NIP21_ORYSJ
ID NIP21_ORYSJ Reviewed; 298 AA.
AC Q6Z2T3; B7EGY5; Q0DXL6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Aquaporin NIP2-1 {ECO:0000305};
DE AltName: Full=Low silicon protein 1 {ECO:0000303|PubMed:16572174};
DE AltName: Full=NOD26-like intrinsic protein 2-1 {ECO:0000303|PubMed:16033806};
DE AltName: Full=OsNIP2;1 {ECO:0000303|PubMed:16033806};
DE AltName: Full=Silicon influx transporter LSI1 {ECO:0000303|PubMed:17625566};
GN Name=NIP2-1 {ECO:0000303|PubMed:16033806};
GN Synonyms=LSI1 {ECO:0000303|PubMed:16572174},
GN SIIT1 {ECO:0000303|PubMed:17625566};
GN OrderedLocusNames=Os02g0745100 {ECO:0000312|EMBL:BAS80898.1},
GN LOC_Os02g51110 {ECO:0000305};
GN ORFNames=OJ1118_G04.16 {ECO:0000312|EMBL:BAD15544.1},
GN OJ1734_E02.43 {ECO:0000312|EMBL:BAD16128.1},
GN OsJ_008085 {ECO:0000312|EMBL:EAZ24602.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND MUTAGENESIS OF ALA-132.
RX PubMed=16572174; DOI=10.1038/nature04590;
RA Ma J.F., Tamai K., Yamaji N., Mitani N., Konishi S., Katsuhara M.,
RA Ishiguro M., Murata Y., Yano M.;
RT "A silicon transporter in rice.";
RL Nature 440:688-691(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sahebi M., Hanafi M.M., Azizi P., Abiri R., Taheri S.;
RT "Oryza sativa NOD26 major intrinsic protein (Lsi1) mRNA.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=16033806; DOI=10.1093/pcp/pci172;
RA Sakurai J., Ishikawa F., Yamaguchi T., Uemura M., Maeshima M.;
RT "Identification of 33 rice aquaporin genes and analysis of their expression
RT and function.";
RL Plant Cell Physiol. 46:1568-1577(2005).
RN [9]
RP FUNCTION.
RX PubMed=17625566; DOI=10.1038/nature05964;
RA Ma J.F., Yamaji N., Mitani N., Tamai K., Konishi S., Fujiwara T.,
RA Katsuhara M., Yano M.;
RT "An efflux transporter of silicon in rice.";
RL Nature 448:209-212(2007).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=17905867; DOI=10.1104/pp.107.107599;
RA Ma J.F., Yamaji N., Tamai K., Mitani N.;
RT "Genotypic difference in silicon uptake and expression of silicon
RT transporter genes in rice.";
RL Plant Physiol. 145:919-924(2007).
RN [11]
RP FUNCTION.
RX PubMed=18626020; DOI=10.1073/pnas.0802361105;
RA Ma J.F., Yamaji N., Mitani N., Xu X.Y., Su Y.H., McGrath S.P., Zhao F.J.;
RT "Transporters of arsenite in rice and their role in arsenic accumulation in
RT rice grain.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9931-9935(2008).
RN [12]
RP FUNCTION.
RX PubMed=19542298; DOI=10.1104/pp.109.140350;
RA Li R.Y., Ago Y., Liu W.J., Mitani N., Feldmann J., McGrath S.P., Ma J.F.,
RA Zhao F.J.;
RT "The rice aquaporin Lsi1 mediates uptake of methylated arsenic species.";
RL Plant Physiol. 150:2071-2080(2009).
CC -!- FUNCTION: Silicon influx transporter responsible for silicon transport
CC from the external solution to the root cells (PubMed:16572174). Is
CC coupled with the silicon efflux transporter LSI2 in both exodermal and
CC endodermal root cells for an efficient silicon transport across the
CC cells into the stele (PubMed:17625566). Silicon is beneficial to plant
CC growth and helps plants to overcome abiotic and biotic stresses by
CC preventing lodging (falling over) and increasing resistance to pests
CC and diseases, as well as other stresses (PubMed:16572174). Is coupled
CC with LSI2 transporter in roots for efficient uptake of arsenite, which
CC is further dispatched in shoots and grains (PubMed:18626020). Mediates
CC uptake of methylated arsenic species in roots (PubMed:19542298).
