397(2003).
RN [8]
RP METHYLATION AT LYS-3, AND 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).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane. Plays an predominant role in root water uptake
CC process in conditions of reduced transpiration, and in osmotic fluid
CC transport. Its function is impaired by Hg(2+). Inhibited by cytosolic
CC acidosis which occurs during anoxia in roots.
CC {ECO:0000269|PubMed:12566588, ECO:0000269|PubMed:14508488,
CC ECO:0000269|PubMed:7920711}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12566588};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12566588}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the root, with a strong
CC expression in the cortex, endodermis, and stele.
CC {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:12566588}.
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 -!- 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; X75884; CAA53478.1; -; mRNA.
DR EMBL; AC006260; AAD18142.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09362.1; -; Genomic_DNA.
DR EMBL; AY086460; AAM63463.1; -; mRNA.
DR PIR; D84789; D84789.
DR PIR; S44085; S44085.
DR RefSeq; NP_181254.1; NM_129273.5.
DR AlphaFoldDB; P43287; -.
DR SMR; P43287; -.
DR BioGRID; 3637; 14.
DR IntAct; P43287; 7.
DR STRING; 3702.AT2G37170.1; -.
DR iPTMnet; P43287; -.
DR PaxDb; P43287; -.
DR PRIDE; P43287; -.
DR ProteomicsDB; 236738; -.
DR EnsemblPlants; AT2G37170.1; AT2G37170.1; AT2G37170.
DR GeneID; 818293; -.
DR Gramene; AT2G37170.1; AT2G37170.1; AT2G37170.
DR KEGG; ath:AT2G37170; -.
DR Araport; AT2G37170; -.
DR TAIR; locus:2061773; AT2G37170.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; P43287; -.
DR PhylomeDB; P43287; -.
DR PRO; PR:P43287; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P43287; baseline and differential.
DR Genevisible; P43287; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0015250; F:water channel activity; 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.
FT CHAIN 1..285
FT /note="Aquaporin PIP2-2"
FT /id="PRO_0000425767"
FT TOPO_DOM 2..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..107
FT /note="NPA 1"
FT MOTIF 226..228
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 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT MUTAGEN 194
FT /note="R->A: Reduced sensitivity to cytosolic
FT acidification. Insensitive to cytosolic acidification; when
FT associated with A-197."
FT /evidence="ECO:0000269|PubMed:14508488"
FT MUTAGEN 195
FT /note="D->A: Reduced sensitivity to cytosolic
FT acidification. Insensitive to cytosolic acidification; when
FT associated with A-197."
FT /evidence="ECO:0000269|PubMed:14508488"
FT MUTAGEN 197
FT /note="H->A: Reduced water transport activity. Reduced
FT sensitivity to cytosolic acidification. Insensitive to
FT cytosolic acidification; when associated with A-194 or A-
FT 195."
FT /evidence="ECO:0000269|PubMed:14508488"
FT MUTAGEN 197
FT /note="H->D: Reduced water transport activity. Insensitive
FT to cytosolic acidification."
FT /evidence="ECO:0000269|PubMed:14508488"
FT MUTAGEN 197
FT /note="H->K: Very low water transport activity. Insensitive
FT to cytosolic acidification."
FT /evidence="ECO:0000269|PubMed:14508488"
FT MUTAGEN 264
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:14508488"
FT CONFLICT 68
FT /note="A -> V (in Ref. 4; AAM63463)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..143
FT /note="VKA -> RQS (in Ref. 1; CAA53478)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="A -> S (in Ref. 1; CAA53478)"
FT /evidence="ECO:0000305"
SQ 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
