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TIP21_ARATH
ID   TIP21_ARATH             Reviewed;         250 AA.
AC   Q41951; Q0WM76; Q42200; Q42201; Q43352; Q8VZ81;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Aquaporin TIP2-1;
DE   AltName: Full=Delta-tonoplast intrinsic protein;
DE            Short=Delta-TIP;
DE   AltName: Full=Tonoplast intrinsic protein 2-1;
DE            Short=AtTIP2;1;
DE   Contains:
DE     RecName: Full=Aquaporin TIP2-1, N-terminally processed;
GN   Name=TIP2-1; OrderedLocusNames=At3g16240; ORFNames=MYA6.10;
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 / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-116.
RC   STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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   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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-106.
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-250.
RC   STRAIN=cv. Columbia; TISSUE=Shoot;
RX   PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA   Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA   Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA   Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA   Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA   Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA   Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT   a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
RN   [9]
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   [10]
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   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=14576283; DOI=10.1104/pp.103.027409;
RA   Liu L.-H., Ludewig U., Gassert B., Frommer W.B., von Wiren N.;
RT   "Urea transport by nitrogen-regulated tonoplast intrinsic proteins in
RT   Arabidopsis.";
RL   Plant Physiol. 133:1220-1228(2003).
RN   [12]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=15665250; DOI=10.1104/pp.104.051268;
RA   Loque D., Ludewig U., Yuan L., von Wiren N.;
RT   "Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3
RT   transport into the vacuole.";
RL   Plant Physiol. 137:671-680(2005).
RN   [13]
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).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA   Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA   Garin J., Bourguignon J.;
RT   "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT   cell culture.";
RL   Mol. Cell. Proteomics 6:394-412(2007).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Aquaporin required to facilitate the transport of water from
CC       the vacuolar compartment to the cytoplasm. Does not promote glycerol
CC       permeability. Its function is impaired by Hg(2+). Transports urea in
CC       yeast cells and Xenopus laevis oocytes in a pH-independent manner.
CC       Transports methylammonium or ammonium in yeast cells and Xenopus laevis
CC       oocytes, preferentially at high medium pH. May participate in vacuolar
CC       compartmentation and detoxification of ammonium.
CC       {ECO:0000269|PubMed:14576283, ECO:0000269|PubMed:15665250,
CC       ECO:0000269|PubMed:8624437}.
CC   -!- SUBUNIT: Interacts with cucumber mosaic virus (CMV) Protein 1a.
CC       {ECO:0000269|PubMed:17030879}.
CC   -!- INTERACTION:
CC       Q41951; Q41951: TIP2-1; NbExp=2; IntAct=EBI-4442669, EBI-4442669;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10737809,
CC       ECO:0000269|PubMed:14576283, ECO:0000269|PubMed:17151019,
CC       ECO:0000269|PubMed:8624437}; Multi-pass membrane protein {ECO:0000255,
CC       ECO:0000269|PubMed:10737809, ECO:0000269|PubMed:14576283,
CC       ECO:0000269|PubMed:8624437}. Note=Tonoplast. It is specifically located
CC       in the tonoplast of protein storage vacuoles (PSV) (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in shoot, rosette, bolt and
CC       flowers. Also expressed in roots, flower buds and above ground.
CC       {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:8624437}.
CC   -!- DEVELOPMENTAL STAGE: Starts to be expressed in seedlings from 2 days
CC       ays after germination. {ECO:0000269|PubMed:14576283}.
CC   -!- INDUCTION: By ammonium nitrate in roots. Expressed in roots with a
CC       circadian rhythm showing an increase after onset of light, a peak
CC       approximately at midday and a decline to lowest levels before offset of
CC       light. {ECO:0000269|PubMed:15665250}.
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   -!- CAUTION: Was originally assigned as At3g16230, which is now a
CC       completely different protein not related to aquaporins. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA79093.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA82298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U39485; AAC49281.1; -; mRNA.
DR   EMBL; U39486; AAC49992.1; -; Genomic_DNA.
DR   EMBL; AB023046; BAB01264.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75789.1; -; Genomic_DNA.
