NIP21_ARATH
ID NIP21_ARATH Reviewed; 288 AA.
AC Q8W037; O64706; Q1ECK8;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Aquaporin NIP2-1;
DE AltName: Full=NOD26-like intrinsic protein 2-1;
DE Short=AtNIP2;1;
DE AltName: Full=Nodulin-26-like major intrinsic protein 4;
DE Short=NodLikeMip4;
DE Short=Protein NLM4;
GN Name=NIP2-1; Synonyms=NLM4; OrderedLocusNames=At2g34390;
GN ORFNames=T31E10.27;
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].
RA Weig A.R., Jakob C.U.;
RT "Functional characterisation of Arabidopsis thaliana aquaglyceroporins.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION.
RA Weig A.R.;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16954136; DOI=10.1093/pcp/pcl004;
RA Mizutani M., Watanabe S., Nakagawa T., Maeshima M.;
RT "Aquaporin NIP2;1 is mainly localized to the ER membrane and shows root-
RT specific accumulation in Arabidopsis thaliana.";
RL Plant Cell Physiol. 47:1420-1426(2006).
CC -!- FUNCTION: Low water transport activity in yeast cells.
CC {ECO:0000269|PubMed:16954136}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16954136}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16954136}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots with high
CC expression in root elongation zone and root stele.
CC {ECO:0000269|PubMed:16954136}.
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}.
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DR EMBL; AJ276475; CAC81707.2; -; mRNA.
DR EMBL; AC004077; AAC26712.1; -; Genomic_DNA.
DR EMBL; AC004481; AAM14952.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08967.1; -; Genomic_DNA.
DR EMBL; BT025726; ABF82629.1; -; mRNA.
DR PIR; T02327; T02327.
DR RefSeq; NP_180986.1; NM_128991.5.
DR AlphaFoldDB; Q8W037; -.
DR SMR; Q8W037; -.
DR BioGRID; 3349; 24.
DR IntAct; Q8W037; 24.
DR STRING; 3702.AT2G34390.1; -.
DR TCDB; 1.A.8.12.4; the major intrinsic protein (mip) family.
DR PaxDb; Q8W037; -.
DR EnsemblPlants; AT2G34390.1; AT2G34390.1; AT2G34390.
DR GeneID; 818002; -.
DR Gramene; AT2G34390.1; AT2G34390.1; AT2G34390.
DR KEGG; ath:AT2G34390; -.
DR Araport; AT2G34390; -.
DR TAIR; locus:2040904; AT2G34390.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_1_1; -.
DR InParanoid; Q8W037; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q8W037; -.
DR PRO; PR:Q8W037; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8W037; baseline and differential.
DR Genevisible; Q8W037; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015727; P:lactate transport; IDA:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IDA: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 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..288
FT /note="Aquaporin NIP2-1"
FT /id="PRO_0000064064"
FT TRANSMEM 50..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 106..108
FT /note="NPA 1"
FT MOTIF 225..227
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61837"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
SQ SEQUENCE 288 AA; 30581 MW; 909D0990C3CFE785 CRC64;
MDDISVSKSN HGNVVVLNIK ASSLADTSLP SNKHESSSPP LLSVHFLQKL LAELVGTYYL
IFAGCAAIAV NAQHNHVVTL VGIAVVWGIV IMVLVYCLGH LSAHFNPAVT LALASSQRFP
LNQVPAYITV QVIGSTLASA TLRLLFDLNN DVCSKKHDVF LGSSPSGSDL QAFVMEFIIT
GFLMLVVCAV TTTKRTTEEL EGLIIGATVT LNVIFAGEVS GASMNPARSI GPALVWGCYK
GIWIYLLAPT LGAVSGALIH KMLPSIQNAE PEFSKTGSSH KRVTDLPL
