PIP25_ARATH
ID PIP25_ARATH Reviewed; 286 AA.
AC Q9SV31;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Probable aquaporin PIP2-5;
DE AltName: Full=Plasma membrane intrinsic protein 2-5;
DE Short=AtPIP2;5;
DE AltName: Full=Plasma membrane intrinsic protein 2d;
DE Short=PIP2d;
GN Name=PIP2-5; Synonyms=PIP2D; OrderedLocusNames=At3g54820;
GN ORFNames=F28P10.200;
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=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 [4]
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 [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 -!- INTERACTION:
CC Q9SV31; Q08733: PIP1-3; NbExp=5; IntAct=EBI-4425112, EBI-4431134;
CC Q9SV31; Q39196: PIP1.4; NbExp=4; IntAct=EBI-4425112, EBI-4427223;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in green siliques.
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. PIP (TC
CC 1.A.8.11) subfamily. {ECO:0000305}.
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DR EMBL; AL049655; CAB41102.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79295.1; -; Genomic_DNA.
DR EMBL; AF370351; AAK44166.1; -; mRNA.
DR EMBL; AY062981; AAL34155.1; -; mRNA.
DR EMBL; BT000670; AAN31817.1; -; mRNA.
DR EMBL; AY084843; AAM61408.1; -; mRNA.
DR PIR; T06738; T06738.
DR RefSeq; NP_191042.1; NM_115339.3.
DR AlphaFoldDB; Q9SV31; -.
DR SMR; Q9SV31; -.
DR BioGRID; 9963; 13.
DR IntAct; Q9SV31; 11.
DR STRING; 3702.AT3G54820.1; -.
DR iPTMnet; Q9SV31; -.
DR PaxDb; Q9SV31; -.
DR PRIDE; Q9SV31; -.
DR ProteomicsDB; 235023; -.
DR EnsemblPlants; AT3G54820.1; AT3G54820.1; AT3G54820.
DR GeneID; 824647; -.
DR Gramene; AT3G54820.1; AT3G54820.1; AT3G54820.
DR KEGG; ath:AT3G54820; -.
DR Araport; AT3G54820; -.
DR TAIR; locus:2082642; AT3G54820.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; Q9SV31; -.
DR OMA; DKAWDHH; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q9SV31; -.
DR PRO; PR:Q9SV31; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SV31; baseline and differential.
DR Genevisible; Q9SV31; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; ISS:TAIR.
DR GO; GO:0006833; P:water transport; IMP: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; PTHR45687; PTHR45687; 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; Cell membrane; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="Probable aquaporin PIP2-5"
FT /id="PRO_0000064055"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 106..108
FT /note="NPA 1"
FT MOTIF 227..229
FT /note="NPA 2"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
SQ SEQUENCE 286 AA; 30590 MW; 63B81E4509E360B1 CRC64;
MTKEVVGDKR SFSGKDYQDP PPEPLFDATE LGKWSFYRAL IAEFIATLLF LYVTIMTVIG
YKSQTDPALN PDQCTGVGVL GIAWAFGGMI FILVYCTAGI SGGHINPAVT FGLLLARKVT
LVRAVMYMVA QCLGAICGVA LVKAFQSAYF TRYGGGANGL SDGYSIGTGV AAEIIGTFVL
VYTVFSATDP KRSARDSHVP VLAPLPIGFA VFIVHLATIP ITGTGINPAR SLGAAIIYNK
DKAWDHHWIF WVGPFAGAAI AAFYHQFVLR AGAIKALGSF RSQPHV
