位置:首页 > 蛋白库 > PIP25_MAIZE
PIP25_MAIZE
ID   PIP25_MAIZE             Reviewed;         285 AA.
AC   Q9XF58;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Aquaporin PIP2-5;
DE   AltName: Full=Plasma membrane intrinsic protein 2-5;
DE   AltName: Full=ZmPIP2-5;
DE   AltName: Full=ZmPIP2;5;
DE   AltName: Full=ZmPIP2a;
GN   Name=PIP2-5;
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; TISSUE=Root;
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], 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, AND 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   [4]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF GLY-104.
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).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16845476; DOI=10.1007/s11103-006-9022-1;
RA   Hachez C., Moshelion M., Zelazny E., Cavez D., Chaumont F.;
RT   "Localization and quantification of plasma membrane aquaporin expression in
RT   maize primary root: a clue to understanding their role as cellular
RT   plumbers.";
RL   Plant Mol. Biol. 62:305-323(2006).
CC   -!- FUNCTION: Water channel required to facilitate the transport of water
CC       across cell membrane. Its function is impaired by Hg(2+). May play a
CC       role in water uptake from the root surface. Active as homomers.
CC       Increased activity when heteromerization with PIP1-2.
CC       {ECO:0000269|PubMed:10759498, ECO:0000269|PubMed:14671024,
CC       ECO:0000269|PubMed:16845476}.
CC   -!- SUBUNIT: Homomers. May interact with PIP1-2 to form heteromers.
CC       {ECO:0000269|PubMed:14671024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14671024};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:14671024}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in roots, in the exodermis,
CC       endodermis and xylem parenchyma. Polar localization to the external
CC       periclinal side of epidermal cells in root apices.
CC       {ECO:0000269|PubMed:10759498, ECO:0000269|PubMed:14671024,
CC       ECO:0000269|PubMed:16845476}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF130975; AAD28761.1; -; mRNA.
DR   EMBL; AY243802; AAO86708.1; -; mRNA.
DR   RefSeq; NP_001105616.1; NM_001112146.1.
DR   AlphaFoldDB; Q9XF58; -.
DR   SMR; Q9XF58; -.
DR   STRING; 4577.GRMZM2G178693_P01; -.
DR   TCDB; 1.A.8.11.7; the major intrinsic protein (mip) family.
DR   PaxDb; Q9XF58; -.
DR   ProMEX; Q9XF58; -.
DR   EnsemblPlants; Zm00001eb077130_T001; Zm00001eb077130_P001; Zm00001eb077130.
DR   GeneID; 542619; -.
DR   Gramene; Zm00001eb077130_T001; Zm00001eb077130_P001; Zm00001eb077130.
DR   KEGG; zma:542619; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_0_1; -.
DR   OMA; MMYMVAQ; -.
DR   OrthoDB; 1152704at2759; -.
DR   Proteomes; UP000007305; Chromosome 2.
DR   ExpressionAtlas; Q9XF58; baseline and differential.
DR   Genevisible; Q9XF58; 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..285
FT                   /note="Aquaporin PIP2-5"
FT                   /id="PRO_0000286022"
FT   TRANSMEM        38..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           107..109
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           228..230
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         104
FT                   /note="G->W: Loss of water transport."
FT                   /evidence="ECO:0000269|PubMed:14671024"
SQ   SEQUENCE   285 AA;  29836 MW;  871B8E5D9EA23F0C CRC64;
     MAKDIEAAAA HEGKDYSDPP PAPLVDAEEL TKWSLYRAVI AEFVATLLFL YITVATVIGY
     KHQTDAAASG PDAACGGVGV LGIAWAFGGM IFILVYCTAG VSGGHINPAV TFGLFLARKV
     SLVRALLYIV AQCLGAICGV GLVKGFQSAF YVRYGGGANE LSAGYSKGTG LAAEIIGTFV
     LVYTVFSATD PKRNARDSHV PVLAPLPIGF AVFMVHLATI PITGTGINPA RSLGAAVIYN
     NDKAWDDHWI FWVGPFIGAA IAAAYHQYVL RASAAKLGSS ASFSR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024