MPO1_YEAST
ID MPO1_YEAST Reviewed; 174 AA.
AC P25338; D6VUC7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=2-hydroxy-palmitic acid dioxygenase MPO1 {ECO:0000303|PubMed:25345524};
DE EC=1.14.18.12 {ECO:0000269|PubMed:30530523};
DE AltName: Full=Metabolism of phytosphingosine to odd-numbered fatty acids protein 1 {ECO:0000303|PubMed:25345524};
DE Short=Metabolism of PHS to odd-numbered FA protein 1 {ECO:0000303|PubMed:25345524};
GN Name=MPO1 {ECO:0000303|PubMed:25345524}; OrderedLocusNames=YGL010W;
GN ORFNames=YGL021;
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].
RC STRAIN=ATCC 46191 / IL125-2B;
RX PubMed=1882554; DOI=10.1002/yea.320070312;
RA Chen W., Capieaux E., Balzi E., Goffeau A.;
RT "The YGL021 gene encodes a putative membrane protein with a putative
RT leucine zipper motif.";
RL Yeast 7:301-303(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 46191 / IL125-2B;
RX PubMed=1882553; DOI=10.1002/yea.320070311;
RA Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.;
RT "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and
RT ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6
RT gene, a new member of the genetic network controlling pleiotropic drug
RT resistance.";
RL Yeast 7:287-299(1991).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=25345524; DOI=10.1038/ncomms6338;
RA Kondo N., Ohno Y., Yamagata M., Obara T., Seki N., Kitamura T.,
RA Naganuma T., Kihara A.;
RT "Identification of the phytosphingosine metabolic pathway leading to odd-
RT numbered fatty acids.";
RL Nat. Commun. 5:5338-5338(2014).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=30530523; DOI=10.1128/mcb.00428-18;
RA Seki N., Mori K., Kitamura T., Miyamoto M., Kihara A.;
RT "Yeast Mpo1 is a novel dioxygenase that catalyzes the alpha-oxidation of a
RT 2-hydroxy fatty acid in an Fe2+-dependent manner.";
RL Mol. Cell. Biol. 39:0-0(2019).
CC -!- FUNCTION: Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy
CC fatty acids in an iron-dependent manner (PubMed:30530523). Involved in
CC metabolism of phytosphingosine and is required for proper endoplasmic
CC reticulum stress response (PubMed:25345524, PubMed:30530523).
CC {ECO:0000269|PubMed:25345524, ECO:0000269|PubMed:30530523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-2-hydroxyhexadecanoate + O2 = CO2 + H2O + pentadecanoate;
CC Xref=Rhea:RHEA:62404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:75927, ChEBI:CHEBI:78795;
CC EC=1.14.18.12; Evidence={ECO:0000269|PubMed:30530523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62405;
CC Evidence={ECO:0000269|PubMed:30530523};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:30530523};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.9 uM for 2-hydroxyhexadecanoate {ECO:0000269|PubMed:30530523};
CC Vmax=4.6 mmol/min/g enzyme toward 2-hydroxyhexadecanoate
CC {ECO:0000269|PubMed:30530523};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25345524}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:25345524}.
CC -!- DISRUPTION PHENOTYPE: Exhibits a defect in the metabolism that converts
CC phytosphingosine to glycerophospholipids (PubMed:25345524). Leads to
CC sensitivity to tunicamycin (PubMed:30530523).
CC {ECO:0000269|PubMed:25345524, ECO:0000269|PubMed:30530523}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MPO1 family. {ECO:0000305}.
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DR EMBL; S58126; AAD13893.1; -; Genomic_DNA.
DR EMBL; S57893; AAB19614.1; -; Genomic_DNA.
DR EMBL; Z72532; CAA96710.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08088.1; -; Genomic_DNA.
DR PIR; S64012; S64012.
DR RefSeq; NP_011505.1; NM_001180875.1.
DR AlphaFoldDB; P25338; -.
DR BioGRID; 33236; 44.
DR DIP; DIP-4727N; -.
DR STRING; 4932.YGL010W; -.
DR PaxDb; P25338; -.
DR PRIDE; P25338; -.
DR EnsemblFungi; YGL010W_mRNA; YGL010W; YGL010W.
DR GeneID; 852874; -.
DR KEGG; sce:YGL010W; -.
DR SGD; S000002978; YGL010W.
DR VEuPathDB; FungiDB:YGL010W; -.
DR eggNOG; KOG3292; Eukaryota.
DR HOGENOM; CLU_081702_2_0_1; -.
DR InParanoid; P25338; -.
DR OMA; VNIFIHM; -.
DR BioCyc; MetaCyc:G3O-30532-MON; -.
DR BioCyc; YEAST:G3O-30532-MON; -.
DR PRO; PR:P25338; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P25338; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA: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:0102672; F:fatty acid alpha-oxygenase activity; IDA:SGD.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IDA:SGD.
DR GO; GO:0046521; P:sphingoid catabolic process; IMP:SGD.
DR InterPro; IPR009305; Mpo1-like.
DR PANTHER; PTHR28026; PTHR28026; 1.
DR Pfam; PF06127; DUF962; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Endoplasmic reticulum; Iron; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..174
FT /note="2-hydroxy-palmitic acid dioxygenase MPO1"
FT /id="PRO_0000202776"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..63
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..131
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 105
FT /note="T -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..174
FT /note="RPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQR
FT Q -> TSQR (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 20173 MW; C6C5DF3C6EDBD3B1 CRC64;
MGEGLLDLRS QLGFYKFYHH NPKNVLIHSI FVPTILFSGS CMLHRVKIYQ SISLTAVLSV
LFSIFYCLLY LPTGLLAGVL LLLLNLALID HRVDLTFKQE LGLFTIGWIF QFVGHGVFEK
RRPALIDNLV QSLVLAPYFI MFEFLFKLGF MPRLKATLEH DLEIKQRNLR MQRQ
