ID NIP42_ARATH Reviewed; 283 AA.
AC Q8W036; Q9FIZ8;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Probable aquaporin NIP4-2;
DE AltName: Full=NOD26-like intrinsic protein 4-2;
DE Short=AtNIP4;2;
DE AltName: Full=Nodulin-26-like major intrinsic protein 5;
DE Short=NodLikeMip5;
DE Short=Protein NLM5;
GN Name=NIP4-2; Synonyms=NLM5; OrderedLocusNames=At5g37820;
GN ORFNames=K22F20.60;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 [MRNA] OF 100-261.
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 [4]
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).
CC -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC neutral solutes across cell membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AB016873; BAB10361.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94236.1; -; Genomic_DNA.
DR EMBL; AJ276476; CAC81708.1; -; mRNA.
DR RefSeq; NP_198598.1; NM_123141.2.
DR AlphaFoldDB; Q8W036; -.
DR SMR; Q8W036; -.
DR STRING; 3702.Q8W036; -.
DR iPTMnet; Q8W036; -.
DR PaxDb; 3702-AT5G37820-1; -.
DR ProteomicsDB; 251154; -.
DR EnsemblPlants; AT5G37820.1; AT5G37820.1; AT5G37820.
DR GeneID; 833760; -.
DR Gramene; AT5G37820.1; AT5G37820.1; AT5G37820.
DR KEGG; ath:AT5G37820; -.
DR Araport; AT5G37820; -.
DR TAIR; AT5G37820; NIP4.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_1_1; -.
DR InParanoid; Q8W036; -.
DR OMA; ITFAVFR; -.
DR PhylomeDB; Q8W036; -.
DR PRO; PR:Q8W036; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W036; baseline and differential.
DR Genevisible; Q8W036; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR NCBIfam; TIGR00861; MIP; 1.
DR PANTHER; PTHR45724; AQUAPORIN NIP2-1; 1.
DR PANTHER; PTHR45724:SF59; AQUAPORIN NIP4-2-RELATED; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..283
FT /note="Probable aquaporin NIP4-2"
FT /id="PRO_0000064067"
FT TRANSMEM 51..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 102..104
FT /note="NPA 1"
FT MOTIF 214..216
FT /note="NPA 2"
FT COMPBIAS 1..18
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 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
SQ SEQUENCE 283 AA; 30277 MW; 2C70900EBCC2AB3A CRC64;
MTSHGEEIED EQISRIEKGN CKDSQGGMET AICSSPSIVC LTQKLIAEMI GTYFIIFSGC
GVVVVNVLYG GTITFPGICV TWGLIVMVMI YSTGHISGAH FNPAVTVTFA VFRRFPWYQV
PLYIGAQLTG SLLASLTLRL MFNVTPKAFF GTTPTDSSGQ ALVAEIIISF LLMFVISGVA
TDSRATGELA GIAVGMTIIL NVFVAGPISG ASMNPARSLG PAIVMGRYKG IWVYIVGPFV
GIFAGGFVYN FMRFTDKPLR ELTKSASFLR SVAQKDNASK SDG
//
