GLPF_BUCAI
ID GLPF_BUCAI Reviewed; 263 AA.
AC P57392;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
GN Name=glpF; OrderedLocusNames=BU306;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: Mediates glycerol diffusion across the cytoplasmic membrane
CC via a pore-type mechanism. {ECO:0000250|UniProtKB:P0AER0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675,
CC ChEBI:CHEBI:17754; Evidence={ECO:0000250|UniProtKB:P0AER0};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AER0};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P0AER0}.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; BA000003; BAB13015.1; -; Genomic_DNA.
DR RefSeq; NP_240129.1; NC_002528.1.
DR RefSeq; WP_010896060.1; NC_002528.1.
DR AlphaFoldDB; P57392; -.
DR SMR; P57392; -.
DR STRING; 107806.10038980; -.
DR EnsemblBacteria; BAB13015; BAB13015; BAB13015.
DR KEGG; buc:BU306; -.
DR PATRIC; fig|107806.10.peg.317; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_9_3_6; -.
DR OMA; ACFPGRK; -.
DR Proteomes; UP000001806; Chromosome.
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 Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..263
FT /note="Glycerol uptake facilitator protein"
FT /id="PRO_0000064078"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 8..36
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 37..41
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 42..62
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 63..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 66..69
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 70..80
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 87..110
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 111..145
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 146..171
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 172..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 182..198
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 199..202
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 203..206
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 207..220
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 221..236
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 237..259
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 260..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT MOTIF 70..72
FT /note="NPA 1"
FT /evidence="ECO:0000305"
FT MOTIF 207..209
FT /note="NPA 2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29720 MW; 7F28F094BB56201B CRC64;
MNIYRKKNII KKCFMEFFGT GLVMFFGIGC LAASKLTNAN FTQFEISCIW GFGVSIAIYF
SSSISGAHLN PAVTIFFWLS SKLNKRKVLP YIISQTLGSF FFTMLTYYLY NNLLISFERN
NNVVRGTQES LNLASIFCVY PNYNNSFIYD FIIEIFSTAL FILIVLEFNN RNSNYFLYNR
SVAPILTGFL VCMINLVINP LNNISLNPAR DLGPKILLSL TGWGLFSFTG GNDNILYCFI
PIMGPILGAN LGGWIHKTLI NNS
