PIP11_MAIZE
ID PIP11_MAIZE Reviewed; 287 AA.
AC Q41870;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Aquaporin PIP1-1;
DE AltName: Full=Plasma membrane intrinsic protein 1-1;
DE AltName: Full=ZmPIP1-1;
DE AltName: Full=ZmPIP1;1;
DE AltName: Full=ZmPIP1a;
GN Name=PIP1-1;
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].
RC STRAIN=cv. DEA; TISSUE=Root meristem;
RX PubMed=7632917; DOI=10.1007/bf00020395;
RA Chevalier C., Bourgeois E., Pradet A., Raymond P.;
RT "Molecular cloning and characterization of six cDNAs expressed during
RT glucose starvation in excised maize (Zea mays L.) root tips.";
RL Plant Mol. Biol. 28:473-485(1995).
RN [2]
RP TISSUE SPECIFICITY.
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 [3]
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 [4]
RP INDUCTION.
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 [5]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF VAL-245; GLN-249; HIS-250 AND
RP ALA-254.
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 PIP1-2, but not as
CC homomers. {ECO:0000269|PubMed:14671024}.
CC -!- SUBUNIT: 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: Highly expressed in roots, shoots and developing
CC tassels, and at lower levels in leaves. {ECO:0000269|PubMed:10759498}.
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; X82633; CAA57955.1; -; mRNA.
DR PIR; S60455; S60455.
DR AlphaFoldDB; Q41870; -.
DR SMR; Q41870; -.
DR PRIDE; Q41870; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41870; baseline and differential.
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:0032991; C:protein-containing complex; TAS:AgBase.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
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..287
FT /note="Aquaporin PIP1-1"
FT /id="PRO_0000286013"
FT TRANSMEM 57..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 115..117
FT /note="NPA 1"
FT /evidence="ECO:0000250"
FT MOTIF 236..238
FT /note="NPA 2"
FT /evidence="ECO:0000250"
FT MUTAGEN 245
FT /note="V->I: Active as heteromers with PIP2-5; when
FT associated with R-249; D-250 and N-254."
FT /evidence="ECO:0000269|PubMed:14671024"
FT MUTAGEN 249
FT /note="Q->R: Active as heteromers with PIP2-5; when
FT associated with V-245; D-250 and N-254."
FT /evidence="ECO:0000269|PubMed:14671024"
FT MUTAGEN 250
FT /note="H->D: Active as heteromers with PIP2-5; when
FT associated with V-245; R-249; and N-254."
FT /evidence="ECO:0000269|PubMed:14671024"
FT MUTAGEN 254
FT /note="A->N: Active as heteromers with PIP2-5; when
FT associated with V-245; R-249 and D-250."
FT /evidence="ECO:0000269|PubMed:14671024"
SQ SEQUENCE 287 AA; 30885 MW; 0F46696F5D64FA47 CRC64;
MEGKEEDVRL GANKFSERHA IGTAAQGTDD KDYKEPPPAP LFEPGELKSW SFYRPGIAEF
VATFLFLYIS ILTVMGVSKS TSKCATVGIQ GIAWSFGGMI LALVYCTAGI SGHINPAVTF
GLFLARKLSL TRAVFYIIMQ CLGAICGRGV VKGFQQGLYM GNGGRRNVVA PGYTKGDGLG
AEIVGTFILV YTVFSATDAK RRARDSHVPI LAPLPIGFAV FLVHLATMGI TGTGINPARS
LGAAVIYNQH HAWADHWIFW VGPFIGAALA AIYHQVIIRA IPFKSRS
