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FRE2_YEAST
ID   FRE2_YEAST              Reviewed;         711 AA.
AC   P36033; D6VWY3;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Ferric/cupric reductase transmembrane component 2;
DE            EC=1.16.1.9;
DE   AltName: Full=Ferric-chelate reductase 2;
DE   Flags: Precursor;
GN   Name=FRE2; OrderedLocusNames=YKL220C;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091865; DOI=10.1002/yea.320100011;
RA   Alexandraki D., Tzermia M.;
RT   "Sequencing of a 13.2 kb segment next to the left telomere of yeast
RT   chromosome XI revealed five open reading frames and recent recombination
RT   events with the right arms of chromosomes III and V.";
RL   Yeast 10:S81-S91(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8164662; DOI=10.1128/mcb.14.5.3065-3073.1994;
RA   Georgatsou E., Alexandraki D.;
RT   "Two distinctly regulated genes are required for ferric reduction, the
RT   first step of iron uptake in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 14:3065-3073(1994).
RN   [5]
RP   INDUCTION.
RX   PubMed=7720713; DOI=10.1002/j.1460-2075.1995.tb07106.x;
RA   Yamaguchi-Iwai Y., Dancis A., Klausner R.D.;
RT   "AFT1: a mediator of iron regulated transcriptional control in
RT   Saccharomyces cerevisiae.";
RL   EMBO J. 14:1231-1239(1995).
RN   [6]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=9153234; DOI=10.1074/jbc.272.21.13786;
RA   Georgatsou E., Mavrogiannis L.A., Fragiadakis G.S., Alexandraki D.;
RT   "The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are
RT   regulated by the copper-modulated Mac1p activator.";
RL   J. Biol. Chem. 272:13786-13792(1997).
RN   [7]
RP   INDUCTION.
RX   PubMed=9200812;
RX   DOI=10.1002/(sici)1097-0061(19970615)13:7<621::aid-yea121>3.0.co;2-u;
RA   Casas C., Aldea M., Espinet C., Gallego C., Gil R., Herrero E.;
RT   "The AFT1 transcriptional factor is differentially required for expression
RT   of high-affinity iron uptake genes in Saccharomyces cerevisiae.";
RL   Yeast 13:621-637(1997).
RN   [8]
RP   INDUCTION.
RX   PubMed=9726978; DOI=10.1074/jbc.273.37.23716;
RA   Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RT   "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 273:23716-23721(1998).
RN   [9]
RP   ERRATUM OF PUBMED:9726978.
RA   Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RL   J. Biol. Chem. 273:30056-30056(1998).
RN   [10]
RP   INDUCTION.
RX   PubMed=10341420;
RX   DOI=10.1002/(sici)1097-0061(199905)15:7<573::aid-yea404>3.0.co;2-7;
RA   Georgatsou E., Alexandraki D.;
RT   "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu
RT   reductase related genes.";
RL   Yeast 15:573-584(1999).
RN   [11]
RP   FUNCTION.
RX   PubMed=11120744; DOI=10.1074/jbc.m010065200;
RA   Yun C.-W., Bauler M., Moore R.E., Klebba P.E., Philpott C.C.;
RT   "The role of the FRE family of plasma membrane reductases in the uptake of
RT   siderophore-iron in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 276:10218-10223(2001).
RN   [12]
RP   INDUCTION BY AFT1 AND AFT2.
RX   PubMed=16024809; DOI=10.1128/mcb.25.15.6760-6771.2005;
RA   Courel M., Lallet S., Camadro J.-M., Blaiseau P.-L.;
RT   "Direct activation of genes involved in intracellular iron use by the yeast
RT   iron-responsive transcription factor Aft2 without its paralog Aft1.";
RL   Mol. Cell. Biol. 25:6760-6771(2005).
RN   [13]
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).
CC   -!- FUNCTION: Metalloreductase responsible for reducing extracellular iron
CC       and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-
CC       salts and Fe(3+) bound to catecholate or hydroxamate siderophores.
CC       Fe(3+) is reduced to Fe(2+), which then dissociates from the
CC       siderophore and can be imported by the high-affinity Fe(2+) transport
CC       complex in the plasma membrane. Also participates in Cu(2+) reduction
CC       and Cu(+) uptake. {ECO:0000269|PubMed:11120744,
CC       ECO:0000269|PubMed:9153234}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC         siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC         Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8164662};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:8164662}.
