TIP23_ARATH
ID TIP23_ARATH Reviewed; 250 AA.
AC Q9FGL2; Q0WNU5; Q53XE4;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Aquaporin TIP2-3;
DE AltName: Full=Tonoplast intrinsic protein 2-3;
DE Short=AtTIP2;3;
GN Name=TIP2-3; OrderedLocusNames=At5g47450; ORFNames=MNJ7.4;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15665250; DOI=10.1104/pp.104.051268;
RA Loque D., Ludewig U., Yuan L., von Wiren N.;
RT "Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3
RT transport into the vacuole.";
RL Plant Physiol. 137:671-680(2005).
RN [7]
RP INTERACTION WITH CMV PROTEIN 1A.
RX PubMed=17030879; DOI=10.1099/vir.0.82252-0;
RA Kim M.J., Kim H.R., Paek K.-H.;
RT "Arabidopsis tonoplast proteins TIP1 and TIP2 interact with the cucumber
RT mosaic virus 1a replication protein.";
RL J. Gen. Virol. 87:3425-3431(2006).
CC -!- FUNCTION: Transports methylammonium or ammonium in yeast cells,
CC preferentially at high medium pH. May participate in vacuolar
CC compartmentation and detoxification of ammonium.
CC {ECO:0000269|PubMed:15665250}.
CC -!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
CC {ECO:0000269|PubMed:17030879}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15665250};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15665250}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11806824}.
CC -!- INDUCTION: By ammonium nitrate in roots. Expressed in roots with a
CC circadian rhythm showing an increase after onset of light, a peak
CC approximately at midday and a decline to lowest levels before offset of
CC light. {ECO:0000269|PubMed:15665250}.
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. TIP (TC
CC 1.A.8.10) subfamily. {ECO:0000305}.
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DR EMBL; AB025628; BAB09071.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95514.1; -; Genomic_DNA.
DR EMBL; BT011212; AAR92248.1; -; mRNA.
DR EMBL; BT011663; AAS47669.1; -; mRNA.
DR EMBL; AK229341; BAF01204.1; -; mRNA.
DR RefSeq; NP_199556.1; NM_124117.3.
DR AlphaFoldDB; Q9FGL2; -.
DR SMR; Q9FGL2; -.
DR BioGRID; 20042; 2.
DR IntAct; Q9FGL2; 1.
DR STRING; 3702.AT5G47450.1; -.
DR TCDB; 1.A.8.10.4; the major intrinsic protein (mip) family.
DR PaxDb; Q9FGL2; -.
DR PRIDE; Q9FGL2; -.
DR ProteomicsDB; 234305; -.
DR EnsemblPlants; AT5G47450.1; AT5G47450.1; AT5G47450.
DR GeneID; 834794; -.
DR Gramene; AT5G47450.1; AT5G47450.1; AT5G47450.
DR KEGG; ath:AT5G47450; -.
DR Araport; AT5G47450; -.
DR TAIR; locus:2168953; AT5G47450.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; Q9FGL2; -.
DR OMA; CRREDIM; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q9FGL2; -.
DR PRO; PR:Q9FGL2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGL2; baseline and differential.
DR Genevisible; Q9FGL2; AT.
DR GO; GO:0042807; C:central vacuole; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0015200; F:methylammonium transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR GO; GO:0006833; P:water transport; 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; PTHR45665; PTHR45665; 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; Membrane; Methylation; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..250
FT /note="Aquaporin TIP2-3"
FT /id="PRO_0000064013"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..54
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..134
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..217
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 83..85
FT /note="NPA 1"
FT MOTIF 197..199
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT CONFLICT 141
FT /note="E -> G (in Ref. 4; BAF01204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 25245 MW; 8946CB520D42603C CRC64;
MVKIEVGSVG DSFSVSSLKA YLSEFIATLL FVFAGVGSAV AFAKLTSDGA LDPAGLVAIA
IAHAFALFVG VSIAANISGG HLNPAVTLGL AIGGNITLIT GFFYWIAQCL GSIVACLLLV
FVTNGKSVPT HGVSAGLGAV EGVVMEIVVT FALVYTVYAT AADPKKGSLG TIAPIAIGFI
VGANILAAGP FSGGSMNPAR SFGPAVVSGD LSQIWIYWVG PLVGGALAGL IYGDVFIGSY
EAVETREIRV
