PIP11_VICFA
ID PIP11_VICFA Reviewed; 286 AA.
AC P61838; P43285; Q8L9H0; Q9LDT6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Aquaporin PIP1.1;
DE AltName: Full=Plasma membrane aquaporin 1;
DE Short=Aquaporin 1;
DE AltName: Full=Plasma membrane intrinsic protein 1a;
DE Short=PIP1a;
GN Name=PIP1.1; Synonyms=AQ1, PIP1A;
OS Vicia faba (Broad bean) (Faba vulgaris).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sun M.-H., Xu W., Zhu Y.-F., Su W.-H., Tang Z.-C.;
RT "A simple method for in situ hybridyzation to RNA in guard cells of Vicia
RT faba L.: the expression of aquaporins in guard cells.";
RL Plant Mol. Biol. Rep. 19:129-135(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sun M.-H., Su W.-H., Tang Z.-C.;
RT "Vicia faba L. aquaporin mRNA.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane. Its function is impaired by Hg(2+).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; AJ289701; CAB93959.1; -; mRNA.
DR EMBL; AF266760; AAF78062.1; -; mRNA.
DR AlphaFoldDB; P61838; -.
DR SMR; P61838; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
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; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..286
FT /note="Aquaporin PIP1.1"
FT /id="PRO_0000064046"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..116
FT /note="NPA 1"
FT MOTIF 235..237
FT /note="NPA 2"
SQ SEQUENCE 286 AA; 30689 MW; 5C0284F6BB5EA7B7 CRC64;
MEGKEEDVRV GANKFPERQP IGTSAQSDKD YKEPPPAPFF EPGELSSWSF WRAGIAEFIA
TFLFLYITVL TVMGVKRSPN MCASVGIQGI AWAFGGMIFA LVYCTAGISG GHINPAVTFG
LFLARKLSLT RALYYIVMQC LGAICGAGVV KGFQPKQYQA LGGGANTVAH GYTKGSGLGA
EIIGTFVLVY TVFSATDAKR NARDSHVPIL APLPIGFAVF LVHLATIPIT GTGINPARSL
GAAIIYNKDH SWDDHWVFWV GPFIGAALAA LYHVVVIRAI PFKSRS