STR3_SCHPO
ID STR3_SCHPO Reviewed; 630 AA.
AC Q92341;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Low affinity heme transporter str3 {ECO:0000303|PubMed:29549126};
DE AltName: Full=Siderophore iron transporter 3;
GN Name=str3 {ECO:0000303|PubMed:12888492};
GN ORFNames=SPAC1F8.03c {ECO:0000312|PomBase:SPAC1F8.03c};
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 INDUCTION.
RX PubMed=12888492; DOI=10.1093/nar/gkg647;
RA Pelletier B., Beaudoin J., Philpott C.C., Labbe S.;
RT "Fep1 represses expression of the fission yeast Schizosaccharomyces pombe
RT siderophore-iron transport system.";
RL Nucleic Acids Res. 31:4332-4344(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, TOPOLOGY,
RP AND MUTAGENESIS OF TYR-530; TYR-534; SER-552 AND TYR-557.
RX PubMed=29549126; DOI=10.1074/jbc.ra118.002132;
RA Normant V., Mourer T., Labbe S.;
RT "The major facilitator transporter Str3 is required for low-affinity heme
RT acquisition in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 293:6349-6362(2018).
CC -!- FUNCTION: Low affinity heme transporter involved in the assimilation of
CC exogenous heme during conditions of low cellular iron.
CC {ECO:0000269|PubMed:29549126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29549126};
CC Multi-pass membrane protein {ECO:0000269|PubMed:29549126}.
CC -!- INDUCTION: Induced in iron-deplete conditions (at protein level)
CC (PubMed:29549126, PubMed:12888492). Repressed in iron-replete
CC conditions by transcriptional repressor fep1 (PubMed:29549126,
CC PubMed:12888492). {ECO:0000269|PubMed:12888492,
CC ECO:0000269|PubMed:29549126}.
CC -!- DISRUPTION PHENOTYPE: Impairs heme import into cell; simultaneous
CC disruption of shu1 exacerbates the effect.
CC {ECO:0000269|PubMed:29549126}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB03597.1; -; Genomic_DNA.
DR PIR; T38110; T38110.
DR RefSeq; NP_592792.1; NM_001018192.2.
DR AlphaFoldDB; Q92341; -.
DR BioGRID; 278381; 16.
DR STRING; 4896.SPAC1F8.03c.1; -.
DR TCDB; 2.A.1.16.9; the major facilitator superfamily (mfs).
DR iPTMnet; Q92341; -.
DR MaxQB; Q92341; -.
DR PaxDb; Q92341; -.
DR PRIDE; Q92341; -.
DR EnsemblFungi; SPAC1F8.03c.1; SPAC1F8.03c.1:pep; SPAC1F8.03c.
DR GeneID; 2541891; -.
DR KEGG; spo:SPAC1F8.03c; -.
DR PomBase; SPAC1F8.03c; str3.
DR VEuPathDB; FungiDB:SPAC1F8.03c; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_012970_2_2_1; -.
DR InParanoid; Q92341; -.
DR OMA; DSFYMLA; -.
DR PhylomeDB; Q92341; -.
DR PRO; PR:Q92341; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0020037; F:heme binding; IDA:PomBase.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904334; P:heme import across plasma membrane; IMP:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..630
FT /note="Low affinity heme transporter str3"
FT /id="PRO_0000084881"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..120
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..241
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..335
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..406
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..465
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..574
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:29549126"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29549126"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..576
FT /note="Heme binding"
FT /evidence="ECO:0000269|PubMed:29549126"
FT REGION 610..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 530
FT /note="Y->A: Decreases heme binding and cellular heme
FT import but does not affect localization to the cell
FT membrane; when associated with A-534; A-552 and A-557."
FT /evidence="ECO:0000269|PubMed:29549126"
FT MUTAGEN 534
FT /note="Y->A: Decreases heme binding and cellular heme
FT import but does not affect localization to the cell
FT membrane; when associated with A-530; A-552 and A-557."
FT /evidence="ECO:0000269|PubMed:29549126"
FT MUTAGEN 552
FT /note="S->A: Decreases heme binding cellular heme import
FT but does not affect localization to the cell membrane; when
FT associated with A-530; A-534 and A-557."
FT /evidence="ECO:0000269|PubMed:29549126"
FT MUTAGEN 557
FT /note="Y->A: Decreases heme binding cellular heme import
FT but does not affect localization to the cell membrane; when
FT associated with A-530; A-534 and A-552."
FT /evidence="ECO:0000269|PubMed:29549126"
SQ SEQUENCE 630 AA; 70558 MW; 1072680A64539FE7 CRC64;
MEAKETHSIS DHEVELQDAK PEEKSENGNF VFEKAFSSDE EKGSGYNTNE TYSKMDNSLQ
HRGVSKIEAV RDSIYQNKRG MYLAYAFGIA ILACSWASAI QSSTTYSYQV YATASFNRTS
MISTLEIATA IISSVCKPIL GKFSDITSRP MTYTLVLLFY VIGFIVVASS STISAYVIGS
VFISIGSSGL DYLNTLVVGD LTSLKWRGFM TALLSTPYIA TVWFTGFIVQ GIIDSNWRWG
YGMFAIIMPA VMTPAVIILM YLERQANKDE NIKKIINYQT EEKNKNKQSK WQKLWKAVLE
VDLFGLILLG VGWSILLLPF SLTSYAKNGW KNPSMIAMMV VGGVILIAYS GYEMFIAPYP
SCPRRVMNRT FITAVIIDFF YYLAGYLQSM YFTTYTWILY DWSYRDWTYF NNTMTIALCV
FGVFAGAMHR VFHRYKYLQI IGLVIKIVGY GILIRPNFAA TGKVDLAWSL ILIGMGGSFS
VVGSQVSCQA SVPHQDLAIA SSLLPLYTNI GGAIGAAIAS PIFSNKVPKY LREYLPSSIN
DTQVYNFYSD SSLIREYPVG TEIRDGAIKA YSRSMFFLLV PAVSLSFIPL AAAFWQSNFY
LGNQQNAVEG DQDHKKKGDK ETTQEEKIII
