PUL3_KLULA
ID PUL3_KLULA Reviewed; 460 AA.
AC Q6CSN0;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=MFS-type transporter PUL3 {ECO:0000303|PubMed:30297402};
DE AltName: Full=Pulcherrimin biosynthesis cluster protein 3 {ECO:0000303|PubMed:30297402};
GN Name=PUL3 {ECO:0000303|PubMed:30297402}; OrderedLocusNames=KLLA0_C19250g;
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 [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).
RN [2]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=30297402; DOI=10.1073/pnas.1806268115;
RA Krause D.J., Kominek J., Opulente D.A., Shen X.X., Zhou X., Langdon Q.K.,
RA DeVirgilio J., Hulfachor A.B., Kurtzman C.P., Rokas A., Hittinger C.T.;
RT "Functional and evolutionary characterization of a secondary metabolite
RT gene cluster in budding yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:11030-11035(2018).
CC -!- FUNCTION: MFS-type transporer required for the uptake of iron via the
CC uptake of the siderophore pulcherrimin-iron complex.
CC {ECO:0000269|PubMed:30297402}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30297402};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Still produces pulcherrimin, but grows poorly
CC when producing pulcherrimin. {ECO:0000269|PubMed:30297402}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; CR382123; CAH01910.1; -; Genomic_DNA.
DR RefSeq; XP_453059.1; XM_453059.1.
DR AlphaFoldDB; Q6CSN0; -.
DR STRING; 284590.Q6CSN0; -.
DR EnsemblFungi; CAH01910; CAH01910; KLLA0_C19250g.
DR GeneID; 2892210; -.
DR KEGG; kla:KLLA0_C19250g; -.
DR eggNOG; ENOG502R1WK; Eukaryota.
DR HOGENOM; CLU_047735_0_0_1; -.
DR InParanoid; Q6CSN0; -.
DR OMA; QAFMIGA; -.
DR Proteomes; UP000000598; Chromosome C.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..460
FT /note="MFS-type transporter PUL3"
FT /id="PRO_0000445899"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 300..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 50444 MW; 28A40AC22861612B CRC64;
MKLTDSQKHL YSQYLAVTLI AVQFSFDTCV YLSSVVQYVK ECGSDDPENY LFILQAVSAA
VQVFFSFIIG DIASYVGSIK WVIIFLYFLS FVGNFLYSCA GAVSLNTLLG GRIICGAASS
SGAVVYSYIT AISKDRTTIF KLFSIYRTSA GICMALAQLV AILFALCDFT VRGYRITSYN
APTFASSFII LLICVLLMFV LENPPVKSAR NPKNYLDAWK KFFSAGSNRL IASLILLWNM
FLSTFFMCEV LYFMPIFLTL NVGWKTEYEG VAFMVSAVLG VAGSFFAPDL VKLFAKLNTP
STQDETDTSD NDKIEKEESE QKSDINTLHR NQVSLTIFAL FVALIGQAFM IGASEALSND
KLPKTNSGIF FTAGLSITML GYNFMGSSVP ALFSMYIDPQ VKVQLMPFIG AIAGVGKLVA
PIVLAALYKT PLGLPIGVGF GMILVGISIP SLVYLRRNKM
