NIP11_ARATH
ID NIP11_ARATH Reviewed; 296 AA.
AC Q8VZW1; O48595; O49416;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Aquaporin NIP1-1;
DE AltName: Full=NOD26-like intrinsic protein 1-1;
DE Short=AtNIP1;1;
DE AltName: Full=Nodulin-26-like major intrinsic protein 1;
DE Short=NodLikeMip1;
DE Short=Protein NLM1;
GN Name=NIP1-1; Synonyms=NLM1; OrderedLocusNames=At4g19030;
GN ORFNames=F13C5.200;
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 [MRNA].
RX PubMed=9276952; DOI=10.1104/pp.114.4.1347;
RA Weig A.R., Deswarte C., Chrispeels M.J.;
RT "The major intrinsic protein family of Arabidopsis has 23 members that form
RT three distinct groups with functional aquaporins in each group.";
RL Plant Physiol. 114:1347-1357(1997).
RN [2]
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 [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].
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 [6]
RP FUNCTION.
RX PubMed=11007982; DOI=10.1016/s0014-5793(00)02027-5;
RA Weig A.R., Jakob C.U.;
RT "Functional identification of the glycerol permease activity of Arabidopsis
RT thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 481:293-298(2000).
RN [7]
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: Water channel probably required to promote glycerol
CC permeability and water transport across cell membranes.
CC {ECO:0000269|PubMed:11007982}.
CC -!- INTERACTION:
CC Q8VZW1; Q9FZ98: At1g28250/F3H9_23; NbExp=3; IntAct=EBI-4424378, EBI-4425682;
CC Q8VZW1; Q9LPF1: At1g44800; NbExp=2; IntAct=EBI-4424378, EBI-4466346;
CC Q8VZW1; Q94AJ5: At1g80170; NbExp=2; IntAct=EBI-4424378, EBI-4457426;
CC Q8VZW1; Q9LDU6: DWF5; NbExp=2; IntAct=EBI-4424378, EBI-4439540;
CC Q8VZW1; P27202: PSBR; NbExp=2; IntAct=EBI-4424378, EBI-4461393;
CC Q8VZW1; Q9FFK1: SYP31; NbExp=2; IntAct=EBI-4424378, EBI-4434817;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {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/Gly (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. NIP (TC
CC 1.A.8.12) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16760.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA68906.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB78905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y07625; CAA68906.1; ALT_INIT; mRNA.
DR EMBL; AL021711; CAA16760.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161550; CAB78905.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84127.1; -; Genomic_DNA.
DR EMBL; AY063796; AAL36152.1; -; mRNA.
DR EMBL; AY117197; AAM51272.1; -; mRNA.
DR EMBL; AY084497; AAM61066.1; -; mRNA.
DR PIR; H85214; H85214.
DR PIR; T05040; T05040.
DR RefSeq; NP_567572.1; NM_118021.4.
DR AlphaFoldDB; Q8VZW1; -.
DR SMR; Q8VZW1; -.
DR BioGRID; 12934; 184.
DR IntAct; Q8VZW1; 184.
DR STRING; 3702.AT4G19030.1; -.
DR TCDB; 1.A.8.12.8; the major intrinsic protein (mip) family.
DR PaxDb; Q8VZW1; -.
DR PRIDE; Q8VZW1; -.
DR ProteomicsDB; 236827; -.
DR EnsemblPlants; AT4G19030.1; AT4G19030.1; AT4G19030.
DR GeneID; 827641; -.
DR Gramene; AT4G19030.1; AT4G19030.1; AT4G19030.
DR KEGG; ath:AT4G19030; -.
DR Araport; AT4G19030; -.
DR TAIR; locus:2117119; AT4G19030.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_1_1; -.
DR InParanoid; Q8VZW1; -.
DR OMA; KHDQFSG; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q8VZW1; -.
DR BioCyc; MetaCyc:MON-21673; -.
DR PRO; PR:Q8VZW1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VZW1; baseline and differential.
DR Genevisible; Q8VZW1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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:0080170; P:hydrogen peroxide transmembrane transport; IDA:TAIR.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; 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; PTHR45724; PTHR45724; 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; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..296
FT /note="Aquaporin NIP1-1"
FT /id="PRO_0000064062"
FT TRANSMEM 57..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 114..116
FT /note="NPA 1"
FT MOTIF 233..235
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
SQ SEQUENCE 296 AA; 31715 MW; 4D66695D9E879C68 CRC64;
MADISGNGYG NAREEVVMVN LKDEVEHQQE MEDIHNPRPL KKQDSLLSVS VPFLQKLIAE
FLGTYFLVFT GCASVVVNMQ NDNVVTLPGI AIVWGLTIMV LIYSLGHISG AHINPAVTIA
FASCGRFPLK QVPAYVISQV IGSTLAAATL RLLFGLDHDV CSGKHDVFIG SSPVGSDLQA
FTMEFIVTFY LMFIISGVAT DNRAIGELAG LAIGSTVLLN VLIAAPVSSA SMNPGRSLGP
ALVYGCYKGI WIYLVAPTLG AIAGAWVYNT VRYTDKPLRE ITKSGSFLKT VRIGST
