PIP24_ARATH
ID PIP24_ARATH Reviewed; 291 AA.
AC Q9FF53; Q0WQH7;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Probable aquaporin PIP2-4;
DE AltName: Full=Plasma membrane intrinsic protein 2.4;
DE Short=AtPIP2;4;
DE Contains:
DE RecName: Full=Probable aquaporin PIP2-4, N-terminally processed;
GN Name=PIP2-4; OrderedLocusNames=At5g60660; ORFNames=MUP24.9;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12566588; DOI=10.1105/tpc.008888;
RA Javot H., Lauvergeat V., Santoni V., Martin-Laurent F., Gueclue J.,
RA Vinh J., Heyes J., Franck K.I., Schaeffner A.R., Bouchez D., Maurel C.;
RT "Role of a single aquaporin isoform in root water uptake.";
RL Plant Cell 15:509-522(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-286, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC neutral solutes across cell membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:11806824}.
CC -!- DOMAIN: The Asn-Pro-Ala (NPA) motifs may contribute to the formation of
CC two hemipores that could generate a narrow channel. {ECO:0000250}.
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; AB005246; BAB09839.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97364.1; -; Genomic_DNA.
DR EMBL; AK228720; BAF00622.1; -; mRNA.
DR EMBL; AY087245; AAM64801.1; -; mRNA.
DR RefSeq; NP_200874.1; NM_125459.4.
DR PDB; 6QIM; X-ray; 3.70 A; A/B=29-279.
DR PDBsum; 6QIM; -.
DR AlphaFoldDB; Q9FF53; -.
DR SMR; Q9FF53; -.
DR BioGRID; 21431; 7.
DR IntAct; Q9FF53; 1.
DR STRING; 3702.AT5G60660.1; -.
DR iPTMnet; Q9FF53; -.
DR PaxDb; Q9FF53; -.
DR PRIDE; Q9FF53; -.
DR ProteomicsDB; 234758; -.
DR EnsemblPlants; AT5G60660.1; AT5G60660.1; AT5G60660.
DR GeneID; 836187; -.
DR Gramene; AT5G60660.1; AT5G60660.1; AT5G60660.
DR KEGG; ath:AT5G60660; -.
DR Araport; AT5G60660; -.
DR TAIR; locus:2175831; AT5G60660.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; Q9FF53; -.
DR OMA; VNESGPP; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q9FF53; -.
DR PRO; PR:Q9FF53; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF53; baseline and differential.
DR Genevisible; Q9FF53; 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:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0015250; F:water channel activity; ISS:TAIR.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP: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 3D-structure; Acetylation; Cell membrane; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..291
FT /note="Probable aquaporin PIP2-4"
FT /id="PRO_0000425769"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q41951"
FT CHAIN 2..291
FT /note="Probable aquaporin PIP2-4, N-terminally processed"
FT /id="PRO_0000064054"
FT TOPO_DOM 2..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..109
FT /note="NPA 1"
FT MOTIF 228..230
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 2
FT /note="N-acetylalanine; in Probable aquaporin PIP2-4, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q41951"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
SQ SEQUENCE 291 AA; 30952 MW; 8ABDC8ACD00F9076 CRC64;
MAKDLDVNES GPPAARDYKD PPPAPFFDME ELRKWPLYRA VIAEFVATLL FLYVSILTVI
GYKAQTDATA GGVDCGGVGI LGIAWAFGGM IFVLVYCTAG ISGGHINPAV TVGLFLARKV
SLVRTVLYIV AQCLGAICGC GFVKAFQSSY YTRYGGGANE LADGYNKGTG LGAEIIGTFV
LVYTVFSATD PKRNARDSHV PVLAPLPIGF AVFMVHLATI PITGTGINPA RSFGAAVIYN
NEKAWDDQWI FWVGPMIGAA AAAFYHQFIL RAAAIKALGS FGSFGSFRSF A
