PIP23_ARATH
ID PIP23_ARATH Reviewed; 285 AA.
AC P30302; Q8L5V1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Aquaporin PIP2-3;
DE AltName: Full=Plasma membrane intrinsic protein 2-3;
DE Short=AtPIP2;3;
DE AltName: Full=Plasma membrane intrinsic protein 2c;
DE Short=PIP2c;
DE AltName: Full=RD28-PIP;
DE AltName: Full=TMP2C;
DE AltName: Full=Water stress-induced tonoplast intrinsic protein;
DE Short=WSI-TIP;
GN Name=PIP2-3; Synonyms=PIP2C, RD28; OrderedLocusNames=At2g37180;
GN ORFNames=T2N18.6;
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 INDUCTION.
RC STRAIN=cv. Columbia;
RA Yamaguchi-Shinozaki K., Koizumi M., Urao S., Shinozaki K.;
RT "Molecular cloning and characterization of 9 cDNAs for genes that are
RT responsive to desiccation in Arabidopsis thaliana: sequence analysis of one
RT cDNA clone that encodes a putative transmembrane channel protein.";
RL Plant Cell Physiol. 33:217-224(1992).
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].
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP THR-223.
RC STRAIN=cv. Columbia;
RX PubMed=7846153; DOI=10.1104/pp.106.4.1325;
RA Daniels M.J., Mirkov T.E., Chrispeels M.J.;
RT "The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive
RT aquaporin that is a homolog of the tonoplast water channel protein TIP.";
RL Plant Physiol. 106:1325-1333(1994).
RN [7]
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).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane; mercury-insensitive.
CC {ECO:0000269|PubMed:7846153}.
CC -!- INTERACTION:
CC P30302; Q08733: PIP1-3; NbExp=2; IntAct=EBI-4431139, EBI-4431134;
CC P30302; Q8LAA6: PIP1-5; NbExp=3; IntAct=EBI-4431139, EBI-4440607;
CC P30302; Q9ZVX8: PIP2-8; NbExp=4; IntAct=EBI-4431139, EBI-4425116;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7846153};
CC Multi-pass membrane protein {ECO:0000269|PubMed:7846153}.
CC -!- TISSUE SPECIFICITY: Widely expressed, except in seeds.
CC {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:7846153}.
CC -!- INDUCTION: By dehydration (Ref.1). Not affected by water stress
CC (PubMed:7846153). {ECO:0000269|PubMed:7846153, ECO:0000269|Ref.1}.
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; D13254; BAA02520.1; -; mRNA.
DR EMBL; AC006260; AAD18141.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09363.1; -; Genomic_DNA.
DR EMBL; AY064029; AAL36385.1; -; mRNA.
DR EMBL; AY096701; AAM20335.1; -; mRNA.
DR EMBL; AY084875; AAM61438.1; -; mRNA.
DR PIR; E84789; E84789.
DR RefSeq; NP_181255.1; NM_129274.4.
DR AlphaFoldDB; P30302; -.
DR SMR; P30302; -.
DR BioGRID; 3638; 17.
DR IntAct; P30302; 12.
DR STRING; 3702.AT2G37180.1; -.
DR TCDB; 1.A.8.11.9; the major intrinsic protein (mip) family.
DR iPTMnet; P30302; -.
DR PaxDb; P30302; -.
DR PRIDE; P30302; -.
DR ProteomicsDB; 234757; -.
DR EnsemblPlants; AT2G37180.1; AT2G37180.1; AT2G37180.
DR GeneID; 818294; -.
DR Gramene; AT2G37180.1; AT2G37180.1; AT2G37180.
DR KEGG; ath:AT2G37180; -.
DR Araport; AT2G37180; -.
DR TAIR; locus:2061763; AT2G37180.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; P30302; -.
DR OMA; IVYGVKP; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P30302; -.
DR PRO; PR:P30302; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P30302; baseline and differential.
DR Genevisible; P30302; 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; HDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP: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; Phosphoprotein; Reference proteome;
KW Repeat; Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..285
FT /note="Aquaporin PIP2-3"
FT /id="PRO_0000425768"
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..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..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..21
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 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 223
FT /note="T->C: Creates some mercury-sensitivity."
FT /evidence="ECO:0000269|PubMed:7846153"
FT CONFLICT 8
FT /note="P -> S (in Ref. 5; AAM61438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 30429 MW; D51213A68EEBB508 CRC64;
MAKDVEGPDG FQTRDYEDPP PTPFFDAEEL TKWSLYRAVI AEFVATLLFL YVTVLTVIGY
KIQSDTKAGG VDCGGVGILG IAWAFGGMIF ILVYCTAGIS GGHINPAVTF GLFLARKVSL
IRAVLYMVAQ CLGAICGVGF VKAFQSSHYV NYGGGANFLA DGYNTGTGLA AEIIGTFVLV
YTVFSATDPK RNARDSHVPV LAPLPIGFAV FMVHLATIPI TGTGINPARS FGAAVIFNKS
KPWDDHWIFW VGPFIGATIA AFYHQFVLRA SGSKSLGSFR SAANV
