ID   AIM14_KLULA             Reviewed;         508 AA.
AC   Q6CIY2;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; OrderedLocusNames=KLLA0F23034g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Probable cell surface metalloreductase. May be involved in
CC       iron or copper homeostasis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family. AIM14
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382126; CAG98815.1; -; Genomic_DNA.
DR   RefSeq; XP_456107.1; XM_456107.1.
DR   AlphaFoldDB; Q6CIY2; -.
DR   SMR; Q6CIY2; -.
DR   STRING; 28985.XP_456107.1; -.
DR   EnsemblFungi; CAG98815; CAG98815; KLLA0_F23034g.
DR   GeneID; 2895365; -.
DR   KEGG; kla:KLLA0_F23034g; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   InParanoid; Q6CIY2; -.
DR   OMA; LIPLHKW; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IEA:EnsemblFungi.
DR   GO; GO:0006915; P:apoptotic process; IEA:EnsemblFungi.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:EnsemblFungi.
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.
DR   SUPFAM; SSF52343; SSF52343; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Ion transport; Membrane; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..508
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408745"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          97..214
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          241..361
FT                   /note="FAD-binding FR-type"
SQ   SEQUENCE   508 AA;  58953 MW;  A2A4F42ED1F3F68A CRC64;
     MDASSLVKRG SSTHYANLPY GYYVLGVIVF YTIFLIVMRW LIPSRYTKVS PWKNKLLQSI
     RTASPCFHMP LLLLLVFVPF IHKYSLVAYI SLYLKRLGRL SYVLVILNVL LTLRPANPIL
     GYHYLDLIPL HKWLSRFVTV IGIIHGIGFI VKWSLDPKVS MISKATKLFN FIGVIAFVPL
     FILMFASVRI WRRYSYRSFY VIHQLGQWAM VFLVPIHARP RVTVPYFFIL LALYIWRGIS
     YIYYSTTVNV TQRVKDDTSL TYVKLDRSAI RDWLPGSHLR LSKYKKKNPL YWLMPTQPYT
     IASLPDESQI DLIIRENLTP YVVVGEYTVV DVYSTVPPSL LYDSQRVAIV VGGSGISFGL
     SIFKYLQTRN LDYLKFIWLI REREDMHILN HCNFETNDLE VYVTRSLPPD DTQTKSMNAN
     GSSEFDDIDF ELETMDESGA LLTNDSKSPS LVHFGRRLDW QVDLAQFIES HALQNSWLVC
     CGPESLLTDG ERYAKQNYCN FVKEFYDI