AIM14_YEAST
ID AIM14_YEAST Reviewed; 570 AA.
AC P53109; D6VTZ1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable metalloreductase AIM14;
DE EC=1.16.1.-;
DE AltName: Full=Altered inheritance of mitochondria protein 14;
GN Name=AIM14; OrderedLocusNames=YGL160W; ORFNames=G1837;
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].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 COPURIFICATION WITH RIBOSOMAL COMPLEXES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Probable cell surface metalloreductase. May be involved in
CC iron or copper homeostasis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ribosomes.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC {ECO:0000269|PubMed:19300474}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family. AIM14
CC subfamily. {ECO:0000305}.
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DR EMBL; Z72682; CAA96872.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07952.1; -; Genomic_DNA.
DR PIR; S60426; S60426.
DR RefSeq; NP_011355.1; NM_001181025.1.
DR AlphaFoldDB; P53109; -.
DR BioGRID; 33093; 59.
DR STRING; 4932.YGL160W; -.
DR MaxQB; P53109; -.
DR PaxDb; P53109; -.
DR PRIDE; P53109; -.
DR EnsemblFungi; YGL160W_mRNA; YGL160W; YGL160W.
DR GeneID; 852716; -.
DR KEGG; sce:YGL160W; -.
DR SGD; S000003128; AIM14.
DR VEuPathDB; FungiDB:YGL160W; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_036508_0_0_1; -.
DR InParanoid; P53109; -.
DR OMA; LIPLHKW; -.
DR BioCyc; YEAST:G3O-30649-MON; -.
DR PRO; PR:P53109; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53109; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IMP:SGD.
DR GO; GO:0006915; P:apoptotic process; IGI:SGD.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:SGD.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
PE 1: Evidence at protein level;
KW Electron transport; FAD; Flavoprotein; Ion transport; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..570
FT /note="Probable metalloreductase AIM14"
FT /id="PRO_0000202731"
FT TOPO_DOM 1..20
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 101..219
FT /note="Ferric oxidoreductase"
FT DOMAIN 250..388
FT /note="FAD-binding FR-type"
FT REGION 480..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 65840 MW; D2534C1404A04FB8 CRC64;
MKESPLITLV KRHSETHFAN IKYGYYVLII SLVYLIGLAL LRAFGRRTPS RSSSAFKNKI
IYRLYDIDPA IHLGILFFAV LIPFYYHYSL TTQSTVYLKR LGRLSYALIP LNLFLTLRPN
WFLRKNCTYT DFIPFHKWFS RIITVIGLLH GIFFIIKWAI DDNVSLKQKL ILKTFNFAGF
IISILVLFLL ICSIGPMRRY NYRLFYIVHN LVNVAFILLT PIHSRPGVKF PFLLLNCTLL
FIHIINRIVF AKSLMILNKN ANYSKTNLVH VRLPRAILPD YFEPGSHIRI SPYRRINPLY
WLLPSHPYTI ASLAEDNSID LIIKETSTAE PGSQIESLRS NPKSFHLDQE KTYTLINSYP
PSVPEECYSQ GTNIAIICGG SGISFALPLF RHFFNKENVK YLKMIWLIKD YSEYELVLDY
LKTNGLTFEK KLSNNKRISV FISGEYTAET RLDEITTNID DENSEYEMGS FNNEDEDLSI
SNFNSENADS NDNTPETSHS PTKENGSMIE VKSKHSFTLS NELKSFNNES AQVNQNETWL
FSCGPPSLLQ LSKKYCNDER INFVCETYGL
