MPO1_SCHPO
ID MPO1_SCHPO Reviewed; 222 AA.
AC O13737;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=2-hydroxy-palmitic acid dioxygenase mpo1 {ECO:0000250|UniProtKB:P25338};
DE EC=1.14.18.12 {ECO:0000250|UniProtKB:P25338};
DE AltName: Full=Metabolism of phytosphingosine to odd-numbered fatty acids protein 1 {ECO:0000250|UniProtKB:P25338};
DE Short=Metabolism of PHS to odd-numbered FA protein 1 {ECO:0000250|UniProtKB:P25338};
GN Name=mpo1; ORFNames=SPAC16E8.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy
CC fatty acids in an iron-dependent manner (By similarity). Involved in
CC metabolism of phytosphingosine and is required for proper endoplasmic
CC reticulum stress response (By similarity).
CC {ECO:0000250|UniProtKB:P25338}.
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:0000250|UniProtKB:P25338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62405;
CC Evidence={ECO:0000250|UniProtKB:P25338};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P25338};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the MPO1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11031.1; -; Genomic_DNA.
DR PIR; T37782; T37782.
DR RefSeq; NP_594214.1; NM_001019637.2.
DR AlphaFoldDB; O13737; -.
DR STRING; 4896.SPAC16E8.02.1; -.
DR PaxDb; O13737; -.
DR EnsemblFungi; SPAC16E8.02.1; SPAC16E8.02.1:pep; SPAC16E8.02.
DR GeneID; 2542322; -.
DR KEGG; spo:SPAC16E8.02; -.
DR PomBase; SPAC16E8.02; -.
DR VEuPathDB; FungiDB:SPAC16E8.02; -.
DR eggNOG; KOG3292; Eukaryota.
DR HOGENOM; CLU_081702_1_0_1; -.
DR InParanoid; O13737; -.
DR OMA; VNIFIHM; -.
DR PhylomeDB; O13737; -.
DR PRO; PR:O13737; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0102672; F:fatty acid alpha-oxygenase activity; ISO:PomBase.
DR GO; GO:0046521; P:sphingoid catabolic process; ISO:PomBase.
DR InterPro; IPR009305; Mpo1-like.
DR PANTHER; PTHR28026; PTHR28026; 1.
DR Pfam; PF06127; DUF962; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Endoplasmic reticulum; Iron; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..222
FT /note="2-hydroxy-palmitic acid dioxygenase mpo1"
FT /id="PRO_0000372356"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 222 AA; 24993 MW; 3F153DCF9DE17114 CRC64;
MTYLSRSYSF YAAYHSNPVN IKIHQVCIPL LLLTALVLLH NFVITLINSK LQINVAHLVG
LAYQIFYVTL DPLDGLLYSP VLYLFSYILP SKLFTIFSRS LVNRSAAVVH VICWILQFIG
HGVFEKRKPA LLDNLIQSLF IAPLFAFLET GPFVGYYPSV VSKIRANIKL KDVGENYPNL
SEFLFPPSMV EDAVSGVVED ASQLSYCIRP LRLSDIDDGI VF
