PIP12_ARATH
ID PIP12_ARATH Reviewed; 286 AA.
AC Q06611; Q8L5V4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 173.
DE RecName: Full=Aquaporin PIP1-2;
DE Short=AtPIP1;2;
DE AltName: Full=Plasma membrane intrinsic protein 1b;
DE Short=PIP1b;
DE AltName: Full=Transmembrane protein A;
DE Short=AthH2;
DE Short=TMP-A;
GN Name=PIP1-2; Synonyms=PIP1B, TMPA; OrderedLocusNames=At2g45960;
GN ORFNames=F4I18.6;
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].
RC STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
RX PubMed=8310069; DOI=10.1104/pp.101.4.1397;
RA Shagan T., Bar-Zvi D.;
RT "Nucleotide sequence of an Arabidopsis thaliana turgor-responsive cDNA
RT clone encoding TMP-A, a transmembrane protein containing the major
RT intrinsic protein motif.";
RL Plant Physiol. 101:1397-1398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C24;
RX PubMed=8292783; DOI=10.1007/bf00042352;
RA Kaldenhoff R., Koelling A., Richter G.;
RT "A novel blue light- and abscisic acid-inducible gene of Arabidopsis
RT thaliana encoding an intrinsic membrane protein.";
RL Plant Mol. Biol. 23:1187-1198(1993).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-286.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [8]
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 [9]
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 [10]
RP FUNCTION.
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 [11]
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 [12]
RP ACETYLATION AT MET-1, 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. Essential for the water permeability of the
CC plasma membrane and for the morphology of the root system. Its function
CC is impaired by Hg(2+). Inhibited by cytosolic acidosis which occurs
CC during anoxia in roots. {ECO:0000269|PubMed:14508488}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10737809,
CC ECO:0000269|PubMed:15060130}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10737809}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q06611-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in roots and above
CC ground. {ECO:0000269|PubMed:11806824}.
CC -!- INDUCTION: By blue light and abscisic acid (ABA).
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; X68293; CAA48356.1; -; mRNA.
DR EMBL; Z17424; CAB37860.1; -; mRNA.
DR EMBL; AC004665; AAC28529.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10622.1; -; Genomic_DNA.
DR EMBL; AY063931; AAL36287.1; -; mRNA.
DR EMBL; AY048294; AAK82556.1; -; mRNA.
DR EMBL; AY091254; AAM14193.1; -; mRNA.
DR EMBL; AY084470; AAM61041.1; -; mRNA.
DR EMBL; Z25965; CAA81120.1; -; mRNA.
DR PIR; T02451; T02451.
DR RefSeq; NP_182120.1; NM_130159.4. [Q06611-1]
DR AlphaFoldDB; Q06611; -.
DR SMR; Q06611; -.
DR BioGRID; 4540; 376.
DR IntAct; Q06611; 31.
DR iPTMnet; Q06611; -.
DR SwissPalm; Q06611; -.
DR PRIDE; Q06611; -.
DR EnsemblPlants; AT2G45960.1; AT2G45960.1; AT2G45960. [Q06611-1]
DR GeneID; 819204; -.
DR Gramene; AT2G45960.1; AT2G45960.1; AT2G45960. [Q06611-1]
DR KEGG; ath:AT2G45960; -.
DR Araport; AT2G45960; -.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; Q06611; -.
DR OMA; DIWTSHW; -.
DR PhylomeDB; Q06611; -.
DR PRO; PR:Q06611; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q06611; baseline and differential.
DR Genevisible; Q06611; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR GO; GO:0009414; P:response to water deprivation; IBA:GO_Central.
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; Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="Aquaporin PIP1-2"
FT /id="PRO_0000064047"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..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..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..116
FT /note="NPA 1"
FT MOTIF 235..237
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:16839310"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT CONFLICT 29
FT /note="Missing (in Ref. 6; AAM61041)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="F -> L (in Ref. 2; CAB37860)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> T (in Ref. 6; AAM61041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 30598 MW; 80F12775B6809013 CRC64;
MEGKEEDVRV GANKFPERQP IGTSAQSDKD YKEPPPAPLF EPGELASWSF WRAGIAEFIA
TFLFLYITVL TVMGVKRSPN MCASVGIQGI AWAFGGMIFA LVYCTAGISG GHINPAVTFG
LFLARKLSLT RAVYYIVMQC LGAICGAGVV KGFQPKQYQA LGGGANTIAH GYTKGSGLGA
EIIGTFVLVY TVFSATDAKR NARDSHVPIL APLPIGFAVF LVHLATIPIT GTGINPARSL
GAAIIFNKDN AWDDHWVFWV GPFIGAALAA LYHVIVIRAI PFKSRS
