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SMF3_YEAST
ID   SMF3_YEAST              Reviewed;         473 AA.
AC   Q12078; D6VY36;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Iron transporter SMF3;
GN   Name=SMF3; OrderedLocusNames=YLR034C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D7;
RA   Ahne F., Leibhardt S., Gstoehl M., Wendel S., Berthe-Corti L.,
RA   Eckardt-Schupp F.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=10930410; DOI=10.1074/jbc.m004611200;
RA   Cohen A., Nelson H., Nelson N.;
RT   "The family of SMF metal ion transporters in yeast cells.";
RL   J. Biol. Chem. 275:33388-33394(2000).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11027260; DOI=10.1128/mcb.20.21.7893-7902.2000;
RA   Portnoy M.E., Liu X.F., Culotta V.C.;
RT   "Saccharomyces cerevisiae expresses three functionally distinct homologues
RT   of the nramp family of metal transporters.";
RL   Mol. Cell. Biol. 20:7893-7902(2000).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Has a role in controlling the cellular iron ion levels.
CC       Mobilizes vacuolar stores of iron in conditions of low iron levels.
CC       {ECO:0000269|PubMed:10930410, ECO:0000269|PubMed:11027260}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC       Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
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DR   EMBL; U34585; AAA77056.1; -; Genomic_DNA.
DR   EMBL; Z73206; CAA97558.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09352.1; -; Genomic_DNA.
DR   PIR; S59365; S59365.
DR   RefSeq; NP_013134.1; NM_001181921.2.
DR   AlphaFoldDB; Q12078; -.
DR   SMR; Q12078; -.
DR   BioGRID; 31308; 62.
DR   DIP; DIP-4163N; -.
DR   MINT; Q12078; -.
DR   STRING; 4932.YLR034C; -.
DR   TCDB; 2.A.55.1.3; the metal ion (mn(2+)-iron) transporter (nramp) family.
DR   iPTMnet; Q12078; -.
DR   MaxQB; Q12078; -.
DR   PaxDb; Q12078; -.
DR   PRIDE; Q12078; -.
DR   EnsemblFungi; YLR034C_mRNA; YLR034C; YLR034C.
DR   GeneID; 850721; -.
DR   KEGG; sce:YLR034C; -.
DR   SGD; S000004024; SMF3.
DR   VEuPathDB; FungiDB:YLR034C; -.
DR   eggNOG; KOG1291; Eukaryota.
DR   HOGENOM; CLU_020088_4_0_1; -.
DR   InParanoid; Q12078; -.
DR   OMA; IATFVNS; -.
DR   BioCyc; YEAST:G3O-32193-MON; -.
DR   PRO; PR:Q12078; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q12078; protein.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022890; F:inorganic cation transmembrane transporter activity; ISS:SGD.
DR   GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR   GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006826; P:iron ion transport; IMP:SGD.
DR   HAMAP; MF_00221; NRAMP; 1.
DR   InterPro; IPR001046; NRAMP_fam.
DR   PANTHER; PTHR11706; PTHR11706; 1.
DR   Pfam; PF01566; Nramp; 1.
DR   PRINTS; PR00447; NATRESASSCMP.
DR   TIGRFAMs; TIGR01197; nramp; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Ion transport; Iron; Iron transport;
KW   Membrane; Metal-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..473
FT                   /note="Iron transporter SMF3"
FT                   /id="PRO_0000270538"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   473 AA;  51775 MW;  09CDB86BA42E18C9 CRC64;
     MRSYMQILQK FAKFIGPGIL VSVAYMDPGN YATSVSGGAQ YKYTLLFSIF ISNIFAVLLQ
     CLCVKLGTIT GYDLAENCRH NLPKKLNYTL YLFAEVAIIA TDLAEVVGTA IALQILFKIP
     LTWGVLLTVL DVLVILMFYT PNGQSLKKVR VFEFGVGILV IGTCICFVLE LFKVSIPDKA
     ELFKGFLPSN IIFKEQQALY ISLGILGATV MPHSLYLGSS IVKPRLHDYD LKKYGKVNAR
     PSLSAIKYTL NYAYAELIIS LFLIATFVNS AILIVAGATL SGQPEAEDAD LLSIYKLLVH
     YISPAAGLIF ALAMLCSGQS AGIICTLAGQ IVSEGFLQWS LPPWATRLCT RLIAIVPCLF
     VTLTMGEKGI SDILNFSQVV LSLILPIVSA PLIYFTANRK LMVVHDENGV VRAPADVNAI
     ADETTPLNSK HSKIVDFTNS RLLTYTSVFV WALIGSLNCY LVISYLLGAD IHF
 
 
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