NIP51_ARATH
ID NIP51_ARATH Reviewed; 304 AA.
AC Q9SV84;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable aquaporin NIP5-1;
DE AltName: Full=NOD26-like intrinsic protein 5-1;
DE Short=AtNIP5;1;
DE AltName: Full=Nodulin-26-like major intrinsic protein 6;
DE Short=NodLikeMip6;
DE Short=Protein NLM6;
GN Name=NIP5-1; Synonyms=NLM6; OrderedLocusNames=At4g10380;
GN ORFNames=F24G24.180;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16679457; DOI=10.1105/tpc.106.041640;
RA Takano J., Wada M., Ludewig U., Schaaf G., von Wiren N., Fujiwara T.;
RT "The Arabidopsis major intrinsic protein NIP5;1 is essential for efficient
RT boron uptake and plant development under boron limitation.";
RL Plant Cell 18:1498-1509(2006).
CC -!- FUNCTION: Boric acid transporter. Low water transport activity. Plays
CC an important role as plasma membrane boric acid channel for the boron
CC uptake required for plant growth and development under boron
CC limitation. {ECO:0000269|PubMed:16679457}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16679457};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16679457}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves.
CC {ECO:0000269|PubMed:11806824}.
CC -!- INDUCTION: By boron limitation in the root elongation and the root hair
CC zones. {ECO:0000269|PubMed:16679457}.
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/Ser/Val (NPA).
CC -!- DISRUPTION PHENOTYPE: Plants display lower boric acid uptake into
CC roots, lower biomass production, and increased sensitivity of root and
CC shoot development to boron deficiency. {ECO:0000269|PubMed:16679457}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. NIP (TC
CC 1.A.8.12) subfamily. {ECO:0000305}.
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DR EMBL; AL049488; CAB39791.1; -; Genomic_DNA.
DR EMBL; AL161517; CAB78161.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82874.1; -; Genomic_DNA.
DR EMBL; AY087560; AAM65102.1; -; mRNA.
DR PIR; T04053; T04053.
DR RefSeq; NP_192776.1; NM_117106.3.
DR AlphaFoldDB; Q9SV84; -.
DR SMR; Q9SV84; -.
DR STRING; 3702.AT4G10380.1; -.
DR TCDB; 1.A.8.12.3; the major intrinsic protein (mip) family.
DR PaxDb; Q9SV84; -.
DR PRIDE; Q9SV84; -.
DR ProteomicsDB; 249443; -.
DR EnsemblPlants; AT4G10380.1; AT4G10380.1; AT4G10380.
DR GeneID; 826630; -.
DR Gramene; AT4G10380.1; AT4G10380.1; AT4G10380.
DR KEGG; ath:AT4G10380; -.
DR Araport; AT4G10380; -.
DR TAIR; locus:2122829; AT4G10380.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_1_1; -.
DR InParanoid; Q9SV84; -.
DR OMA; ASQSNCW; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q9SV84; -.
DR PRO; PR:Q9SV84; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV84; baseline and differential.
DR Genevisible; Q9SV84; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0046715; F:active borate transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015105; F:arsenite transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR GO; GO:0015700; P:arsenite transport; IDA:TAIR.
DR GO; GO:0046713; P:borate transport; IDA:TAIR.
DR GO; GO:0080029; P:cellular response to boron-containing substance levels; IEP:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
DR GO; GO:0010036; P:response to boron-containing substance; IMP:TAIR.
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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..304
FT /note="Probable aquaporin NIP5-1"
FT /id="PRO_0000064068"
FT TRANSMEM 80..100
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 137..139
FT /note="NPA 1"
FT MOTIF 248..250
FT /note="NPA 2"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
SQ SEQUENCE 304 AA; 31493 MW; 0B7D0C626F723337 CRC64;
MAPPEAEVGA VMVMAPPTPG TPGTPGGPLI TGMRVDSMSF DHRKPTPRCK CLPVMGSTWG
QHDTCFTDFP SPDVSLTRKL GAEFVGTFIL IFTATAGPIV NQKYDGAETL IGNAACAGLA
VMIIILSTGH ISGAHLNPSL TIAFAALRHF PWAHVPAYIA AQVSASICAS FALKGVFHPF
MSGGVTIPSV SLGQAFALEF IITFILLFVV TAVATDTRAV GELAGIAVGA TVMLNILVAG
PSTGGSMNPV RTLGPAVASG NYRSLWVYLV APTLGAISGA AVYTGVKLND SVTDPPRPVR
SFRR
