TIP22_ARATH
ID TIP22_ARATH Reviewed; 250 AA.
AC Q41975; O23577;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Probable aquaporin TIP2-2;
DE AltName: Full=Tonoplast intrinsic protein 2-2;
DE Short=AtTIP2;2;
GN Name=TIP2-2; OrderedLocusNames=At4g17340; ORFNames=dl4705w, FCAALL.412;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-110.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10737809; DOI=10.1073/pnas.97.7.3718;
RA Cutler S.R., Ehrhardt D.W., Griffitts J.S., Somerville C.R.;
RT "Random GFP::cDNA fusions enable visualization of subcellular structures in
RT cells of Arabidopsis at a high frequency.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3718-3723(2000).
RN [8]
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 [9]
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: Aquaporins facilitate the transport of water and small
CC 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:0000269|PubMed:10737809};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10737809}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Expressed above groung and in roots.
CC {ECO:0000269|PubMed:11806824}.
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; Z97343; CAB10515.1; -; Genomic_DNA.
DR EMBL; AL161546; CAB78737.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83878.1; -; Genomic_DNA.
DR EMBL; AY056063; AAL06963.1; -; mRNA.
DR EMBL; AF367283; AAK56272.1; -; mRNA.
DR EMBL; AY088929; AAM67235.1; -; mRNA.
DR EMBL; Z18142; CAA79115.1; -; mRNA.
DR PIR; F71442; F71442.
DR RefSeq; NP_193465.1; NM_117838.4.
DR AlphaFoldDB; Q41975; -.
DR SMR; Q41975; -.
DR BioGRID; 12739; 12.
DR IntAct; Q41975; 10.
DR STRING; 3702.AT4G17340.1; -.
DR PaxDb; Q41975; -.
DR ProteomicsDB; 246429; -.
DR EnsemblPlants; AT4G17340.1; AT4G17340.1; AT4G17340.
DR GeneID; 827446; -.
DR Gramene; AT4G17340.1; AT4G17340.1; AT4G17340.
DR KEGG; ath:AT4G17340; -.
DR Araport; AT4G17340; -.
DR TAIR; locus:2130883; AT4G17340.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; Q41975; -.
DR OMA; YILFPQS; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q41975; -.
DR PRO; PR:Q41975; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q41975; baseline and differential.
DR Genevisible; Q41975; 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:0000325; C:plant-type vacuole; HDA:TAIR.
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 1: Evidence at protein level;
KW Acetylation; Membrane; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..250
FT /note="Probable aquaporin TIP2-2"
FT /id="PRO_0000064012"
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..53
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..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..133
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..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..210
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..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 MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
SQ SEQUENCE 250 AA; 25080 MW; C1FF7901609A2108 CRC64;
MVKIEIGSVG DSFSVASLKA YLSEFIATLL FVFAGVGSAL AFAKLTSDAA LDPAGLVAVA
VAHAFALFVG VSIAANISGG HLNPAVTLGL AVGGNITVIT GFFYWIAQCL GSIVACLLLV
FVTNGESVPT HGVAAGLGAI EGVVMEIVVT FALVYTVYAT AADPKKGSLG TIAPIAIGFI
VGANILAAGP FSGGSMNPAR SFGPAVVSGD FSQIWIYWVG PLVGGALAGL IYGDVFIGSY
APAPTTESYP
