LACP_KLULA
ID LACP_KLULA Reviewed; 587 AA.
AC P07921;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Lactose permease;
GN Name=LAC12; OrderedLocusNames=KLLA0B14861g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=3053697; DOI=10.1016/s0021-9258(18)37446-5;
RA Chang Y.-D., Dickson R.C.;
RT "Primary structure of the lactose permease gene from the yeast
RT Kluyveromyces lactis. Presence of an unusual transcript structure.";
RL J. Biol. Chem. 263:16696-16703(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: LAC12 mediates the transport of lactose and it would appear
CC that the permease works in part by a proton symport mechanism.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; X06997; CAA30053.1; -; Genomic_DNA.
DR EMBL; CR382122; CAH02586.1; -; Genomic_DNA.
DR PIR; A31776; A31776.
DR RefSeq; XP_452193.1; XM_452193.1.
DR AlphaFoldDB; P07921; -.
DR SMR; P07921; -.
DR STRING; 284590.P07921; -.
DR TCDB; 2.A.1.1.9; the major facilitator superfamily (mfs).
DR EnsemblFungi; CAH02586; CAH02586; KLLA0_B14861g.
DR GeneID; 2897085; -.
DR KEGG; kla:KLLA0_B14861g; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_13_1; -.
DR InParanoid; P07921; -.
DR OMA; IFQIGQM; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Sugar transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..587
FT /note="Lactose permease"
FT /id="PRO_0000050426"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 587 AA; 65383 MW; CC1F4C8854F75266 CRC64;
MADHSSSSSS LQKKPINTIE HKDTLGNDRD HKEALNSDND NTSGLKINGV PIEDAREEVL
LPGYLSKQYY KLYGLCFITY LCATMQGYDG ALMGSIYTED AYLKYYHLDI NSSSGTGLVF
SIFNVGQICG AFFVPLMDWK GRKPAILIGC LGVVIGAIIS SLTTTKSALI GGRWFVAFFA
TIANAAAPTY CAEVAPAHLR GKVAGLYNTL WSVGSIVAAF STYGTNKNFP NSSKAFKIPL
YLQMMFPGLV CIFGWLIPES PRWLVGVGRE EEAREFIIKY HLNGDRTHPL LDMEMAEIIE
SFHGTDLSNP LEMLDVRSLF RTRSDRYRAM LVILMAWFGQ FSGNNVCSYY LPTMLRNVGM
KSVSLNVLMN GVYSIVTWIS SICGAFFIDK IGRREGFLGS ISGAALALTG LSICTARYEK
TKKKSASNGA LVFIYLFGGI FSFAFTPMQS MYSTEVSTNL TRSKAQLLNF VVSGVAQFVN
QFATPKAMKN IKYWFYVFYV FFDIFEFIVI YFFFVETKGR SLEELEVVFE APNPRKASVD
QAFLAQVRAT LVQRNDVRVA NAQNLKEQEP LKSDADHVEK LSEAESV