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Protein

Probable metalloreductase AIM14

Gene

AIM14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity).By similarity

GO - Molecular functioni

  • oxidoreductase activity, oxidizing metal ions Source: SGD
  • superoxide-generating NADPH oxidase activity Source: SGD

GO - Biological processi

  • apoptotic process Source: SGD
  • ion transport Source: UniProtKB-KW
  • regulation of actin cytoskeleton organization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Ion transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciYEAST:G3O-30649-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable metalloreductase AIM14 (EC:1.16.1.-)
Alternative name(s):
Altered inheritance of mitochondria protein 14
Gene namesi
Name:AIM14
Ordered Locus Names:YGL160W
ORF Names:G1837
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL160w.
EuPathDBiFungiDB:YGL160W.
SGDiS000003128. AIM14.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020ExtracellularSequence AnalysisAdd
BLAST
Transmembranei21 – 4121HelicalSequence AnalysisAdd
BLAST
Topological domaini42 – 6928CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei70 – 9021HelicalSequence AnalysisAdd
BLAST
Topological domaini91 – 14151ExtracellularSequence AnalysisAdd
BLAST
Transmembranei142 – 16221HelicalSequence AnalysisAdd
BLAST
Topological domaini163 – 17614CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei177 – 19721HelicalSequence AnalysisAdd
BLAST
Topological domaini198 – 373176ExtracellularSequence AnalysisAdd
BLAST
Transmembranei374 – 39421HelicalSequence AnalysisAdd
BLAST
Topological domaini395 – 570176CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • perinuclear endoplasmic reticulum Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Increases frequency of mitochondrial genome loss.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 570570Probable metalloreductase AIM14PRO_0000202731Add
BLAST

Proteomic databases

MaxQBiP53109.
PaxDbiP53109.

Interactioni

Subunit structurei

Interacts with ribosomes.

Protein-protein interaction databases

BioGridi33093. 20 interactions.
STRINGi4932.YGL160W.

Structurei

3D structure databases

ProteinModelPortaliP53109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 219119Ferric oxidoreductaseAdd
BLAST
Domaini250 – 388139FAD-binding FR-typeAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.Curated
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG267494.
GeneTreeiENSGT00530000068386.
InParanoidiP53109.
OMAiVNIICGG.
OrthoDBiEOG7N37NK.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53109-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKESPLITLV KRHSETHFAN IKYGYYVLII SLVYLIGLAL LRAFGRRTPS
60 70 80 90 100
RSSSAFKNKI IYRLYDIDPA IHLGILFFAV LIPFYYHYSL TTQSTVYLKR
110 120 130 140 150
LGRLSYALIP LNLFLTLRPN WFLRKNCTYT DFIPFHKWFS RIITVIGLLH
160 170 180 190 200
GIFFIIKWAI DDNVSLKQKL ILKTFNFAGF IISILVLFLL ICSIGPMRRY
210 220 230 240 250
NYRLFYIVHN LVNVAFILLT PIHSRPGVKF PFLLLNCTLL FIHIINRIVF
260 270 280 290 300
AKSLMILNKN ANYSKTNLVH VRLPRAILPD YFEPGSHIRI SPYRRINPLY
310 320 330 340 350
WLLPSHPYTI ASLAEDNSID LIIKETSTAE PGSQIESLRS NPKSFHLDQE
360 370 380 390 400
KTYTLINSYP PSVPEECYSQ GTNIAIICGG SGISFALPLF RHFFNKENVK
410 420 430 440 450
YLKMIWLIKD YSEYELVLDY LKTNGLTFEK KLSNNKRISV FISGEYTAET
460 470 480 490 500
RLDEITTNID DENSEYEMGS FNNEDEDLSI SNFNSENADS NDNTPETSHS
510 520 530 540 550
PTKENGSMIE VKSKHSFTLS NELKSFNNES AQVNQNETWL FSCGPPSLLQ
560 570
LSKKYCNDER INFVCETYGL
Length:570
Mass (Da):65,840
Last modified:October 1, 1996 - v1
Checksum:iD2534C1404A04FB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72682 Genomic DNA. Translation: CAA96872.1.
BK006941 Genomic DNA. Translation: DAA07952.1.
PIRiS60426.
RefSeqiNP_011355.1. NM_001181025.1.

Genome annotation databases

EnsemblFungiiYGL160W; YGL160W; YGL160W.
GeneIDi852716.
KEGGisce:YGL160W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72682 Genomic DNA. Translation: CAA96872.1.
BK006941 Genomic DNA. Translation: DAA07952.1.
PIRiS60426.
RefSeqiNP_011355.1. NM_001181025.1.

3D structure databases

ProteinModelPortaliP53109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33093. 20 interactions.
STRINGi4932.YGL160W.

Proteomic databases

MaxQBiP53109.
PaxDbiP53109.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL160W; YGL160W; YGL160W.
GeneIDi852716.
KEGGisce:YGL160W.

Organism-specific databases

CYGDiYGL160w.
EuPathDBiFungiDB:YGL160W.
SGDiS000003128. AIM14.

Phylogenomic databases

eggNOGiNOG267494.
GeneTreeiENSGT00530000068386.
InParanoidiP53109.
OMAiVNIICGG.
OrthoDBiEOG7N37NK.

Enzyme and pathway databases

BioCyciYEAST:G3O-30649-MONOMER.

Miscellaneous databases

NextBioi972088.
PROiP53109.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43."
    James C.M., Indge K.J., Oliver S.G.
    Yeast 11:1413-1419(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
    Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
    Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: COPURIFICATION WITH RIBOSOMAL COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "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.
  6. "Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis."
    Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J., Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M., Troyanskaya O.G., Caudy A.A.
    PLoS Genet. 5:E1000407-E1000407(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAIM14_YEAST
AccessioniPrimary (citable) accession number: P53109
Secondary accession number(s): D6VTZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.