ID   PIP13_MAIZE             Reviewed;         292 AA.
AC   Q9AQU5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Aquaporin PIP1-3/PIP1-4;
DE   AltName: Full=Plasma membrane intrinsic protein 1-3;
DE   AltName: Full=Plasma membrane intrinsic protein 1-4;
DE   AltName: Full=ZmPIP1-3;
DE   AltName: Full=ZmPIP1-4;
DE   AltName: Full=ZmPIP1;3;
DE   AltName: Full=ZmPIP1;4;
GN   Name=PIP1-3;
GN   and
GN   Name=PIP1-4;
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).
CC   -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC       neutral solutes across cell membranes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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; AF326487; AAK26754.1; -; mRNA.
DR   EMBL; AF326488; AAK26755.1; -; mRNA.
DR   RefSeq; NP_001105022.1; NM_001111552.1.
DR   AlphaFoldDB; Q9AQU5; -.
DR   SMR; Q9AQU5; -.
DR   STRING; 4577.GRMZM2G392975_P01; -.
DR   PaxDb; Q9AQU5; -.
DR   PRIDE; Q9AQU5; -.
DR   ProMEX; Q9AQU5; -.
DR   EnsemblPlants; Zm00001eb186900_T001; Zm00001eb186900_P001; Zm00001eb186900.
DR   GeneID; 541886; -.
DR   Gramene; Zm00001eb186900_T001; Zm00001eb186900_P001; Zm00001eb186900.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_0_1; -.
DR   OMA; YEFTGAS; -.
DR   OrthoDB; 1152704at2759; -.
DR   Proteomes; UP000007305; Chromosome 4.
DR   ExpressionAtlas; Q9AQU5; baseline and differential.
DR   Genevisible; Q9AQU5; ZM.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
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   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..292
FT                   /note="Aquaporin PIP1-3/PIP1-4"
FT                   /id="PRO_0000286015"
FT   TRANSMEM        61..81
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..118
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           120..122
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           241..243
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  30998 MW;  EAB96CCE83F69DE9 CRC64;
     MEGKEEDVRL GANKFSERQP IGTAAQGAGA GDDDKDYKEP PPAPLFEPGE LKSWSFYRAG
     IAEFVATFLF LYITVLTVMG VSKSTSKCAT VGIQGIAWSF GGMIFALVYC TAGISGGHIN
     PAVTFGLFLA RKLSLTRAIF YIIMQCLGAI CGAGVVKGFQ QGLYMGNGGG ANVVAPGYTK
     GDGLGAEIVG TFILVYTVFS ATDAKRNARD SHVPILAPLP IGFAVFLVHL ATIPITGTGI
     NPARSLGAAI IYNRDHAWSD HWIFWVGPFI GAALAAIYHQ VIIRAIPFKS RS