Reviewed, UniProtKB/Swiss-Prot Q04800 (FRP1_SCHPO)

Names and origin

Protein names

Recommended name:
    Ferric reductase transmembrane component 1
    EC=1.16.1.7
Alternative name(s):
    Ferric-chelate reductase 1

Gene names

Name:	frp1
ORF Names:	SPBC1683.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Is required for the uptake of Fe3+ ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe3+ ion) via FAD and heme intermediates.
Catalytic activity	2 Fe2+ + NAD+ = 2 Fe3+ + NADH.
Cofactor	FAD Probable.
Subcellular location	Membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ferric reductase (FRE) family. Contains 1 FAD-binding FR-type domain. Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
Biological process	Electron transport Ion transport Iron transport Transport
Cellular component	Membrane
Domain	Transmembrane
Ligand	FAD Iron NAD
Molecular function	Oxidoreductase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW iron assimilation by reduction and transport Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe iron ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro ferric-chelate reductase activity Ref.1 Traceable author statement. Source: GeneDB_SPombe iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 564	564	Ferric reductase transmembrane component 1		PRO_0000210152
Regions
	Transmembrane	10 – 30	21	Potential
	Transmembrane	73 – 93	21	Potential
	Transmembrane	117 – 137	21	Potential
	Transmembrane	160 – 180	21	Potential
	Transmembrane	193 – 213	21	Potential
	Transmembrane	417 – 437	21	Potential
	Domain	121 – 254	134	Ferric oxidoreductase
	Domain	255 – 410	156	FAD-binding FR-type
	Nucleotide binding	317 – 323	7	FAD Potential
	Nucleotide binding	419 – 427	9	NAD Potential
Amino acid modifications
	Modified residue	362	1	Phosphoserine Ref.3
	Modified residue	381	1	Phosphoserine Ref.3
	Modified residue	383	1	Phosphoserine Ref.3
	Glycosylation	4	1	N-linked (GlcNAc...) Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Glycosylation	268	1	N-linked (GlcNAc...) Potential
	Glycosylation	360	1	N-linked (GlcNAc...) Potential
	Glycosylation	501	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q04800-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 336CC2AF934A736B	FASTA	564	64,092
	10 20 30 40 50 60 MAINSSDKWT VIAICLILGI LLAFILMFWL ERFRVIIKSN AHKHDPSDKR QIWLEKYYLF 70 80 90 100 110 120 VRQIYTYLVT HKVILTLIAV PVVFAISIPF IGMQTPASSH GKQTTQVSTG NWSKNAVAAR 130 140 150 160 170 180 LGFLACGLYV TSYFFSIKNN PFALLLISSH EKMNYVHRRL SQYAIMIGAI HGFAYIGLAA 190 200 210 220 230 240 QGKRALLTAR VTIIGYVILG LMVIMIVSSL PFFRRRFYEW FFVLHHMCSI GFLITIWLHH 250 260 270 280 290 300 RRCVVYMKVC VAVYVFDRGC RMLRSFLNRS KFDVVLVEDD LIYMKGPRPK KSFFGLPWGA 310 320 330 340 350 360 GNHMYINIPS LSYWQIHPFT IASVPSDDFI ELFVAVRAGF TKRLAKKVSS KSLSDVSDIN 370 380 390 400 410 420 ISDEKIEKNG DVGIEVMERH SLSQEDLVFE SSAAKVSVLM DGPYGPVSNP YKDYSYLFLF 430 440 450 460 470 480 AGGVGVSYIL PIILDTIKKQ SRTVHITFVW SARSSALLNI VHKSLCEAVR YTEMNINIFC 490 500 510 520 530 540 HLTNSYPVEE VSSLNSQSAR NYSLQYLNGR PDVNDYFKDF LHATGTQTAA LASCGSDKLL 550 560 RHLKSCVNTH SPSTVDLYQH YEEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The fission yeast ferric reductase gene frp1+ is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase." Roman D.G., Dancis A., Anderson G.J., Klausner R.D. Mol. Cell. Biol. 13:4342-4350(1993) [PubMed: 8321236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-381 AND SER-383, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L07749 Genomic DNA. Translation: AAA68045.1. CU329671 Genomic DNA. Translation: CAB91171.1.
PIR	A48141.
RefSeq	NP_595065.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2539711.
KEGG	spo:SPBC1683.09c.
NMPDR	fig|4896.1.peg.931.
Organism-specific databases
GeneDB_Spombe	SPBC1683.09c.
Phylogenomic databases
OMA	Q04800. TEMNINI.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003170-MON.
BRENDA	1.16.1.7. 653.
Gene expression databases
ArrayExpress	Q04800.
Family and domain databases
InterPro	IPR013112. FAD_bd_8. IPR017927. Fd_Rdtase_FAD-bd. IPR013130. Fe3_reduct_TM_N. IPR013121. Fe_red_NAD_bd_6. [Graphical view]
Pfam	PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. [Graphical view]
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FRP1_SCHPO

Accession

Primary (citable) accession number: Q04800

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)