PIP27_MUSAC
ID PIP27_MUSAC Reviewed; 282 AA.
AC A0A6M3QG69;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Aquaporin PIP2-7 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:31841963};
DE AltName: Full=PIP2-6-like protein PIP2-7 {ECO:0000312|EMBL:QJC58694.1};
DE AltName: Full=Plasma membrane intrinsic protein 2-7 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:31841963};
DE Short=MaPIP2-7 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:31841963};
DE Short=MaPIP2;7 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:31841963};
GN Name=PIP2-7 {ECO:0000303|PubMed:26307965, ECO:0000303|PubMed:31841963};
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, INDUCTION BY SALT; COLD AND OSMOTIC
RP STRESSES, AND BIOTECHNOLOGY.
RC STRAIN=cv. Brazilian (AAA);
RX PubMed=31841963; DOI=10.1016/j.plaphy.2019.12.011;
RA Xu Y., Hu W., Liu J., Song S., Hou X., Jia C., Li J., Miao H., Wang Z.,
RA Tie W., Xu B., Jin Z.;
RT "An aquaporin gene MaPIP2-7 is involved in tolerance to drought, cold and
RT salt stresses in transgenic banana (Musa acuminata L.).";
RL Plant Physiol. Biochem. 147:66-76(2020).
RN [2]
RP TISSUE SPECIFICITY, INDUCTION BY SALT, 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).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane; mercury-insensitive (By similarity). Contributes
CC to the tolerance to multiple abiotic stresses including salt (NaCl),
CC cold and water deprivation, by modulating cytosolic K(+)/Na(+) ratio,
CC maintaining osmotic balance, and reducing membrane injury (e.g.
CC oxidative injury) (PubMed:31841963). Regulates also the expression of
CC abscisic acid (ABA)- biosynthetic and -responsive genes during
CC dehydration and salt stresses (PubMed:31841963).
CC {ECO:0000250|UniProtKB:P30302, ECO:0000269|PubMed:31841963}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30302};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and fruits.
CC {ECO:0000269|PubMed:26307965}.
CC -!- DEVELOPMENTAL STAGE: Present in fruit throughout the development and
CC ripening. {ECO:0000269|PubMed:26307965}.
CC -!- INDUCTION: Slightly induced by salt (NaCl) (PubMed:26307965,
CC PubMed:31841963). Accumulates in response to osmotic (mannitol) and
CC cold treatments (PubMed:31841963). {ECO:0000269|PubMed:26307965,
CC ECO:0000269|PubMed:31841963}.
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:31841963}.
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; MN380439; QJC58694.1; -; mRNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IDA:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; 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..282
FT /note="Aquaporin PIP2-7"
FT /id="PRO_0000455809"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..71
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..162
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 102..104
FT /note="NPA 1"
FT /evidence="ECO:0000255"
FT MOTIF 223..225
FT /note="NPA 2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 282 AA; 29941 MW; 5E6EDC2FFFA439B9 CRC64;
MSKEVSVEGE QPPVKDYTDP PPEPLLNFGE LRLWSFYRAL IAEFVATLLF LYVTIATVIG
HKEQNAADQC SGVGLLGIAW AFGGMIFILV YCTAGISGGH INPAVTLGLF LARKVSLIRA
LLYMVAQCLG AIVGVGIVKG IMKHQYNSLG GGANVVAAGY SKGTALGAEI IGTFVLVYTV
FSATDPKRSA RDSHVPVLAP LPIGFAVFMV HLATIPITGT GINPARSLGA AVIYNQDKPW
DDHWILWVGP FVGALAAAAY HQYILRAAAI KALGSFRSNP SN
