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FIP1_SCHPO
ID   FIP1_SCHPO              Reviewed;         397 AA.
AC   Q09919;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Plasma membrane iron permease;
GN   Name=fip1; ORFNames=SPAC1F7.07c;
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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-338; THR-340;
RP   SER-346; SER-347; SER-355; THR-357; SER-374; SER-375 AND SER-376, 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).
CC   -!- FUNCTION: Permease for high affinity iron uptake.
CC       {ECO:0000269|PubMed:8995275}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the oxidase-dependent Fe transporter (OFeT) (TC
CC       9.A.10.1) family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA91954.1; -; Genomic_DNA.
DR   PIR; S62579; S62579.
DR   RefSeq; NP_594493.1; NM_001019922.2.
DR   AlphaFoldDB; Q09919; -.
DR   BioGRID; 278056; 2.
DR   STRING; 4896.SPAC1F7.07c.1; -.
DR   TCDB; 2.A.108.1.5; the iron/lead transporter (ilt) family.
DR   iPTMnet; Q09919; -.
DR   MaxQB; Q09919; -.
DR   PaxDb; Q09919; -.
DR   PRIDE; Q09919; -.
DR   EnsemblFungi; SPAC1F7.07c.1; SPAC1F7.07c.1:pep; SPAC1F7.07c.
DR   GeneID; 2541557; -.
DR   KEGG; spo:SPAC1F7.07c; -.
DR   PomBase; SPAC1F7.07c; fip1.
DR   VEuPathDB; FungiDB:SPAC1F7.07c; -.
DR   eggNOG; ENOG502QQWE; Eukaryota.
DR   HOGENOM; CLU_046738_1_1_1; -.
DR   InParanoid; Q09919; -.
DR   OMA; ITMLKMD; -.
DR   PhylomeDB; Q09919; -.
DR   PRO; PR:Q09919; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0033573; C:high-affinity iron permease complex; IGI:PomBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0061840; F:high-affinity ferrous iron transmembrane transporter activity; IGI:PomBase.
DR   GO; GO:0034755; P:iron ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0033215; P:reductive iron assimilation; IGI:PomBase.
DR   InterPro; IPR004923; FTR1/Fip1/EfeU.
DR   PANTHER; PTHR31632; PTHR31632; 1.
DR   Pfam; PF03239; FTR1; 1.
PE   1: Evidence at protein level;
KW   Ion transport; Iron; Iron transport; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..397
FT                   /note="Plasma membrane iron permease"
FT                   /id="PRO_0000159651"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          337..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         340
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         357
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   397 AA;  44315 MW;  1D98E41AD1FD708F CRC64;
     MAKDVFSVAI FFIVLRETLE ASIIVSVLMS FISQTLMDKD GNVTDPKLKR KFMLQVWIGS
     FTALFICLAI GGGFIGAFYA LDKDIWSGSE EIWEGVFSLI AVVLITVMGF AMLRVSHLQE
     KWRKKLMKSI ANRKAKGISN WGKKYSMFLL PFFTVLREGL EVVVFVGGVG LETPATAFPL
     PVICGLIVGC LIGYFIYRGG NVMNLQWFLI ASTCILYLIS AGLMSKATFY FEMNKWNHQT
     GGDAGELGDG PGSYPFKSAV WHVNYGNPEM NSNGGYMIFN AILGWNNTGT YGSILSYIIY
     WLFVAFIMFL MWYKERRAAR LLIAKLGDKV VDLEAASSHT PVQSSSSEDE FKINSPTDDK
     GDKAIDIVTE VRESSSPVEE HKDDKTVDVI NEIRESH
 
 
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