ID   PIP24_MAIZE             Reviewed;         288 AA.
AC   Q9ATM6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Aquaporin PIP2-4;
DE   AltName: Full=Plasma membrane intrinsic protein 2-4;
DE   AltName: Full=ZmPIP2-4;
DE   AltName: Full=ZmPIP2;4;
GN   Name=PIP2-4;
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   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   [3]
RP   FUNCTION, AND SUBUNIT.
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. May 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 the root growing zone at 5-6 mm from
CC       the root tip. {ECO:0000269|PubMed:12355166}.
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; AF326494; AAK26761.1; -; mRNA.
DR   RefSeq; NP_001105026.1; NM_001111556.1.
DR   AlphaFoldDB; Q9ATM6; -.
DR   SMR; Q9ATM6; -.
DR   STRING; 4577.GRMZM2G154628_P01; -.
DR   PaxDb; Q9ATM6; -.
DR   PRIDE; Q9ATM6; -.
DR   ProMEX; Q9ATM6; -.
DR   EnsemblPlants; Zm00001eb247760_T001; Zm00001eb247760_P001; Zm00001eb247760.
DR   GeneID; 541890; -.
DR   Gramene; Zm00001eb247760_T001; Zm00001eb247760_P001; Zm00001eb247760.
DR   KEGG; zma:541890; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_0_1; -.
DR   OMA; IVYGVKP; -.
DR   OrthoDB; 1152704at2759; -.
DR   Proteomes; UP000007305; Chromosome 5.
DR   ExpressionAtlas; Q9ATM6; baseline and differential.
DR   Genevisible; Q9ATM6; ZM.
DR   GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015250; F:water channel activity; IBA:GO_Central.
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..288
FT                   /note="Aquaporin PIP2-4"
FT                   /id="PRO_0000286021"
FT   TRANSMEM        42..62
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           111..113
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           232..234
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   288 AA;  30322 MW;  2A6D191B34E757C1 CRC64;
     MAKDIEASGP EAGEFSAKDY TDPPPAPLID AEELTQWSLY RAVIAEFIAT LLFLYITVAT
     VIGYKHQTDA SASGPDAACG GVGILGIAWA FGGMIFILVY CTAGISGGHI NPAVTFGLFL
     ARKVSLVRAL LYIIAQCLGA ICGVGLVKGF QSAYYVRYGG GANELSDGYS KGTGLAAEII
     GTFVLVYTVF SATDPKRSAR DSHVPVLAPL PIGFAVFMVH LATIPITGTG INPARSLGAA
     VIYNKDKAWD DQWIFWVGPL IGAAIAAAYH QYVLRASATK LGSYRSNA