PIP11_MUSAC
ID PIP11_MUSAC Reviewed; 286 AA.
AC S5ZH89;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Aquaporin PIP1-1 {ECO:0000303|PubMed:24606771, ECO:0000303|PubMed:26307965};
DE AltName: Full=Plasma membrane intrinsic protein 1-1 {ECO:0000303|PubMed:24606771, ECO:0000303|PubMed:26307965};
DE Short=MaPIP1-1 {ECO:0000303|PubMed:26307965};
DE Short=MaPIP1;1 {ECO:0000303|PubMed:24606771};
GN Name=PIP1-1 {ECO:0000303|PubMed:24606771, ECO:0000303|PubMed:26307965};
OS Musa acuminata (Banana) (Musa cavendishii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX NCBI_TaxID=4641;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY
RP SALT; COLD AND WATER DEPRIVATION, TISSUE SPECIFICITY, AND BIOTECHNOLOGY.
RC STRAIN=cv. Brazilian (AAA);
RX PubMed=24606771; DOI=10.1186/1471-2229-14-59;
RA Xu Y., Hu W., Liu J., Zhang J., Jia C., Miao H., Xu B., Jin Z.;
RT "A banana aquaporin gene, MaPIP1;1, is involved in tolerance to drought and
RT salt stresses.";
RL BMC Plant Biol. 14:59-59(2014).
RN [2]
RP REPRESSION BY COLD, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Cavendish (AAA);
RX PubMed=26307965; DOI=10.3390/ijms160819728;
RA Hu W., Hou X., Huang C., Yan Y., Tie W., Ding Z., Wei Y., Liu J., Miao H.,
RA Lu Z., Li M., Xu B., Jin Z.;
RT "Genome-wide identification and expression analyses of aquaporin gene
RT family during development and abiotic stress in banana.";
RL Int. J. Mol. Sci. 16:19728-19751(2015).
RN [3]
RP FUNCTION, AND BIOTECHNOLOGY.
RC STRAIN=cv. Brazilian (AAA), and cv. Mas (AA);
RX PubMed=34512687; DOI=10.3389/fpls.2021.699230;
RA Xu Y., Liu J., Jia C., Hu W., Song S., Xu B., Jin Z.;
RT "Overexpression of a banana aquaporin gene MaPIP1;1 enhances tolerance to
RT multiple abiotic stresses in transgenic banana and analysis of its
RT interacting transcription factors.";
RL Front. Plant Sci. 12:699230-699230(2021).
RN [4]
RP ERRATUM OF PUBMED:34512687.
RX PubMed=34691136; DOI=10.3389/fpls.2021.780544;
RG Frontiers Production Office;
RL Front. Plant Sci. 12:780544-780544(2021).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane; mercury-insensitive (By similarity). Promotes
CC primary root elongation and root hair formation (PubMed:24606771).
CC Contributes to the tolerance to multiple abiotic stresses including
CC salt (NaCl), cold and water deprivation, by modulating cytosolic
CC K(+)/Na(+) ratio, maintaining osmotic balance, and reducing membrane
CC injury (e.g. oxidative injury) (PubMed:24606771, PubMed:34512687).
CC Regulates also the expression of abscisic acid (ABA)-responsive genes
CC during dehydration and salt stresses (PubMed:24606771,
CC PubMed:34512687). {ECO:0000250|UniProtKB:P30302,
CC ECO:0000269|PubMed:24606771, ECO:0000269|PubMed:34512687}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24606771};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers and
CC fruits, with highest levels in roots. {ECO:0000269|PubMed:24606771,
CC ECO:0000269|PubMed:26307965}.
CC -!- DEVELOPMENTAL STAGE: Present in fruit throughout the development, but
CC fades out during ripening. {ECO:0000269|PubMed:26307965}.
CC -!- INDUCTION: Induced by salt (NaCl) and water deprivation
CC (PubMed:24606771). Repressed by chilling treatment (PubMed:24606771,
CC PubMed:26307965). Seems to be regulated by several transcription factor
CC genes, including MaERF14, MaDREB1G, MaMYB1R1, MaERF1/39, MabZIP53 and
CC MaMYB22 under salt or cold stresses (PubMed:34512687).
CC {ECO:0000269|PubMed:24606771, ECO:0000269|PubMed:26307965,
CC ECO:0000269|PubMed:34512687}.
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). {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Can be used to improve resistance to abiotic stresses
CC such as cold, drought and salt. {ECO:0000269|PubMed:24606771,
CC ECO:0000269|PubMed:34512687}.
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; KC969669; AGT36590.1; -; mRNA.
DR SMR; S5ZH89; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IDA:UniProtKB.
DR GO; GO:0080022; P:primary root development; IDA:UniProtKB.
DR GO; GO:2000070; P:regulation of response to water deprivation; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IDA:UniProtKB.
DR GO; GO:0080147; P:root hair cell development; IDA:UniProtKB.
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 Abscisic acid signaling pathway; Cell membrane; Membrane; Stress response;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="Aquaporin PIP1-1"
FT /id="PRO_0000455806"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..88
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 89..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..174
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..256
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 114..116
FT /note="NPA 1"
FT /evidence="ECO:0000255"
FT MOTIF 235..237
FT /note="NPA 2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 286 AA; 30599 MW; A3385DB73C7031C8 CRC64;
MEGKEEDVRL GANKFSERQP IGTAAQSDKG YKEPPPAPLF EPGELTSWSF YRAGIAEFMA
TFLFLYITIL TVMGVVKSNS KCSTVGIQGI AWAFGGMIFA LVYCTAGISG GHINPAVTFG
LFLARKLSLT RALFYMVMQC LGAICGAGVV KGYQKGLYES NGGGANVVAP GYTKGDGLGA
EIVGTFILVY TVFSATDAKR NARDSHVPIL APLPIGFAVF LVHLATIPIT GTGINPARSL
GAAIIYNKKH AWDDHWIFWV GPFIGAALAA IYHQIVIRAI PFKSRP