CC {ECO:0000269|PubMed:16572174, ECO:0000269|PubMed:17625566,
CC ECO:0000269|PubMed:18626020, ECO:0000269|PubMed:19542298}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16572174};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16572174}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the roots (PubMed:16033806,
CC PubMed:16572174, PubMed:17905867). In roots, it localizes in the main
CC and lateral roots, but not in root hairs (PubMed:16572174). Within a
CC root, it localizes on the plasma membrane of the distal side of both
CC exodermis and endodermis, where casparian strips exist (at protein
CC level) (PubMed:16572174, PubMed:17905867). Expressed low levels in
CC leaves and anthers (PubMed:16033806). {ECO:0000269|PubMed:16033806,
CC ECO:0000269|PubMed:16572174, ECO:0000269|PubMed:17905867}.
CC -!- INDUCTION: Regulated by silicon level; the expression being decreased
CC 4-fold by continuous silicon supply for 3 days.
CC {ECO:0000269|PubMed:16572174}.
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. NIP (TC
CC 1.A.8.12) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB222272; BAE92561.1; -; mRNA.
DR EMBL; KT284741; ALS20398.1; -; mRNA.
DR EMBL; KT284742; ALS20399.1; -; mRNA.
DR EMBL; AP004114; BAD15544.1; -; Genomic_DNA.
DR EMBL; AP005297; BAD16128.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF10022.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80898.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ24602.1; -; Genomic_DNA.
DR EMBL; AK069842; BAG91632.1; -; mRNA.
DR RefSeq; XP_015626173.1; XM_015770687.1.
DR PDB; 7CJS; X-ray; 1.80 A; A/B/C/D/E/F/G/H=47-298.
DR PDB; 7NL4; X-ray; 3.00 A; A/B/C/D/E/F/G/H=38-264.
DR PDBsum; 7CJS; -.
DR PDBsum; 7NL4; -.
DR AlphaFoldDB; Q6Z2T3; -.
DR SMR; Q6Z2T3; -.
DR STRING; 4530.OS02T0745100-01; -.
DR TCDB; 1.A.8.12.2; the major intrinsic protein (mip) family.
DR PaxDb; Q6Z2T3; -.
DR PRIDE; Q6Z2T3; -.
DR EnsemblPlants; Os02t0745100-01; Os02t0745100-01; Os02g0745100.
DR GeneID; 4330713; -.
DR Gramene; Os02t0745100-01; Os02t0745100-01; Os02g0745100.
DR KEGG; osa:4330713; -.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_1_1; -.
DR InParanoid; Q6Z2T3; -.
DR OMA; IRAIAYF; -.
DR OrthoDB; 1152704at2759; -.
DR BioCyc; MetaCyc:MON-21679; -.
DR PlantReactome; R-OSA-9618218; Arsenic uptake and detoxification.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6Z2T3; OS.
DR GO; GO:0048226; C:Casparian strip; IDA:Gramene.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:Gramene.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0015115; F:silicate transmembrane transporter activity; IDA:Gramene.
DR GO; GO:0015708; P:silicic acid import across plasma membrane; IMP:Gramene.
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; PTHR45724; PTHR45724; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Aquaporin NIP2-1"
FT /id="PRO_0000235239"
FT TRANSMEM 51..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 108..110
FT /note="NPA 1"
FT MOTIF 219..221
FT /note="NPA 2"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 132
FT /note="A->T: In lsi; impairs silicon uptake. Grain
FT discoloration. Reduces grain yield 10-fold."
FT /evidence="ECO:0000269|PubMed:16572174"
FT HELIX 47..74
FT /evidence="ECO:0007829|PDB:7CJS"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:7CJS"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 126..147
FT /evidence="ECO:0007829|PDB:7CJS"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 163..186
FT /evidence="ECO:0007829|PDB:7CJS"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:7NL4"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:7CJS"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:7CJS"
FT HELIX 238..257
FT /evidence="ECO:0007829|PDB:7CJS"
SQ SEQUENCE 298 AA; 31978 MW; 4C2E2C3C48580959 CRC64;
MASNNSRTNS RANYSNEIHD LSTVQNGTMP TMYYGEKAIA DFFPPHLLKK VVSEVVATFL
LVFMTCGAAG ISGSDLSRIS QLGQSIAGGL IVTVMIYAVG HISGAHMNPA VTLAFAVFRH
FPWIQVPFYW AAQFTGAICA SFVLKAVIHP VDVIGTTTPV GPHWHSLVVE VIVTFNMMFV
TLAVATDTRA VGELAGLAVG SAVCITSIFA GAISGGSMNP ARTLGPALAS NKFDGLWIYF
LGPVMGTLSG AWTYTFIRFE DTPKEGSSQK LSSFKLRRLR SQQSIAADDV DEMENIQV
