PIP11_ARATH
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 25-MAY-2022, entry version 146.
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 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].
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 [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 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 [8]
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 (TC
CC 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://web.expasy.org/spotlight/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; 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 IntAct; P61837; 5.
DR STRING; 3702.AT3G61430.2; -.
DR TCDB; 1.A.8.11.3; the major intrinsic protein (mip) family.
DR iPTMnet; P61837; -.
DR PaxDb; P61837; -.
DR PRIDE; P61837; -.
DR ProteomicsDB; 234958; -.
DR EnsemblPlants; AT3G61430.1; AT3G61430.1; AT3G61430.
DR EnsemblPlants; AT3G61430.2; AT3G61430.2; AT3G61430.
DR GeneID; 825316; -.
DR Gramene; AT3G61430.1; AT3G61430.1; AT3G61430.
DR Gramene; AT3G61430.2; AT3G61430.2; AT3G61430.
DR KEGG; ath:AT3G61430; -.
DR Araport; AT3G61430; -.
DR TAIR; locus:2082822; AT3G61430.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; P61837; -.
DR OMA; GSFANWV; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P61837; -.
DR PRO; PR:P61837; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P61837; baseline and differential.
DR Genevisible; P61837; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 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. 5; 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
