TIP13_ARATH
ID TIP13_ARATH Reviewed; 252 AA.
AC O82598; A0MF47; Q1PEC5;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Aquaporin TIP1-3;
DE AltName: Full=Gamma-tonoplast intrinsic protein 3;
DE Short=Gamma-TIP3;
DE AltName: Full=Tonoplast intrinsic protein 1-3;
DE Short=AtTIP1;3;
GN Name=TIP1-3; OrderedLocusNames=At4g01470; ORFNames=F11O4.1;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NOMENCLATURE.
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 [5]
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: Potential aquaporin, which may facilitate the transport of
CC water and small neutral solutes across cell membranes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
CC {ECO:0000269|PubMed:17030879}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Tonoplast.
CC -!- INDUCTION: By dehydration. Not affected by water stress.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28617.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF096370; AAC62778.1; -; Genomic_DNA.
DR EMBL; AL161492; CAB77717.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82031.1; -; Genomic_DNA.
DR EMBL; DQ446793; ABE66039.1; -; mRNA.
DR EMBL; DQ653172; ABK28617.1; ALT_SEQ; mRNA.
DR PIR; T01947; T01947.
DR RefSeq; NP_192056.1; NM_116377.2.
DR AlphaFoldDB; O82598; -.
DR SMR; O82598; -.
DR BioGRID; 13342; 1.
DR IntAct; O82598; 1.
DR STRING; 3702.AT4G01470.1; -.
DR TCDB; 1.A.8.10.6; the major intrinsic protein (mip) family.
DR PaxDb; O82598; -.
DR PRIDE; O82598; -.
DR ProteomicsDB; 234280; -.
DR EnsemblPlants; AT4G01470.1; AT4G01470.1; AT4G01470.
DR GeneID; 828051; -.
DR Gramene; AT4G01470.1; AT4G01470.1; AT4G01470.
DR KEGG; ath:AT4G01470; -.
DR Araport; AT4G01470; -.
DR TAIR; locus:2116987; AT4G01470.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; O82598; -.
DR OMA; NPIHAVC; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; O82598; -.
DR PRO; PR:O82598; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O82598; baseline and differential.
DR Genevisible; O82598; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR GO; GO:0015840; P:urea transport; IDA: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; PTHR45665; PTHR45665; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Reference proteome; Repeat; Stress response;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..252
FT /note="Aquaporin TIP1-3"
FT /id="PRO_0000064010"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..55
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..143
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..219
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 85..87
FT /note="NPA 1"
FT MOTIF 199..201
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
SQ SEQUENCE 252 AA; 25914 MW; F2FCC1D9DA44A76A CRC64;
MPINRIAIGT PGEASRPDAI RAAFAEFFSM VIFVFAGQGS GMAYGKLTGD GPATPAGLVA
ASLSHAFALF VAVSVGANVS GGHVNPAVTF GAFIGGNITL LRAILYWIAQ LLGAVVACLL
LKVSTGGMET AAFSLSYGVT PWNAVVFEIV MTFGLVYTVY ATAVDPKKGD IGIIAPLAIG
LIVGANILVG GAFDGASMNP AVSFGPAVVS WIWTNHWVYW VGPFIGAAIA AIVYDTIFIG
SNGHEPLPSN DF
