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   27-MAR-2024, entry version 138.
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; 92.
DR   STRING; 4932.YGL160W; -.
DR   MaxQB; P53109; -.
DR   PaxDb; 4932-YGL160W; -.
DR   PeptideAtlas; P53109; -.
DR   EnsemblFungi; YGL160W_mRNA; YGL160W; YGL160W.
DR   GeneID; 852716; -.
DR   KEGG; sce:YGL160W; -.
DR   AGR; SGD:S000003128; -.
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   OrthoDB; 2052724at2759; -.
DR   BioCyc; YEAST:G3O-30649-MONOMER; -.
DR   BioGRID-ORCS; 852716; 0 hits in 10 CRISPR screens.
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: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   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 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   PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   SFLD; SFLDF00463; AIM14; 1.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 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
//