HMX1_YEAST
ID HMX1_YEAST Reviewed; 317 AA.
AC P32339; D6VYK6; Q05782; Q86ZS9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Heme-binding protein HMX1;
GN Name=HMX1; OrderedLocusNames=YLR205C; ORFNames=L8167.18;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Hong E.L., Cherry J.M.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-317.
RX PubMed=1523888; DOI=10.1002/yea.320080707;
RA Simon M., della Seta F., Sor F., Faye G.;
RT "Analysis of the MSS51 region on chromosome XII of Saccharomyces
RT cerevisiae.";
RL Yeast 8:559-567(1992).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12840010; DOI=10.1074/jbc.m306584200;
RA Protchenko O., Philpott C.C.;
RT "Regulation of intracellular heme levels by HMX1, a homologue of heme
RT oxygenase, in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:36582-36587(2003).
RN [7]
RP COFACTOR.
RX PubMed=12699699; DOI=10.1016/s1046-5928(02)00699-x;
RA Auclair K., Huang H.-W., Moenne-Loccoz P., Ortiz de Montellano P.R.;
RT "Cloning and expression of a heme binding protein from the genome of
RT Saccharomyces cerevisiae.";
RL Protein Expr. Purif. 28:340-349(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11566881; DOI=10.1093/emboj/20.18.5176;
RA Reggiori F., Pelham H.R.B.;
RT "Sorting of proteins into multivesicular bodies: ubiquitin-dependent and
RT -independent targeting.";
RL EMBO J. 20:5176-5186(2001).
RN [9]
RP INDUCTION.
RX PubMed=11112771; DOI=10.1074/jbc.m005804200;
RA Foury F., Talibi D.;
RT "Mitochondrial control of iron homeostasis. A genome wide analysis of gene
RT expression in a yeast frataxin-deficient strain.";
RL J. Biol. Chem. 276:7762-7768(2001).
CC -!- FUNCTION: Plays an important role in the degradation of heme under
CC conditions of iron deprivation. {ECO:0000269|PubMed:12840010}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:12699699};
CC Note=Binds 1 heme group. {ECO:0000269|PubMed:12699699};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:12840010}; Single-pass
CC type IV membrane protein {ECO:0000269|PubMed:11566881,
CC ECO:0000269|PubMed:12840010}.
CC -!- INDUCTION: By iron deprivation. {ECO:0000269|PubMed:11112771}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB23216.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U14913; AAB67439.2; -; Genomic_DNA.
DR EMBL; AY260884; AAP21752.1; -; Genomic_DNA.
DR EMBL; S43721; AAB23216.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006945; DAA09522.1; -; Genomic_DNA.
DR PIR; S48556; S48556.
DR RefSeq; NP_013306.2; NM_001182092.1.
DR AlphaFoldDB; P32339; -.
DR SMR; P32339; -.
DR BioGRID; 31473; 93.
DR DIP; DIP-5080N; -.
DR IntAct; P32339; 1.
DR STRING; 4932.YLR205C; -.
DR PaxDb; P32339; -.
DR PRIDE; P32339; -.
DR EnsemblFungi; YLR205C_mRNA; YLR205C; YLR205C.
DR GeneID; 850902; -.
DR KEGG; sce:YLR205C; -.
DR SGD; S000004195; HMX1.
DR VEuPathDB; FungiDB:YLR205C; -.
DR eggNOG; KOG4480; Eukaryota.
DR GeneTree; ENSGT00390000017673; -.
DR HOGENOM; CLU_049906_0_0_1; -.
DR InParanoid; P32339; -.
DR OMA; GTNFFTF; -.
DR BioCyc; YEAST:YLR205C-MON; -.
DR PRO; PR:P32339; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32339; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:SGD.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0042167; P:heme catabolic process; IMP:SGD.
DR GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
DR CDD; cd19165; HemeO; 1.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR PANTHER; PTHR10720; PTHR10720; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Heme-binding protein HMX1"
FT /id="PRO_0000209704"
FT TOPO_DOM 1..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT CONFLICT 128
FT /note="Q -> H (in Ref. 5; AAB23216)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="A -> V (in Ref. 5; AAB23216)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="V -> VK (in Ref. 5; AAB23216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 37179 MW; 4F768CDACA02AE0A CRC64;
MEDSSNTIIP SPTDVGALAN RINFQTRDAH NKINTFMGIK MAIAMRHGFI YRQGILAYYY
VFDAIEQEID RLLNDPVTEE ELQTSTILKQ FWLEDFRRST QIYKDLKLLY SNTFKSTESL
NEFLATFQKP PLLQQFINNI HENIHKEPCT ILSYCHVLYL ALFAGGKLIR SNLYRRLGLF
PNFEKLSQKE LVKKGTNFFT FSDLGPTEET RLKWEYKKNY ELATRTELTE AQKLQIISVA
EGIFDWNFNI VAEIGELNRR ELMGKFSFKC ITYLYEEWMF NKDSATRRAL HTVMLLVLSI
IAIWVLYFLV KSFLSIV
