GLA_LACLC
ID GLA_LACLC Reviewed; 289 AA.
AC P22094;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Glycerol facilitator-aquaporin gla;
DE AltName: Full=Aquaglyceroporin;
DE AltName: Full=Glyceroaquaporin;
GN Name=gla;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P8-2-47;
RX PubMed=1674655; DOI=10.1128/aem.57.1.38-44.1991;
RA Mayo B., Kok J., Venema K., Bockelmann W., Teuber M., Reinke H., Venema G.;
RT "Molecular cloning and sequence analysis of the X-prolyl dipeptidyl
RT aminopeptidase gene from Lactococcus lactis subsp. cremoris.";
RL Appl. Environ. Microbiol. 57:38-44(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 763 / ML3;
RX PubMed=1674656; DOI=10.1128/aem.57.1.45-50.1991;
RA Nardi M., Chopin M.-C., Chopin A., Cals M.M., Gripon J.-C.;
RT "Cloning and DNA sequence analysis of an X-prolyl dipeptidyl aminopeptidase
RT gene from Lactococcus lactis subsp. lactis NCDO 763.";
RL Appl. Environ. Microbiol. 57:45-50(1991).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=NCDO 763 / ML3;
RX PubMed=11320116; DOI=10.1099/00221287-147-5-1129;
RA Froger A., Rolland J.-P., Bron P., Lagree V., Le Caherec F., Deschamps S.,
RA Hubert J.-F., Pellerin I., Thomas D., Delamarche C.;
RT "Functional characterization of a microbial aquaglyceroporin.";
RL Microbiology 147:1129-1135(2001).
CC -!- FUNCTION: Mixed channel protein that transports both water and
CC glycerol.
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.
CC {ECO:0000305}.
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DR EMBL; M58315; AAA25231.1; -; Genomic_DNA.
DR EMBL; M35865; AAA25206.1; -; Genomic_DNA.
DR PIR; B43747; B43747.
DR PIR; B43748; B43748.
DR RefSeq; WP_011677122.1; NZ_WJUX01000052.1.
DR AlphaFoldDB; P22094; -.
DR SMR; P22094; -.
DR TCDB; 1.A.8.2.2; the major intrinsic protein (mip) family.
DR GeneID; 61110371; -.
DR OMA; ACFPGRK; -.
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 GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00333; MIP; 1.
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; 2.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycerol metabolism; Membrane; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..289
FT /note="Glycerol facilitator-aquaporin gla"
FT /id="PRO_0000064094"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 68..70
FT /note="NPA 1"
FT MOTIF 235..237
FT /note="NPA 2"
SQ SEQUENCE 289 AA; 30935 MW; 8850C2040365A268 CRC64;
MDVTWTVKYI TEFVGTALLI IMGNGAVANV ELKGTKAHAQ SWMIIGWGYG LGVMLPAVAF
GNITSQINPA FTLGLAASGL FPWAHVAQYI IAQVLGAMFG QLLIVMVYRP YYLKTQNPNA
ILGTFSTIDN VDDNSEKTRL GATINGFLNE FLGSFVLFFG AVAATNIFFG SQSITWMTNY
LKGQGADVSS SDVMNQIWVQ ASGASASKMI AHLFLGFLVM GLVVALGGPT GPGLNPARDF
GPRLVHSLLP KSVLGEAKGS SKWWYAWVPV LAPILASLAA VALFKMIYL