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Protein

Iron transport multicopper oxidase fio1

Gene

fio1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Could be a iron transport multicopper oxidase, which is required for Fe2+ high affinity uptake. May be required to oxidize Fe2+ and release it from the transporter. Essential component of copper-dependent iron transport.1 Publication

Cofactori

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Copper 1; type 2By similarity
Metal bindingi87 – 871Copper 2; type 3By similarity
Metal bindingi129 – 1291Copper 2; type 3By similarity
Metal bindingi131 – 1311Copper 3; type 3By similarity
Metal bindingi417 – 4171Copper 4; type 1By similarity
Metal bindingi420 – 4201Copper 1; type 2By similarity
Metal bindingi422 – 4221Copper 3; type 3By similarity
Metal bindingi480 – 4801Copper 3; type 3By similarity
Metal bindingi481 – 4811Copper 4; type 1By similarity
Metal bindingi482 – 4821Copper 2; type 3By similarity
Metal bindingi486 – 4861Copper 4; type 1By similarity

GO - Molecular functioni

GO - Biological processi

  • ferrous iron import across plasma membrane Source: PomBase
  • iron assimilation by reduction and transport Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Copper, Iron, Metal-binding

Protein family/group databases

TCDBi2.A.108.1.5. the iron/lead transporter (ilt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron transport multicopper oxidase fio1 (EC:1.-.-.-)
Gene namesi
Name:fio1
ORF Names:SPAC1F7.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1F7.08.
PomBaseiSPAC1F7.08. fio1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 553531ExtracellularSequence analysisAdd
BLAST
Transmembranei554 – 57421HelicalSequence analysisAdd
BLAST
Topological domaini575 – 62248CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 622600Iron transport multicopper oxidase fio1PRO_0000002965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence analysis
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence analysis
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ09920.

Interactioni

Protein-protein interaction databases

BioGridi278057. 19 interactions.
MINTiMINT-4696415.

Structurei

3D structure databases

ProteinModelPortaliQ09920.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 14799Plastocyanin-like 1Add
BLAST
Domaini194 – 304111Plastocyanin-like 2Add
BLAST
Domaini386 – 498113Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000159793.
InParanoidiQ09920.
KOiK19791.
OrthoDBiEOG7VB2Q3.
PhylomeDBiQ09920.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q09920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKFFSFPIL GLLLTCVRFV VAKERLFEWN VTDVYDVDPD GSGNSRWVIG
60 70 80 90 100
VNNKWPIDPL VVDYGDQVII KMTNSLANNR TTSLHSHGLF QKFTPYMDGV
110 120 130 140 150
PQSTQCEIPP GATFYYNYTA LQNGTYWVHS HDMSQYPDGL RTPFIINALE
160 170 180 190 200
EPYDYDEEYI ISMTDWYYTP FNILVPDEFK TWKNPTGAEP VPDTGLFNDT
210 220 230 240 250
ANATFAMEPG KTYRLRFINI GAFNNYDVMI EDHNMTIIEV DGEYTEPQEV
260 270 280 290 300
SSIHLTVAQR YSVLVTAKNS TDRNYAITAY MDESLFDTIP DNYNPNVTAW
310 320 330 340 350
LSYNSDASYD LGPDIDEIDS YDDAELNPLY SWDVTESNHS INIWFDFFTL
360 370 380 390 400
GDGANYAEIN DSSYVFPKVP SIMIANSTNV DGYNLEPVTY GPYTNAYIFE
410 420 430 440 450
YGDVVDVIID NHDTGKHPFH LHGHTFQVLE RGEENAGLYS DQESHTYYDN
460 470 480 490 500
PMRRDTVEIE PGSFIVIRFI ADNPGAWVIH CHIEWHMESG LLATFIEAPE
510 520 530 540 550
MIPSISSPDF VKEQCMLDGV PTIGNGAGNY KNISDLSGAP SPPGEMPAGW
560 570 580 590 600
TSKAIGTMAA CVISACIGMG SIIFYGASIH PVPTEELDEN DDLQEAALEN
610 620
AAMFLDTDKA VEKVVEGKDE IK
Length:622
Mass (Da):69,908
Last modified:February 1, 1996 - v1
Checksum:iA78899C7CADF2AD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91955.1.
PIRiS62580.
RefSeqiNP_594494.1. NM_001019923.2.

Genome annotation databases

EnsemblFungiiSPAC1F7.08.1; SPAC1F7.08.1:pep; SPAC1F7.08.
GeneIDi2541558.
KEGGispo:SPAC1F7.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91955.1.
PIRiS62580.
RefSeqiNP_594494.1. NM_001019923.2.

3D structure databases

ProteinModelPortaliQ09920.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278057. 19 interactions.
MINTiMINT-4696415.

Protein family/group databases

TCDBi2.A.108.1.5. the iron/lead transporter (ilt) family.

Proteomic databases

MaxQBiQ09920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1F7.08.1; SPAC1F7.08.1:pep; SPAC1F7.08.
GeneIDi2541558.
KEGGispo:SPAC1F7.08.

Organism-specific databases

EuPathDBiFungiDB:SPAC1F7.08.
PomBaseiSPAC1F7.08. fio1.

Phylogenomic databases

HOGENOMiHOG000159793.
InParanoidiQ09920.
KOiK19791.
OrthoDBiEOG7VB2Q3.
PhylomeDBiQ09920.

Miscellaneous databases

NextBioi20802654.
PROiQ09920.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "An oxidase-permease-based iron transport system in Schizosaccharomyces pombe and its expression in Saccharomyces cerevisiae."
    Askwith C., Kaplan J.
    J. Biol. Chem. 272:401-405(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiFIO1_SCHPO
AccessioniPrimary (citable) accession number: Q09920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.