ID   NIP41_ARATH             Reviewed;         283 AA.
AC   Q9FIZ9;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Putative aquaporin NIP4-1;
DE   AltName: Full=NOD26-like intrinsic protein 4-1;
DE            Short=AtNIP4;1;
GN   Name=NIP4-1; OrderedLocusNames=At5g37810; ORFNames=K22F20.50;
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   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: Potential aquaporin, which may facilitate the transport of
CC       water and small 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; BAB10360.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94235.1; -; Genomic_DNA.
DR   RefSeq; NP_198597.1; NM_123140.2.
DR   AlphaFoldDB; Q9FIZ9; -.
DR   SMR; Q9FIZ9; -.
DR   BioGRID; 19010; 17.
DR   IntAct; Q9FIZ9; 17.
DR   STRING; 3702.AT5G37810.1; -.
DR   iPTMnet; Q9FIZ9; -.
DR   PaxDb; Q9FIZ9; -.
DR   PRIDE; Q9FIZ9; -.
DR   ProteomicsDB; 251153; -.
DR   EnsemblPlants; AT5G37810.1; AT5G37810.1; AT5G37810.
DR   GeneID; 833759; -.
DR   Gramene; AT5G37810.1; AT5G37810.1; AT5G37810.
DR   KEGG; ath:AT5G37810; -.
DR   Araport; AT5G37810; -.
DR   TAIR; locus:2156020; AT5G37810.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_1_1; -.
DR   InParanoid; Q9FIZ9; -.
DR   OMA; RADNICA; -.
DR   OrthoDB; 1152704at2759; -.
DR   PhylomeDB; Q9FIZ9; -.
DR   PRO; PR:Q9FIZ9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIZ9; baseline.
DR   Genevisible; Q9FIZ9; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Acetylation; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..283
FT                   /note="Putative aquaporin NIP4-1"
FT                   /id="PRO_0000064066"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
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   MOTIF           102..104
FT                   /note="NPA 1"
FT   MOTIF           214..216
FT                   /note="NPA 2"
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;  30217 MW;  690AEAA1D711E189 CRC64;
     MSSHSDEIEE EQISRIEKGK GKDCQGGIET VICTSPSIVC LTQKLIAEMI GTYFIVFSGC
     GVVVVNVLYG GTITFPGICV TWGLIVMVMI YSTGHISGAH FNPAVTVTFA IFRRFPWHQV
     PLYIGAQFAG SLLASLTLRL MFKVTPEAFF GTTPADSPAR ALVAEIIISF LLMFVISGVA
     TDNRAVGELA GIAVGMTIMV NVFVAGPISG ASMNPARSLG PALVMGVYKH IWVYIVGPVL
     GVISGGFVYN LIRFTDKPLR ELTKSASFLR AVSPSHKGSS SKT