ID   PIP11_ARATH             Reviewed;         286 AA.
AC   P61837; P43285; Q0WP60; Q8L9H0; Q9LDT6;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   02-SEP-2026, entry version 162.
DE   RecName: Full=Aquaporin PIP1-1;
DE            Short=AtPIP1;1;
DE   AltName: Full=Plasma membrane aquaporin-1;
DE   AltName: Full=Plasma membrane intrinsic protein 1a;
DE            Short=PIP1a;
GN   Name=PIP1-1; Synonyms=PIP1A; OrderedLocusNames=At3g61430;
GN   ORFNames=F2A19.30;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
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   [9]
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. Its function is impaired by Hg(2+).
CC       {ECO:0000269|PubMed:7920711}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7920711};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:7920711}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in roots, above ground
CC       and in flower buds. {ECO:0000269|PubMed:11806824,
CC       ECO:0000269|PubMed:7920711}.
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}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Liquid states - Issue 36 of
CC       July 2003;
CC       URL="https://www.proteinspotlight.org/back_issues/036";
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DR   EMBL; X75881; CAA53475.1; -; mRNA.
DR   EMBL; AL132962; CAB71073.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80201.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80202.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7045306.1; -; Genomic_DNA.
DR   EMBL; AY097398; AAM19914.1; -; mRNA.
DR   EMBL; AY058113; AAL25530.1; -; mRNA.
DR   EMBL; AK229222; BAF01089.1; -; mRNA.
DR   EMBL; AY088439; AAM65975.1; -; mRNA.
DR   PIR; T47935; T47935.
DR   RefSeq; NP_001078323.1; NM_001084854.2.
DR   RefSeq; NP_191702.1; NM_116008.4.
DR   AlphaFoldDB; P61837; -.
DR   SMR; P61837; -.
DR   BioGRID; 10630; 12.
DR   FunCoup; P61837; 206.
DR   IntAct; P61837; 5.
DR   STRING; 3702.P61837; -.
DR   TCDB; 1.A.8.11.3; the major intrinsic protein (mip) family.
DR   iPTMnet; P61837; -.
DR   PaxDb; 3702-P61837; -.
DR   ProteomicsDB; 234958; -.
DR   GeneID; 825316; -.
DR   KEGG; ath:AT3G61430; -.
DR   Araport; AT3G61430; -.
DR   TAIR; AT3G61430; PIP1A.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_0_1; -.
DR   InParanoid; P61837; -.
DR   OMA; QASCHEF; -.
DR   OrthoDB; 1026065at2759; -.
DR   PhylomeDB; P61837; -.
DR   PRO; PR:P61837; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P61837; baseline and differential.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; 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   FunFam; 1.20.1080.10:FF:000001; Probable aquaporin PIP1-2; 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   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..286
FT                   /note="Aquaporin PIP1-1"
FT                   /id="PRO_0000064045"
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..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..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        15
FT                   /note="F -> L (in Ref. 6; AAM65975)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="G -> A (in Ref. 1; CAA53475)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   286 AA;  30689 MW;  5C0284F6BB5EA7B7 CRC64;
     MEGKEEDVRV GANKFPERQP IGTSAQSDKD YKEPPPAPFF EPGELSSWSF WRAGIAEFIA
     TFLFLYITVL TVMGVKRSPN MCASVGIQGI AWAFGGMIFA LVYCTAGISG GHINPAVTFG
     LFLARKLSLT RALYYIVMQC LGAICGAGVV KGFQPKQYQA LGGGANTVAH GYTKGSGLGA
     EIIGTFVLVY TVFSATDAKR NARDSHVPIL APLPIGFAVF LVHLATIPIT GTGINPARSL
     GAAIIYNKDH SWDDHWVFWV GPFIGAALAA LYHVVVIRAI PFKSRS
//