TIP31_ARATH
ID TIP31_ARATH Reviewed; 268 AA.
AC P26587;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Aquaporin TIP3-1;
DE AltName: Full=Alpha-tonoplast intrinsic protein;
DE Short=Alpha-TIP;
DE AltName: Full=Tonoplast intrinsic protein 3-1;
DE Short=AtTIP3;1;
DE Contains:
DE RecName: Full=Aquaporin TIP3-1, N-terminally processed;
GN Name=TIP3-1; OrderedLocusNames=At1g73190; ORFNames=T18K17.14;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16668923; DOI=10.1104/pp.99.2.561;
RA Hoefte H.R., Hubbard L., Reizer J., Ludevid D., Kerman E.M.,
RA Chrispeels M.J.;
RT "Vegetative and seed-specific forms of tonoplast intrinsic protein in the
RT vacuolar membrane of Arabidopsis thaliana.";
RL Plant Physiol. 99:561-570(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 TISSUE SPECIFICITY.
RX PubMed=8624437; DOI=10.2307/3870337;
RA Daniels M.J., Chaumont F., Mirkov T.E., Chrispeels M.J.;
RT "Characterization of a new vacuolar membrane aquaporin sensitive to mercury
RT at a unique site.";
RL Plant Cell 8:587-599(1996).
RN [6]
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).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC from the vacuolar compartment to the cytoplasm.
CC {ECO:0000269|PubMed:16668923}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16668923};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16668923}.
CC Note=Tonoplast. It is specifically located in the tonoplast of protein
CC storage vacuoles (PSV) of the embryo and endosperm.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in developing embryos
CC (seeds). Also expressed in green siliques.
CC {ECO:0000269|PubMed:16668923, ECO:0000269|PubMed:8624437}.
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; X63551; CAA45114.1; -; Genomic_DNA.
DR EMBL; M84343; AAA32748.1; -; Genomic_DNA.
DR EMBL; AC010556; AAG52132.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35427.1; -; Genomic_DNA.
DR EMBL; AY064054; AAL36410.1; -; mRNA.
DR EMBL; AY117339; AAM51414.1; -; mRNA.
DR PIR; S22201; S22201.
DR RefSeq; NP_177462.1; NM_105978.4.
DR AlphaFoldDB; P26587; -.
DR SMR; P26587; -.
DR BioGRID; 28872; 5.
DR IntAct; P26587; 5.
DR STRING; 3702.AT1G73190.1; -.
DR TCDB; 1.A.8.10.1; the major intrinsic protein (mip) family.
DR PaxDb; P26587; -.
DR PRIDE; P26587; -.
DR ProteomicsDB; 234404; -.
DR EnsemblPlants; AT1G73190.1; AT1G73190.1; AT1G73190.
DR GeneID; 843653; -.
DR Gramene; AT1G73190.1; AT1G73190.1; AT1G73190.
DR KEGG; ath:AT1G73190; -.
DR Araport; AT1G73190; -.
DR TAIR; locus:2197279; AT1G73190.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; P26587; -.
DR OMA; VMVAVMD; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P26587; -.
DR PRO; PR:P26587; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P26587; baseline and differential.
DR Genevisible; P26587; 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:0000326; C:protein storage vacuole; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; TAS:TAIR.
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; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..268
FT /note="Aquaporin TIP3-1"
FT /id="PRO_0000425762"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q41951"
FT CHAIN 2..268
FT /note="Aquaporin TIP3-1, N-terminally processed"
FT /id="PRO_0000064014"
FT TOPO_DOM 2..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..64
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..146
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..225
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 93..95
FT /note="NPA 1"
FT MOTIF 207..209
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 2
FT /note="N-acetylalanine; in Aquaporin TIP3-1, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:Q41951"
SQ SEQUENCE 268 AA; 28308 MW; E9D6C84D1DA1E4BA CRC64;
MATSARRAYG FGRADEATHP DSIRATLAEF LSTFVFVFAA EGSILSLDKL YWEHAAHAGT
NTPGGLILVA LAHAFALFAA VSAAINVSGG HVNPAVTFGA LVGGRVTAIR AIYYWIAQLL
GAILACLLLR LTTNGMRPVG FRLASGVGAV NGLVLEIILT FGLVYVVYST LIDPKRGSLG
IIAPLAIGLI VGANILVGGP FSGASMNPAR AFGPALVGWR WHDHWIYWVG PFIGSALAAL
IYEYMVIPTE PPTHHAHGVH QPLAPEDY
