PIP12_MAIZE
ID PIP12_MAIZE Reviewed; 289 AA.
AC Q9XF59;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Aquaporin PIP1-2;
DE AltName: Full=Plasma membrane intrinsic protein 1-2;
DE AltName: Full=ZmPIP1-2;
DE AltName: Full=ZmPIP1;2;
DE AltName: Full=ZmPIP1b;
GN Name=PIP1-2;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Ohio 43; TISSUE=Seed;
RX PubMed=10759498; DOI=10.1104/pp.122.4.1025;
RA Chaumont F., Barrieu F., Jung R., Chrispeels M.J.;
RT "Plasma membrane intrinsic proteins from maize cluster in two sequence
RT subgroups with differential aquaporin activity.";
RL Plant Physiol. 122:1025-1034(2000).
RN [2]
RP GENE FAMILY, AND NOMENCLATURE.
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12355166; DOI=10.1007/s00425-002-0841-2;
RA Hukin D., Doering-Saad C., Thomas C.R., Pritchard J.;
RT "Sensitivity of cell hydraulic conductivity to mercury is coincident with
RT symplasmic isolation and expression of plasmalemma aquaporin genes in
RT growing maize roots.";
RL Planta 215:1047-1056(2002).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH PIP2-1.
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 heteromers with PIP1-1, PIP2-1, PIP2-4
CC or PIP2-5, but not as homomers. {ECO:0000269|PubMed:14671024}.
CC -!- SUBUNIT: Interacts with PIP2-1 to form heteromers.
CC {ECO:0000269|PubMed:14671024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10759498,
CC ECO:0000269|PubMed:14671024}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10759498, ECO:0000269|PubMed:14671024}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing tassels and at lower
CC levels in roots, shoots, ears and embryos. Expressed in the root
CC growing zone at 5-6 mm from the root tip. Expressed in xylem
CC parenchyma. {ECO:0000269|PubMed:10759498, ECO:0000269|PubMed:12355166,
CC ECO:0000269|PubMed:14671024}.
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; AF131201; AAD29676.1; -; mRNA.
DR RefSeq; NP_001104934.1; NM_001111464.1.
DR AlphaFoldDB; Q9XF59; -.
DR SMR; Q9XF59; -.
DR STRING; 4577.AC209208.3_FGP002; -.
DR PaxDb; Q9XF59; -.
DR PRIDE; Q9XF59; -.
DR GeneID; 541779; -.
DR KEGG; zma:541779; -.
DR eggNOG; KOG0223; Eukaryota.
DR OrthoDB; 1152704at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9XF59; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IPI: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..289
FT /note="Aquaporin PIP1-2"
FT /id="PRO_0000286014"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..119
FT /note="NPA 1"
FT /evidence="ECO:0000250"
FT MOTIF 238..240
FT /note="NPA 2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 289 AA; 30796 MW; 94B15361FA34266E CRC64;
MEGKEEDVRL GANKFSERQP IGTAAQGAAD DKDYKEPPPA PLFEPGELKS WSFYRAGIAE
FVATFLFLYI TILTVMGVSK STSKCATVGI QGIAWSFGGM IFALVYCTAG ISGGHINPAV
TFGLFLARKL SLTRALFYII MQCLGAVCGA GVVKGFQQGL YMGNGGGANV VAPGYTKGDG
LGAEIVGTFI LVYTVFSATD AKRNARDSHV PILAPLPIGF AVFLVHLATI PITGTGINPA
RSLGAAIIYN RDHAWNDHWI FWVGPFIGAA LAAIYHQVII RAIPFKSRS
