PIP21_MAIZE
ID PIP21_MAIZE Reviewed; 290 AA.
AC Q84RL7; Q9ATM9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Aquaporin PIP2-1;
DE AltName: Full=Plasma membrane intrinsic protein 2-1;
DE AltName: Full=ZmPIP2-1;
DE AltName: Full=ZmPIP2;1;
GN Name=PIP2-1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. B73;
RX PubMed=11244102; DOI=10.1104/pp.125.3.1206;
RA Chaumont F., Barrieu F., Wojcik E., Chrispeels M.J., Jung R.;
RT "Aquaporins constitute a large and highly divergent protein family in
RT maize.";
RL Plant Physiol. 125:1206-1215(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Root;
RX PubMed=14701934; DOI=10.1093/pcp/pcg168;
RA Lopez F., Bousser A., Sissoeff I., Gaspar M., Lachaise B., Hoarau J.,
RA Mahe A.;
RT "Diurnal regulation of water transport and aquaporin gene expression in
RT maize roots: contribution of PIP2 proteins.";
RL Plant Cell Physiol. 44:1384-1395(2003).
RN [3]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH PIP1-2.
RX PubMed=14671024; DOI=10.1105/tpc.017194;
RA Fetter K., van Wilder V., Moshelion M., Chaumont F.;
RT "Interactions between plasma membrane aquaporins modulate their water
RT channel activity.";
RL Plant Cell 16:215-228(2004).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane. Active as homomers. Increased activity when
CC heteromerization with PIP1-2. {ECO:0000269|PubMed:14671024}.
CC -!- SUBUNIT: Homomers. Can interact with PIP1-2 to form heteromers.
CC {ECO:0000269|PubMed:14671024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:14701934}.
CC -!- INDUCTION: Expressed in roots with a circadian rhythm showing an
CC increase at the end of the night period, a peak during the first part
CC of the light period and then a decrease. {ECO:0000269|PubMed:14701934}.
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. PIP (TC
CC 1.A.8.11) subfamily. {ECO:0000305}.
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DR EMBL; AF326491; AAK26758.1; -; mRNA.
DR EMBL; AY243801; AAO86707.1; -; mRNA.
DR RefSeq; NP_001105024.1; NM_001111554.2.
DR AlphaFoldDB; Q84RL7; -.
DR SMR; Q84RL7; -.
DR ProMEX; Q84RL7; -.
DR EnsemblPlants; Zm00001eb306380_T001; Zm00001eb306380_P001; Zm00001eb306380.
DR GeneID; 541888; -.
DR Gramene; Zm00001eb306380_T001; Zm00001eb306380_P001; Zm00001eb306380.
DR KEGG; zma:541888; -.
DR HOGENOM; CLU_020019_3_0_1; -.
DR OMA; FNNKKAW; -.
DR OrthoDB; 1152704at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; Q84RL7; baseline and differential.
DR Genevisible; Q84RL7; ZM.
DR GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; TAS:AgBase.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR GO; GO:0051290; P:protein heterotetramerization; TAS:AgBase.
DR GO; GO:0051289; P:protein homotetramerization; TAS:AgBase.
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; PTHR45687; PTHR45687; 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 Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..290
FT /note="Aquaporin PIP2-1"
FT /id="PRO_0000286018"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 112..114
FT /note="NPA 1"
FT /evidence="ECO:0000250"
FT MOTIF 233..235
FT /note="NPA 2"
FT /evidence="ECO:0000250"
FT CONFLICT 176
FT /note="L -> F (in Ref. 2; AAO86707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 30215 MW; 57EB0A9C6ADEF035 CRC64;
MGKDDVIESG AGGGEFAAKD YTDPPPAPLI DAAELGSWSL YRAVIAEFIA TLLFLYITVA
TVIGYKHQTD ASASGADAAC GGVGVLGIAW AFGGMIFVLV YCTAGISGGH INPAVTFGLF
LARKVSLVRA LLYIVAQCLG AICGVGLVKA FQSAYFDRYG GGANSLASGY SRGTGLGAEI
IGTFVLVYTV FSATDPKRNA RDSHVPVLAP LPIGFAVFMV HLATIPVTGT GINPARSLGA
AVIYNKDKPW DDHWIFWVGP LVGAAIAAFY HQYILRAGAI KALGSFRSNA
