| Tag | Content |
|---|
| CPLM ID | CPLM-011866 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ferric reductase transmembrane component 6 |
Protein Synonyms/Alias | Ferric-chelate reductase 6 |
Gene Name | FRE6 |
Gene Synonyms/Alias | YLL051C; L0593 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 625 | TQKTAVTKAANARDQ | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Metalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol. Catalyzes the reduction of Fe(3+) to Fe(2+) and Cu(2+) to Cu(+), respectively, which can then be transported by the respective vacuolar efflux systems to the cytosol. |
Sequence Annotation | DOMAIN 287 411 Ferric oxidoreductase.
DOMAIN 412 546 FAD-binding FR-type.
NP_BIND 493 499 FAD (Potential).
NP_BIND 538 541 NADP (Potential).
NP_BIND 678 679 NADP (Potential).
METAL 323 323 Iron (heme 1 axial ligand) (By
METAL 337 337 Iron (heme 2 axial ligand) (By
METAL 393 393 Iron (heme 1 axial ligand) (By
METAL 407 407 Iron (heme 2 axial ligand) (By
CARBOHYD 89 89 N-linked (GlcNAc...) (Potential).
CARBOHYD 112 112 N-linked (GlcNAc...) (Potential).
CARBOHYD 124 124 N-linked (GlcNAc...) (Potential). |
Keyword | Complete proteome; Electron transport; FAD; Glycoprotein; Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP; Oxidoreductase; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport; Vacuole. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 712 AA |
Protein Sequence | MHRTLLFLTW LISLTKAFNI KLPHTEKKDH LESNAVLACA SYINTLKWSF DSSVVPGFYS 60
TICSYSPAFD TWSLCIFNSL TDQIIPMDNT SFEESLGNVR KTCSFVDKKF SNISLEQYYS 120
SLNNASSHAL EDYGSIESLS TSIRVDRETR SRWIRAFHAH AYNLDISSVY GAYLTYYFVI 180
VGIIAVFFHM SHYNGLNRAL FASRFVNYIR GHFVLPTFLV DKHANHFKFL NVEVFTGLMP 240
NSLEAWIIFG YTLANIIFLS ISYIIDPYNL IFNSHLSQFT RLLADRSGIL AFTQFPLIII 300
FTARNSFLEF LTGVKFNSFI SFHKWIGRIM VLNATIHSLS YSLFAIINHA FKISNKQLYW 360
KFGIASITVL CVLLVLSLGI VRKRHYEFFL YTHIILALLF FYCCWQHVKI FNGWKEWIVV 420
SLLIWGLEKL FRIWNILQFR FPKATLINLN TSNNPHDEMF KVIIPKYNRR WHSKPGQYCF 480
IYFLHPLVFW QCHPFTIIDE GEKCVLVIKP KSGLTRFIYN HILQSLNGKL QLRVAIEGPY 540
GPSNLHLDKF DHLLLLSGGT GLPGPLDHAI KLSRNPDKPK SIDLIMAIKN PSFLNGYKSE 600
ILELKNSRSH VNVQVYLTQK TAVTKAANAR DQLIHFDDIM TELTSFAHIG NARPNFSNVI 660
ENAIKSTPPG DSLAVVCCGP PVLVDDVRNT VSQKLLGYPE RIIEYFEEYQ CW 712 |
Gene Ontology | GO:0000329; C:fungal-type vacuole membrane; IDA:SGD. GO:0016021; C:integral to membrane; ISM:SGD. GO:0000293; F:ferric-chelate reductase activity; IDA:SGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0015677; P:copper ion import; IGI:SGD. GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. GO:0006880; P:intracellular sequestering of iron ion; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |