PIP11_ORYSJ
ID PIP11_ORYSJ Reviewed; 289 AA.
AC Q6EU94; A3A9X2; O48664; O49913; Q0DYV2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Aquaporin PIP1-1;
DE AltName: Full=OsPIP1;1;
DE AltName: Full=Plasma membrane intrinsic protein 1-1;
DE AltName: Full=Plasma membrane intrinsic protein 1a;
DE Short=PIP1a;
DE AltName: Full=Water channel protein RWC1;
DE Short=RWC-1;
GN Name=PIP1-1; Synonyms=PIP1A, RWC1;
GN OrderedLocusNames=Os02g0666200, LOC_Os02g44630;
GN ORFNames=OJ1486_E07.10, OsJ_007594, P0461B08.25;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Meristem;
RX PubMed=10527423; DOI=10.1023/a:1006265528015;
RA Malz S., Sauter M.;
RT "Expression of two PIP genes in rapidly growing internodes of rice is not
RT primarily controlled by meristem activity or cell expansion.";
RL Plant Mol. Biol. 40:985-995(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Wasetoittu;
RX PubMed=10725557; DOI=10.1016/s0168-9452(99)00269-1;
RA Li L.-G., Li S.-F., Tao Y., Kitagawa Y.;
RT "Molecular cloning of a novel water channel from rice: its products
RT expression in Xenopus oocytes and involvement in chilling tolerance.";
RL Plant Sci. 154:43-51(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16033806; DOI=10.1093/pcp/pci172;
RA Sakurai J., Ishikawa F., Yamaguchi T., Uemura M., Maeshima M.;
RT "Identification of 33 rice aquaporin genes and analysis of their expression
RT and function.";
RL Plant Cell Physiol. 46:1568-1577(2005).
CC -!- FUNCTION: May function as water channel to facilitate the transport of
CC water across cell membrane. {ECO:0000269|PubMed:10725557}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and anthers.
CC {ECO:0000269|PubMed:10527423, ECO:0000269|PubMed:10725557,
CC ECO:0000269|PubMed:16033806}.
CC -!- INDUCTION: Down-regulated by osmotic stress, chilling, drought and
CC treatment with gibberellin and abscisic acid (ABA). Increased
CC expression in the recovery (post-stress) phase of gibberellin and
CC abscisic acid treatment or drought. {ECO:0000269|PubMed:10527423,
CC ECO:0000269|PubMed:10725557, ECO:0000269|PubMed:16033806}.
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 -!- MISCELLANEOUS: Recovery of PIP1.1 expression after chilling is
CC increased by pretreatment with mannitol.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC
CC 1.A.8.11) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAZ24111.1; Type=Frameshift; Evidence={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; AJ224327; CAA11896.1; -; mRNA.
DR EMBL; AB009665; BAA24016.1; -; mRNA.
DR EMBL; AP004139; BAD27775.1; -; Genomic_DNA.
DR EMBL; AP005108; BAD28398.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09586.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80186.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ24111.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_015625393.1; XM_015769907.1.
DR AlphaFoldDB; Q6EU94; -.
DR SMR; Q6EU94; -.
DR STRING; 4530.OS02T0666200-01; -.
DR PaxDb; Q6EU94; -.
DR PRIDE; Q6EU94; -.
DR EnsemblPlants; Os02t0666200-01; Os02t0666200-01; Os02g0666200.
DR EnsemblPlants; Os02t0666200-02; Os02t0666200-02; Os02g0666200.
DR GeneID; 4330248; -.
DR Gramene; Os02t0666200-01; Os02t0666200-01; Os02g0666200.
DR Gramene; Os02t0666200-02; Os02t0666200-02; Os02g0666200.
DR KEGG; osa:4330248; -.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; Q6EU94; -.
DR OMA; ANKQENN; -.
DR OrthoDB; 1152704at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6EU94; baseline and differential.
DR Genevisible; Q6EU94; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..289
FT /note="Aquaporin PIP1-1"
FT /id="PRO_0000064031"
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 MOTIF 238..240
FT /note="NPA 2"
FT CONFLICT 10..11
FT /note="LG -> PR (in Ref. 2; BAA24016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 30760 MW; 6EB095DA21FB0EEC CRC64;
MEGKEEDVRL GANRYSERQP IGTAAQGAGD DKDYKEPPPA PLFEPGELKS WSFYRAGIAE
FVATFLFLYI TILTVMGVSK SSSKCATVGI QGIAWSFGGM IFALVYCTAG ISGGHINPAV
TFGLFLARKL SLTRAIFYIV MQCLGAICGA GVVKGFQQGL YMGNGGGANV VASGYTKGDG
LGAEIVGTFI LVYTVFSATD AKRNARDSHV PILAPLPIGF AVFLVHLATI PITGTGINPA
RSLGAAIIYN KDHAWNDHWI FWVGPFVGAA LAAIYHQVII RAIPFKSRS
