FIO1_SCHPO
ID FIO1_SCHPO Reviewed; 622 AA.
AC Q09920;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Iron transport multicopper oxidase fio1;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=fio1; ORFNames=SPAC1F7.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=8995275; DOI=10.1074/jbc.272.1.401;
RA Askwith C., Kaplan J.;
RT "An oxidase-permease-based iron transport system in Schizosaccharomyces
RT pombe and its expression in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 272:401-405(1997).
CC -!- FUNCTION: Could be an iron transport multicopper oxidase, which is
CC required for Fe(2+) high affinity uptake. May be required to oxidize
CC Fe(2+) and release it from the transporter. Essential component of
CC copper-dependent iron transport. {ECO:0000269|PubMed:8995275}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91955.1; -; Genomic_DNA.
DR PIR; S62580; S62580.
DR RefSeq; NP_594494.1; NM_001019923.2.
DR AlphaFoldDB; Q09920; -.
DR SMR; Q09920; -.
DR BioGRID; 278057; 21.
DR STRING; 4896.SPAC1F7.08.1; -.
DR TCDB; 2.A.108.1.5; the iron/lead transporter (ilt) family.
DR MaxQB; Q09920; -.
DR PaxDb; Q09920; -.
DR PRIDE; Q09920; -.
DR EnsemblFungi; SPAC1F7.08.1; SPAC1F7.08.1:pep; SPAC1F7.08.
DR GeneID; 2541558; -.
DR KEGG; spo:SPAC1F7.08; -.
DR PomBase; SPAC1F7.08; fio1.
DR VEuPathDB; FungiDB:SPAC1F7.08; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR InParanoid; Q09920; -.
DR OMA; VHYDDTM; -.
DR PhylomeDB; Q09920; -.
DR PRO; PR:Q09920; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0033573; C:high-affinity iron permease complex; IGI:PomBase.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IMP:PomBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0033215; P:reductive iron assimilation; IMP:PomBase.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Glycoprotein; Ion transport; Iron; Iron transport;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..622
FT /note="Iron transport multicopper oxidase fio1"
FT /id="PRO_0000002965"
FT TOPO_DOM 23..553
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..147
FT /note="Plastocyanin-like 1"
FT DOMAIN 194..304
FT /note="Plastocyanin-like 2"
FT DOMAIN 386..498
FT /note="Plastocyanin-like 3"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 69908 MW; A78899C7CADF2AD4 CRC64;
MNKFFSFPIL GLLLTCVRFV VAKERLFEWN VTDVYDVDPD GSGNSRWVIG VNNKWPIDPL
VVDYGDQVII KMTNSLANNR TTSLHSHGLF QKFTPYMDGV PQSTQCEIPP GATFYYNYTA
LQNGTYWVHS HDMSQYPDGL RTPFIINALE EPYDYDEEYI ISMTDWYYTP FNILVPDEFK
TWKNPTGAEP VPDTGLFNDT ANATFAMEPG KTYRLRFINI GAFNNYDVMI EDHNMTIIEV
DGEYTEPQEV SSIHLTVAQR YSVLVTAKNS TDRNYAITAY MDESLFDTIP DNYNPNVTAW
LSYNSDASYD LGPDIDEIDS YDDAELNPLY SWDVTESNHS INIWFDFFTL GDGANYAEIN
DSSYVFPKVP SIMIANSTNV DGYNLEPVTY GPYTNAYIFE YGDVVDVIID NHDTGKHPFH
LHGHTFQVLE RGEENAGLYS DQESHTYYDN PMRRDTVEIE PGSFIVIRFI ADNPGAWVIH
CHIEWHMESG LLATFIEAPE MIPSISSPDF VKEQCMLDGV PTIGNGAGNY KNISDLSGAP
SPPGEMPAGW TSKAIGTMAA CVISACIGMG SIIFYGASIH PVPTEELDEN DDLQEAALEN
AAMFLDTDKA VEKVVEGKDE IK
