DAP1_SCHPO
ID DAP1_SCHPO Reviewed; 166 AA.
AC O13995;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cytochrome P450 regulator dap1;
GN Name=dap1; ORFNames=SPAC25B8.01, SPAC26H5.15;
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 INDUCTION.
RX PubMed=16537923; DOI=10.1128/mcb.26.7.2817-2831.2006;
RA Todd B.L., Stewart E.V., Burg J.S., Hughes A.L., Espenshade P.J.;
RT "Sterol regulatory element binding protein is a principal regulator of
RT anaerobic gene expression in fission yeast.";
RL Mol. Cell. Biol. 26:2817-2831(2006).
RN [3]
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH ERG5 AND
RP ERG11, INDUCTION, HEME-BINDING, MUTAGENESIS OF 4-THR--TRP-21 AND TYR-138,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17276356; DOI=10.1016/j.cmet.2006.12.009;
RA Hughes A.L., Powell D.W., Bard M., Eckstein J., Barbuch R., Link A.J.,
RA Espenshade P.J.;
RT "Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes.";
RL Cell Metab. 5:143-149(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for sterol biosynthesis. Functions as a positive
CC regulator of cytochrome P450 enzymes erg5 and erg11. Function requires
CC bound heme. {ECO:0000269|PubMed:17276356}.
CC -!- SUBUNIT: Interacts with erg5 and erg11. {ECO:0000269|PubMed:17276356}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by sre1 in response to absence of oxygen.
CC {ECO:0000269|PubMed:16537923, ECO:0000269|PubMed:17276356}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 77 and 101. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells are viable under normal growth conditions,
CC but contains a reduced amount of ergosterol and elevated amounts of the
CC ergosterol biosynthetic intermediates, 24-methylene lanosterol,
CC ergosta-5,7,24(28)-trienol and ergosta-5,7-dienol. Deletion mutant is
CC sensitive to the inhibitors of sterol synthesis itraconazole and
CC CoCl(2). {ECO:0000269|PubMed:17276356}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB16199.1; -; Genomic_DNA.
DR PIR; T38433; T38433.
DR RefSeq; NP_594461.1; NM_001019890.2.
DR AlphaFoldDB; O13995; -.
DR SMR; O13995; -.
DR BioGRID; 279141; 7.
DR STRING; 4896.SPAC25B8.01.1; -.
DR iPTMnet; O13995; -.
DR MaxQB; O13995; -.
DR PaxDb; O13995; -.
DR PRIDE; O13995; -.
DR EnsemblFungi; SPAC25B8.01.1; SPAC25B8.01.1:pep; SPAC25B8.01.
DR GeneID; 2542688; -.
DR KEGG; spo:SPAC25B8.01; -.
DR PomBase; SPAC25B8.01; dap1.
DR VEuPathDB; FungiDB:SPAC25B8.01; -.
DR eggNOG; KOG1110; Eukaryota.
DR HOGENOM; CLU_042860_1_1_1; -.
DR InParanoid; O13995; -.
DR OMA; YSNFAGH; -.
DR PhylomeDB; O13995; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-9013405; RHOD GTPase cycle.
DR PRO; PR:O13995; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IMP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005496; F:steroid binding; ISM:PomBase.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:PomBase.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..166
FT /note="Cytochrome P450 regulator dap1"
FT /id="PRO_0000121746"
FT TRANSMEM 4..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 42..145
FT /note="Cytochrome b5 heme-binding"
FT BINDING 138
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 4..21
FT /note="Missing: Binds heme."
FT /evidence="ECO:0000269|PubMed:17276356"
FT MUTAGEN 138
FT /note="Y->F: No heme-binding; accumulates 24-methylene
FT lanosterol, ergosta-5,7,24(28)-trienol and ergosta-5,7-
FT dienol; when associated with 4-T--W-21 del."
FT /evidence="ECO:0000269|PubMed:17276356"
SQ SEQUENCE 166 AA; 18874 MW; 940BE5977503F735 CRC64;
MASTQVVFIV TLFLYLLITR WRRKNEKSFI ASEEPKQPEW RDYTPAELKE YNGSKNSLVF
LAIKGTVYNV TMGSKFYGPQ GPYSAFAGHD ASRGLAKNSF DDEFIPDSDA EELDDCSDLN
DEERQALNDW KAFFDQKYQA VGRLISPREA RAAATISETE EKVAHN
