TIP32_ARATH
ID TIP32_ARATH Reviewed; 267 AA.
AC O22588; Q0WPM9;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Probable aquaporin TIP3-2;
DE AltName: Full=Beta-tonoplast intrinsic protein;
DE Short=Beta-TIP;
DE AltName: Full=Tonoplast intrinsic protein 3-2;
DE Short=AtTIP3;2;
DE Contains:
DE RecName: Full=Probable aquaporin TIP3-2, N-terminally processed;
GN Name=TIP3-2; OrderedLocusNames=At1g17810; ORFNames=F2H15.4;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Peck S.C., Trentmann S.M., Kende H.;
RT "Regulation of Arabidopsis Beta-TIP in etiolated seedlings.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
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;
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).
CC -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC neutral solutes across cell membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Tonoplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22588-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in developing seeds. Also
CC expressed in rosette leaves. {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; AF026275; AAB84183.1; -; mRNA.
DR EMBL; AC034106; AAF97261.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29639.1; -; Genomic_DNA.
DR EMBL; AK229035; BAF00920.1; -; mRNA.
DR PIR; B86313; B86313.
DR RefSeq; NP_173223.1; NM_101644.3. [O22588-1]
DR AlphaFoldDB; O22588; -.
DR SMR; O22588; -.
DR BioGRID; 23598; 4.
DR IntAct; O22588; 3.
DR STRING; 3702.AT1G17810.1; -.
DR PaxDb; O22588; -.
DR PRIDE; O22588; -.
DR EnsemblPlants; AT1G17810.1; AT1G17810.1; AT1G17810. [O22588-1]
DR GeneID; 838359; -.
DR Gramene; AT1G17810.1; AT1G17810.1; AT1G17810. [O22588-1]
DR KEGG; ath:AT1G17810; -.
DR Araport; AT1G17810; -.
DR TAIR; locus:2030968; AT1G17810.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; O22588; -.
DR OMA; WTPGPLH; -.
DR PhylomeDB; O22588; -.
DR PRO; PR:O22588; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22588; baseline and differential.
DR Genevisible; O22588; 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: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; Alternative splicing; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..267
FT /note="Probable aquaporin TIP3-2"
FT /id="PRO_0000425763"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q41951"
FT CHAIN 2..267
FT /note="Probable aquaporin TIP3-2, N-terminally processed"
FT /id="PRO_0000064015"
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..66
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..151
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..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..226
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..267
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 Probable aquaporin TIP3-2, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q41951"
SQ SEQUENCE 267 AA; 28183 MW; 859E0DE51ACF36FE CRC64;
MATSARRAYG FGRADEATHP DSIRATLAEF LSTFVFVFAG EGSILALDKL YWDTAAHTGT
NTPGGLVLVA LAHALALFAA VSAAINVSGG HVNPAVTFAA LIGGRISVIR AIYYWVAQLI
GAILACLLLR LATNGLRPVG FHVASGVSEL HGLLMEIILT FALVYVVYST AIDPKRGSIG
IIAPLAIGLI VGANILVGGP FDGASMNPAR AFGPALVGWR WSNHWIYWVG PFIGGALAAL
IYEYMIIPSV NEPPHHSTHQ PLAPEDY
