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   27-MAR-2024, entry version 180.
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
CC       (TC 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   STRING; 3702.Q06611; -.
DR   iPTMnet; Q06611; -.
DR   SwissPalm; 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   TAIR; AT2G45960; PIP1B.
DR   HOGENOM; CLU_020019_3_0_1; -.
DR   InParanoid; Q06611; -.
DR   OMA; MSIVIAM; -.
DR   PhylomeDB; Q06611; -.
DR   PRO; PR:Q06611; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q06611; baseline and differential.
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; Glycerol uptake facilitator protein; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   NCBIfam; TIGR00861; MIP; 1.
DR   PANTHER; PTHR45687; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1.
DR   PANTHER; PTHR45687:SF45; AQUAPORIN PIP1-2; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
DR   PROSITE; PS00221; MIP; 1.
DR   Genevisible; Q06611; AT.
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
//