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P38925 (SMF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Manganese transporter SMF1
Gene names
Name:SMF1
Synonyms:ESP1
Ordered Locus Names:YOL122C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High-affinity manganese transporter involved in manganese uptake from the extracellular environment. Contributes also to cellular accumulation of other divalent metal ions such as cadmium, cobalt, copper, iron and nickel. Ref.6 Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Targeted to the vacuolar lumen in presence of excess manganese, where it is degraded. Ref.7

Sequence similarities

Belongs to the NRAMP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Manganese transporter SMF1 HAMAP-Rule MF_00221
PRO_0000212605

Regions

Topological domain1 – 7070Extracellular Potential
Transmembrane71 – 9121Helical; Potential
Topological domain92 – 10817Cytoplasmic Potential
Transmembrane109 – 12921Helical; Potential
Topological domain130 – 15627Extracellular Potential
Transmembrane157 – 17721Helical; Potential
Topological domain178 – 1792Cytoplasmic Potential
Transmembrane180 – 20021Helical; Potential
Topological domain201 – 21818Extracellular Potential
Transmembrane219 – 23921Helical; Potential
Topological domain240 – 26627Cytoplasmic Potential
Transmembrane267 – 28721Helical; Potential
Topological domain288 – 34457Extracellular Potential
Transmembrane345 – 36521Helical; Potential
Topological domain366 – 39631Cytoplasmic Potential
Transmembrane397 – 41721Helical; Potential
Topological domain418 – 46346Extracellular Potential
Transmembrane464 – 48421Helical; Potential
Topological domain485 – 54359Cytoplasmic Potential
Transmembrane544 – 56421Helical; Potential
Topological domain565 – 57511Extracellular Potential

Amino acid modifications

Modified residue241Phosphoserine Ref.8

Experimental info

Sequence conflict3051E → D Ref.1
Sequence conflict4161S → A Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38925 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: AC0EEEF1BBF34ACB

FASTA57563,264
        10         20         30         40         50         60 
MVNVGPSHAA VAVDASEARK RNISEEVFEL RDKKDSTVVI EGEAPVRTFT SSSSNHERED 

        70         80         90        100        110        120 
TYVSKRQVMR DIFAKYLKFI GPGLMVSVAY IDPGNYSTAV DAGASNQFSL LCIILLSNFI 

       130        140        150        160        170        180 
AIFLQCLCIK LGSVTGLDLS RACREYLPRW LNWTLYFFAE CAVIATDIAE VIGTAIALNI 

       190        200        210        220        230        240 
LIKVPLPAGV AITVVDVFLI MFTYKPGASS IRFIRIFECF VAVLVVGVCI CFAIELAYIP 

       250        260        270        280        290        300 
KSTSVKQVFR GFVPSAQMFD HNGIYTAISI LGATVMPHSL FLGSALVQPR LLDYDVKHGN 

       310        320        330        340        350        360 
YTVSEEQDKV KKSKSTEEIM EEKYFNYRPT NAAIKYCMKY SMVELSITLF TLALFVNCAI 

       370        380        390        400        410        420 
LVVAGSTLYN SPEADGADLF TIHELLSRNL APAAGTIFML ALLLSGQSAG VVCTMSGQIV 

       430        440        450        460        470        480 
SEGHINWKLQ PWQRRLATRC ISIIPCLVIS ICIGREALSK ALNASQVVLS IVLPFLVAPL 

       490        500        510        520        530        540 
IFFTCKKSIM KTEITVDHTE EDSHNHQNNN DRSAGSVIEQ DGSSGMEIEN GKDVKIVYMA 

       550        560        570 
NNWIITVIAI IVWLFLSLLN VYAIVQLGMS HGDIS 

« Hide

References

« Hide 'large scale' references
[1]"Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein."
West A.H., Clark D.J., Martin J., Neupert W., Hartl F.-U., Horwich A.L.
J. Biol. Chem. 267:24625-24633(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria."
Supek F., Supekova L., Nelson H., Nelson N.
Proc. Natl. Acad. Sci. U.S.A. 93:5105-5110(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 200060 / W303.
[3]"DNA sequence analysis of a 10 624 bp fragment of the left arm of chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein, a mitochondrial protein, two ribosomal proteins and two new open reading frames."
Lafuente M.J., Gamo F.-J., Gancedo C.
Yeast 12:1041-1045(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"The family of SMF metal ion transporters in yeast cells."
Cohen A., Nelson H., Nelson N.
J. Biol. Chem. 275:33388-33394(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Saccharomyces cerevisiae expresses three functionally distinct homologues of the nramp family of metal transporters."
Portnoy M.E., Liu X.F., Culotta V.C.
Mol. Cell. Biol. 20:7893-7902(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[9]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[10]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15929 Genomic DNA. Translation: AAB48984.1.
X95258 Genomic DNA. Translation: CAA64547.1.
Z74864 Genomic DNA. Translation: CAA99141.1.
BK006948 Genomic DNA. Translation: DAA10662.1.
PIRS58647.
RefSeqNP_014519.1. NM_001183376.1.

3D structure databases

ProteinModelPortalP38925.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34279. 31 interactions.
IntActP38925. 3 interactions.
STRING4932.YOL122C.

Protein family/group databases

TCDB2.A.55.1.1. the metal ion (mn(2+)-iron) transporter (nramp) family.

Proteomic databases

PaxDbP38925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL122C; YOL122C; YOL122C.
GeneID854027.
KEGGsce:YOL122C.

Organism-specific databases

CYGDYOL122c.
SGDS000005482. SMF1.

Phylogenomic databases

eggNOGCOG1914.
GeneTreeENSGT00390000006526.
HOGENOMHOG000152204.
KOK12346.
OMADSRVEMG.
OrthoDBEOG7NSBBM.

Enzyme and pathway databases

BioCycYEAST:G3O-33518-MONOMER.

Gene expression databases

GenevestigatorP38925.

Family and domain databases

HAMAPMF_00221. NRAMP.
InterProIPR001046. NRAMP-like.
[Graphical view]
PANTHERPTHR11706. PTHR11706. 1 hit.
PfamPF01566. Nramp. 1 hit.
[Graphical view]
PRINTSPR00447. NATRESASSCMP.
TIGRFAMsTIGR01197. nramp. 1 hit.
ProtoNetSearch...

Other

NextBio975571.

Entry information

Entry nameSMF1_YEAST
AccessionPrimary (citable) accession number: P38925
Secondary accession number(s): D6W1U6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families