ENB1_YEAST
ID ENB1_YEAST Reviewed; 606 AA.
AC Q08299; D6W1R2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Siderophore iron transporter ENB1;
DE AltName: Full=Enterobactin permease;
DE AltName: Full=Siderophore iron transporter ARN4;
GN Name=ENB1; Synonyms=ARN4; OrderedLocusNames=YOL158C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10744769; DOI=10.1074/jbc.275.14.10709;
RA Yun C.-W., Ferea T., Rashford J., Ardon O., Brown P.O., Botstein D.,
RA Kaplan J., Philpott C.C.;
RT "Desferrioxamine-mediated iron uptake in Saccharomyces cerevisiae. Evidence
RT for two pathways of iron uptake.";
RL J. Biol. Chem. 275:10709-10715(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=12196168; DOI=10.1042/bst0300698;
RA Philpott C.C., Protchenko O., Kim Y.W., Boretsky Y., Shakoury-Elizeh M.;
RT "The response to iron deprivation in Saccharomyces cerevisiae: expression
RT of siderophore-based systems of iron uptake.";
RL Biochem. Soc. Trans. 30:698-702(2002).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in the transport of siderophore enterobactin and so
CC has a role in iron homeostasis. {ECO:0000269|PubMed:12196168}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; Z74900; CAA99180.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10628.1; -; Genomic_DNA.
DR PIR; S66857; S66857.
DR RefSeq; NP_014484.1; NM_001183411.1.
DR AlphaFoldDB; Q08299; -.
DR BioGRID; 34260; 48.
DR STRING; 4932.YOL158C; -.
DR TCDB; 2.A.1.16.2; the major facilitator superfamily (mfs).
DR iPTMnet; Q08299; -.
DR MaxQB; Q08299; -.
DR PaxDb; Q08299; -.
DR PRIDE; Q08299; -.
DR EnsemblFungi; YOL158C_mRNA; YOL158C; YOL158C.
DR GeneID; 854007; -.
DR KEGG; sce:YOL158C; -.
DR SGD; S000005518; ENB1.
DR VEuPathDB; FungiDB:YOL158C; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_012970_2_1_1; -.
DR InParanoid; Q08299; -.
DR OMA; MSVYQIG; -.
DR BioCyc; YEAST:G3O-33546-MON; -.
DR PRO; PR:Q08299; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08299; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0033101; C:cellular bud membrane; IDA:SGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0015620; F:ferric-enterobactin transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015343; F:siderophore transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0015685; P:ferric-enterobactin import into cell; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Endosome; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..606
FT /note="Siderophore iron transporter ENB1"
FT /id="PRO_0000084865"
FT TOPO_DOM 1..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..187
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..279
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..337
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..390
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..435
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..550
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 606 AA; 66970 MW; 4ED81A2A6A43815D CRC64;
MLETDHSRND NLDDKSTVCY SEKTDSNVEK STTSGLRRID AVNKVLSDYS SFTAFGVTFS
SLKTALLVAL FLQGYCTGLG GQISQSIQTY AANSFGKHSQ VGSINTVKSI VASVVAVPYA
RISDRFGRIE CWIFALVLYT IGEIISAATP TFSGLFAGIV IQQFGYSGFR LLATALTGDL
SGLRDRTFAM NIFLIPVIIN TWVSGNIVSS VAGNVAPYKW RWGYGIFCII VPISTLILVL
PYVYAQYISW RSGKLPPLKL KEKGQTLRQT LWKFADDINL IGVILFTAFL VLVLLPLTIA
GGATSKWREG HIIAMIVVGG CLGFIFLIWE LKFAKNPFIP RVYLGDPTIY VALLMEFVWR
LGLQIELEYL VTVLMVAFGE STLSAQRIAQ LYNFLQSCTN IVVGIMLHFY PHPKVFVVAG
SLLGVIGMGL LYKYRVVYDG ISGLIGAEIV VGIAGGMIRF PMWTLVHAST THNEMATVTG
LLMSVYQIGD AVGASIAGAI WTQRLAKELI QRLGSSLGMA IYKSPLNYLK KYPIGSEVRV
QMIESYSKIQ RLLIIVSISF AAFNAVLCFF LRGFTVNKKQ SLSAEEREKE KLKIKQQSWL
RRVIGY
