TIP51_ARATH
ID TIP51_ARATH Reviewed; 256 AA.
AC Q9STX9;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable aquaporin TIP5-1;
DE AltName: Full=Tonoplast intrinsic protein 5-1;
DE Short=AtTIP5;1;
GN Name=TIP5-1; OrderedLocusNames=At3g47440; ORFNames=T21L8.190;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
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: Potential aquaporin, which may facilitate the transport of
CC water and small neutral solutes across cell membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AL096860; CAB51216.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78281.1; -; Genomic_DNA.
DR EMBL; BX826124; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T12999; T12999.
DR RefSeq; NP_190328.1; NM_114612.4.
DR AlphaFoldDB; Q9STX9; -.
DR SMR; Q9STX9; -.
DR BioGRID; 9218; 1.
DR IntAct; Q9STX9; 1.
DR STRING; 3702.AT3G47440.1; -.
DR TCDB; 1.A.8.10.7; the major intrinsic protein (mip) family.
DR PaxDb; Q9STX9; -.
DR PRIDE; Q9STX9; -.
DR ProteomicsDB; 246445; -.
DR EnsemblPlants; AT3G47440.1; AT3G47440.1; AT3G47440.
DR GeneID; 823898; -.
DR Gramene; AT3G47440.1; AT3G47440.1; AT3G47440.
DR KEGG; ath:AT3G47440; -.
DR Araport; AT3G47440; -.
DR TAIR; locus:2099595; AT3G47440.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; Q9STX9; -.
DR OMA; MSSRKLM; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q9STX9; -.
DR PRO; PR:Q9STX9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STX9; baseline and differential.
DR Genevisible; Q9STX9; 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:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR GO; GO:0048235; P:pollen sperm cell differentiation; IEP:TAIR.
DR GO; GO:0015840; P:urea transport; IDA:TAIR.
DR GO; GO:0006833; P:water transport; IBA:GO_Central.
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 PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..256
FT /note="Probable aquaporin TIP5-1"
FT /id="PRO_0000064017"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 87..89
FT /note="NPA 1"
FT MOTIF 200..202
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT CONFLICT 237
FT /note="N -> T (in Ref. 3; BX826124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 26643 MW; 9E128A148943E84E CRC64;
MRRMIPTSFS SKFQGVLSMN ALRCYVSEFI STFFFVLAAV GSVMSSRKLM AGDVSGPFGV
LIPAIANALA LSSSVYISWN VSGGHVNPAV TFAMAVAGRI SVPTAMFYWT SQMIASVMAC
LVLKVTVMEQ HVPIYKIAGE MTGFGASVLE GVLAFVLVYT VFTASDPRRG LPLAVGPIFI
GFVAGANVLA AGPFSGGSMN PACAFGSAMV YGSFKNQAVY WVGPLLGGAT AALVYDNVVV
PVEDDRGSST GDAIGV
