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Aquaporin TIP1-3 (Gamma-tonoplast intrinsic protein 3) (Gamma-TIP3) (Tonoplast intrinsic protein 1-3) (AtTIP1;3) [Cleaved into: Aquaporin TIP1-3, N-terminally processed]

 TIP13_ARATH             Reviewed;         252 AA.
O82598; A0MF47; Q1PEC5;
27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
30-AUG-2017, entry version 134.
RecName: Full=Aquaporin TIP1-3;
AltName: Full=Gamma-tonoplast intrinsic protein 3;
Short=Gamma-TIP3;
AltName: Full=Tonoplast intrinsic protein 1-3;
Short=AtTIP1;3;
Name=TIP1-3; OrderedLocusNames=At4g01470; ORFNames=F11O4.1;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
"Simultaneous high-throughput recombinational cloning of open reading
frames in closed and open configurations.";
Plant Biotechnol. J. 4:317-324(2006).
[4]
NOMENCLATURE.
PubMed=11806824;
Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
"From genome to function: the Arabidopsis aquaporins.";
Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
[5]
INTERACTION WITH CMV PROTEIN 1A.
PubMed=17030879; DOI=10.1099/vir.0.82252-0;
Kim M.J., Kim H.R., Paek K.-H.;
"Arabidopsis tonoplast proteins TIP1 and TIP2 interact with the
cucumber mosaic virus 1a replication protein.";
J. Gen. Virol. 87:3425-3431(2006).
-!- FUNCTION: Potential aquaporin, which may facilitate the transport
of water and small neutral solutes across cell membranes.
{ECO:0000250}.
-!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
{ECO:0000269|PubMed:17030879}.
-!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Note=Tonoplast.
-!- INDUCTION: By dehydration. Not affected by water stress.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA).
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP
(TC 1.A.8.10) subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABK28617.1; Type=Erroneous termination; Positions=253; Note=Translated as stop.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF096370; AAC62778.1; -; Genomic_DNA.
EMBL; AL161492; CAB77717.1; -; Genomic_DNA.
EMBL; CP002687; AEE82031.1; -; Genomic_DNA.
EMBL; DQ446793; ABE66039.1; -; mRNA.
EMBL; DQ653172; ABK28617.1; ALT_SEQ; mRNA.
PIR; T01947; T01947.
RefSeq; NP_192056.1; NM_116377.2.
UniGene; At.65315; -.
ProteinModelPortal; O82598; -.
SMR; O82598; -.
BioGrid; 13342; 1.
STRING; 3702.AT4G01470.1; -.
TCDB; 1.A.8.10.6; the major intrinsic protein (mip) family.
PaxDb; O82598; -.
EnsemblPlants; AT4G01470.1; AT4G01470.1; AT4G01470.
GeneID; 828051; -.
Gramene; AT4G01470.1; AT4G01470.1; AT4G01470.
KEGG; ath:AT4G01470; -.
Araport; AT4G01470; -.
TAIR; locus:2116987; AT4G01470.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; O82598; -.
KO; K09873; -.
OMA; MAYGKLT; -.
OrthoDB; EOG09360J95; -.
PhylomeDB; O82598; -.
Reactome; R-ATH-432047; Passive transport by Aquaporins.
PRO; PR:O82598; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; O82598; AT.
GO; GO:0042807; C:central vacuole; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
GO; GO:0015204; F:urea transmembrane transporter activity; IDA:TAIR.
GO; GO:0015250; F:water channel activity; IDA:TAIR.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0015840; P:urea transport; IDA:TAIR.
GO; GO:0006833; P:water transport; IDA:TAIR.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Membrane; Reference proteome; Repeat;
Stress response; Transmembrane; Transmembrane helix; Transport;
Vacuole.
CHAIN 1 252 Aquaporin TIP1-3.
/FTId=PRO_0000064010.
TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.
TRANSMEM 23 43 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 44 55 Vacuolar. {ECO:0000255}.
TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 77 114 Cytoplasmic. {ECO:0000255}.
TRANSMEM 115 135 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 136 143 Vacuolar. {ECO:0000255}.
TRANSMEM 144 164 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 165 170 Cytoplasmic. {ECO:0000255}.
TRANSMEM 171 191 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 192 219 Vacuolar. {ECO:0000255}.
TRANSMEM 220 240 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 241 252 Cytoplasmic. {ECO:0000255}.
MOTIF 85 87 NPA 1.
MOTIF 199 201 NPA 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P61837}.
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


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