DR   EMBL; AY065181; AAL38357.1; -; mRNA.
DR   EMBL; AY081622; AAM10184.1; -; mRNA.
DR   EMBL; AK229954; BAF01780.1; -; mRNA.
DR   EMBL; AY085921; AAM63133.1; -; mRNA.
DR   EMBL; Z18064; CAA79093.1; ALT_INIT; mRNA.
DR   EMBL; Z29043; CAA82298.1; ALT_INIT; mRNA.
DR   EMBL; Z29044; CAA82299.1; -; mRNA.
DR   RefSeq; NP_188245.1; NM_112495.4.
DR   PDB; 5I32; X-ray; 1.18 A; A=2-250.
DR   PDBsum; 5I32; -.
DR   AlphaFoldDB; Q41951; -.
DR   SMR; Q41951; -.
DR   BioGRID; 6204; 6.
DR   DIP; DIP-61927N; -.
DR   IntAct; Q41951; 4.
DR   STRING; 3702.AT3G16240.1; -.
DR   TCDB; 1.A.8.10.10; the major intrinsic protein (mip) family.
DR   iPTMnet; Q41951; -.
DR   PaxDb; Q41951; -.
DR   PRIDE; Q41951; -.
DR   ProteomicsDB; 232426; -.
DR   EnsemblPlants; AT3G16240.1; AT3G16240.1; AT3G16240.
DR   GeneID; 820870; -.
DR   Gramene; AT3G16240.1; AT3G16240.1; AT3G16240.
DR   KEGG; ath:AT3G16240; -.
DR   Araport; AT3G16240; -.
DR   TAIR; locus:2094977; AT3G16240.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_4_1; -.
DR   InParanoid; Q41951; -.
DR   OMA; IYPNVFM; -.
DR   OrthoDB; 1152704at2759; -.
DR   PhylomeDB; Q41951; -.
DR   PRO; PR:Q41951; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q41951; baseline and differential.
DR   Genevisible; Q41951; AT.
DR   GO; GO:0042807; C:central vacuole; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA: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:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0000326; C:protein storage vacuole; IDA:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0015200; F:methylammonium transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015250; F:water channel activity; 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   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..250
FT                   /note="Aquaporin TIP2-1"
FT                   /id="PRO_0000425759"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..250
FT                   /note="Aquaporin TIP2-1, N-terminally processed"
FT                   /id="PRO_0000064011"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..54
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..141
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..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..215
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..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         2
FT                   /note="N-acetylalanine; in Aquaporin TIP2-1, N-terminally
FT                   processed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MUTAGEN         116
FT                   /note="C->S: Reduces the mercury-sensitivity."
FT                   /evidence="ECO:0000269|PubMed:8624437"
FT   CONFLICT        40
FT                   /note="I -> Y (in Ref. 6; CAA79093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="W -> L (in Ref. 6; CAA79093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124..126
FT                   /note="GGL -> KTQ (in Ref. 8; CAA82298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="G -> E (in Ref. 4; AAL38357/AAM10184)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..12
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           15..46
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           53..74
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   TURN            75..78
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           84..92
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           98..122
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           139..160
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           169..188
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   TURN            189..192
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           198..208
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   TURN            212..215
FT                   /evidence="ECO:0007829|PDB:5I32"
FT   HELIX           216..235
FT                   /evidence="ECO:0007829|PDB:5I32"
SQ   SEQUENCE   250 AA;  25027 MW;  4CBEF20B22CC40D9 CRC64;
     MAGVAFGSFD DSFSLASLRA YLAEFISTLL FVFAGVGSAI AYAKLTSDAA LDTPGLVAIA
     VCHGFALFVA VAIGANISGG HVNPAVTFGL AVGGQITVIT GVFYWIAQLL GSTAACFLLK
     YVTGGLAVPT HSVAAGLGSI EGVVMEIIIT FALVYTVYAT AADPKKGSLG TIAPLAIGLI
     VGANILAAGP FSGGSMNPAR SFGPAVAAGD FSGHWVYWVG PLIGGGLAGL IYGNVFMGSS
     EHVPLASADF
 
 
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