CC   -!- INDUCTION: By transcription factors AFT1 and AFT2 upon iron
CC       deprivation. {ECO:0000269|PubMed:10341420, ECO:0000269|PubMed:16024809,
CC       ECO:0000269|PubMed:7720713, ECO:0000269|PubMed:9153234,
CC       ECO:0000269|PubMed:9200812, ECO:0000269|PubMed:9726978}.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC       {ECO:0000305}.
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DR   EMBL; X75950; CAA53553.1; -; Genomic_DNA.
DR   EMBL; Z28220; CAA82065.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08949.1; -; Genomic_DNA.
DR   PIR; S38063; S38063.
DR   RefSeq; NP_012702.1; NM_001179785.1.
DR   AlphaFoldDB; P36033; -.
DR   SMR; P36033; -.
DR   BioGRID; 33945; 58.
DR   DIP; DIP-7473N; -.
DR   IntAct; P36033; 1.
DR   MINT; P36033; -.
DR   STRING; 4932.YKL220C; -.
DR   TCDB; 5.B.1.5.3; the phagocyte (gp91(phox)) nadph oxidase family.
DR   PaxDb; P36033; -.
DR   PRIDE; P36033; -.
DR   EnsemblFungi; YKL220C_mRNA; YKL220C; YKL220C.
DR   GeneID; 853660; -.
DR   KEGG; sce:YKL220C; -.
DR   SGD; S000001703; FRE2.
DR   VEuPathDB; FungiDB:YKL220C; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   GeneTree; ENSGT00940000176303; -.
DR   HOGENOM; CLU_010365_4_0_1; -.
DR   InParanoid; P36033; -.
DR   OMA; TFHRHIA; -.
DR   BioCyc; MetaCyc:YKL220C-MON; -.
DR   BioCyc; YEAST:YKL220C-MON; -.
DR   PRO; PR:P36033; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36033; protein.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0015677; P:copper ion import; IDA:SGD.
DR   GO; GO:0006826; P:iron ion transport; IDA:SGD.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:SGD.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Copper; Copper transport; Electron transport; FAD;
KW   Flavoprotein; Glycoprotein; Heme; Ion transport; Iron; Iron transport;
KW   Membrane; Metal-binding; NADP; Oxidoreductase; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..711
FT                   /note="Ferric/cupric reductase transmembrane component 2"
FT                   /id="PRO_0000010138"
FT   TOPO_DOM        24..164
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..280
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..317
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..340
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..353
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        375..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..423
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..711
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          280..414
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          415..534
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         316
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         479..485
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         526..529
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   BINDING         677..678
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   711 AA;  80072 MW;  3C60346577C80E53 CRC64;
     MHWTSILSAI LLFCLSGARA SPAKTVIRNK VPLLVTNACT RIFQKVTWEY TSKSKRSSPV
     CSYEPAFQSM LYCIYETLDE KGYSNKTLEK TFSTIKKNCA SYSDALQNMT NSEFYDVLNN
     GTRHMTPYVK GSANLTYPVE MDTQLRKAYY HALHGFYANL DVGNIYGGII CAYFVAIMAF
     AGVLHCMNYT PFKTVLLKQK LVGYVRGYLT LPTIGSKHAS DFSYFRIFTG YLPTRLEGII
     ILGYLVLHTV FLAYGYEYDP ENIIFKSRRV QVARYVADRS GVLAFAHFPL IVLFAGRNNF
     LEYISGVKYT SFIMFHKWLG RMMFLDAMIH GSAYTSYTVA NKTWATSKNR LYWQFGVAAL
     CLAGTMVFFS FAVFRKYFYE AFLFLHIVLG AMFFYACWEH VVSLSGIEWI YTAIAIWIVD
     RIIRIIKASY FGFPKASLQL IGDDLIRLTV KKPARPWRAK PGQYVFVSFL HPLYFWQSHP
     FTVLDSVSKN GELVIILKEK KGVTRLVKKY VCRNGGKTSM RLAIEGPYGS SSPVNNYNNV
     LLLTGGTGLP GPIAHAIKLG KTSAAAGKQS VKLVIAVRGF DVLEAYKPEL MCLENLNVQL
     HIYNTMEVPS LTPSDSLDIS QQDEKADEKG TVVATTLEKS ANPLGFDGVV FHCGRPNVKE
     LLHEAAELSG SLSVVCCGPP IFVDKVRNET AKIVLDKSAK AIEYFEEYQC W
 
 
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