TIP41_ARATH
ID TIP41_ARATH Reviewed; 249 AA.
AC O82316; Q53XD1;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Aquaporin TIP4-1;
DE AltName: Full=Epsilon-tonoplast intrinsic protein;
DE Short=Epsilon-TIP;
DE AltName: Full=Tonoplast intrinsic protein 4-1;
DE Short=AtTIP4;1;
GN Name=TIP4-1; OrderedLocusNames=At2g25810; ORFNames=F17H15.16;
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=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 [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 Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-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 DEVELOPMENTAL STAGE.
RX PubMed=14576283; DOI=10.1104/pp.103.027409;
RA Liu L.-H., Ludewig U., Gassert B., Frommer W.B., von Wiren N.;
RT "Urea transport by nitrogen-regulated tonoplast intrinsic proteins in
RT Arabidopsis.";
RL Plant Physiol. 133:1220-1228(2003).
CC -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC neutral solutes across cell membranes. Transports urea in yeast cells
CC in a pH-independent manner. {ECO:0000269|PubMed:14576283}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14576283};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14576283}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:11806824}.
CC -!- DEVELOPMENTAL STAGE: Starts to be expressed in seedlings from 2 days
CC ays after germination. {ECO:0000269|PubMed:14576283}.
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; AC005395; AAC42249.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07755.1; -; Genomic_DNA.
DR EMBL; BT012635; AAT06454.1; -; mRNA.
DR EMBL; AK226190; BAE98355.1; -; mRNA.
DR PIR; A84653; A84653.
DR RefSeq; NP_180152.1; NM_128141.6.
DR AlphaFoldDB; O82316; -.
DR SMR; O82316; -.
DR BioGRID; 2475; 16.
DR IntAct; O82316; 16.
DR STRING; 3702.AT2G25810.1; -.
DR PaxDb; O82316; -.
DR ProteomicsDB; 234431; -.
DR EnsemblPlants; AT2G25810.1; AT2G25810.1; AT2G25810.
DR GeneID; 817123; -.
DR Gramene; AT2G25810.1; AT2G25810.1; AT2G25810.
DR KEGG; ath:AT2G25810; -.
DR Araport; AT2G25810; -.
DR TAIR; locus:2043505; AT2G25810.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; O82316; -.
DR OMA; YETHTPL; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; O82316; -.
DR PRO; PR:O82316; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82316; baseline and differential.
DR Genevisible; O82316; 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: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 2: Evidence at transcript level;
KW Acetylation; Membrane; Methylation; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..249
FT /note="Aquaporin TIP4-1"
FT /id="PRO_0000064016"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..49
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..137
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..212
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 79..81
FT /note="NPA 1"
FT MOTIF 193..195
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"
SQ SEQUENCE 249 AA; 26073 MW; 1A52B34B5CEF4693 CRC64;
MKKIELGHHS EAAKPDCIKA LIVEFITTFL FVFAGVGSAM ATDSLVGNTL VGLFAVAVAH
AFVVAVMISA GHISGGHLNP AVTLGLLLGG HISVFRAFLY WIDQLLASSA ACFLLSYLTG
GMGTPVHTLA SGVSYTQGII WEIILTFSLL FTVYATIVDP KKGSLDGFGP LLTGFVVGAN
ILAGGAFSGA SMNPARSFGP ALVSGNWTDH WVYWVGPLIG GGLAGFIYEN VLIDRPHVPV
ADDEQPLLN
