PHF1_SCHPO
ID PHF1_SCHPO Reviewed; 461 AA.
AC P87233;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=SWM histone demethylase complex subunit phf1;
DE AltName: Full=PHD finger domain-containing protein phf1;
GN Name=phf1; Synonyms=saf50, swp1; ORFNames=SPCC4G3.07c;
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 IDENTIFICATION IN THE SWM HISTONE DEMETHYLASE COMPLEX.
RX PubMed=16990277; DOI=10.1074/jbc.m606349200;
RA Nicolas E., Lee M.G., Hakimi M.-A., Cam H.P., Grewal S.I.S.,
RA Shiekhattar R.;
RT "Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a
RT common set of genes with diverse functions.";
RL J. Biol. Chem. 281:35983-35988(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 IN THE SWM HISTONE DEMETHYLASE COMPLEX, AND FUNCTION OF THE
RP SWM COMPLEX.
RX PubMed=17434129; DOI=10.1016/j.molcel.2007.02.023;
RA Lan F., Zaratiegui M., Villen J., Vaughn M.W., Verdel A., Huarte M.,
RA Shi Y., Gygi S.P., Moazed D., Martienssen R.A., Shi Y.;
RT "S. pombe LSD1 homologs regulate heterochromatin propagation and
RT euchromatic gene transcription.";
RL Mol. Cell 26:89-101(2007).
RN [5]
RP IDENTIFICATION IN THE SWM HISTONE DEMETHYLASE COMPLEX, AND FUNCTION OF THE
RP SWM COMPLEX.
RX PubMed=17440621; DOI=10.1371/journal.pone.0000386;
RA Opel M., Lando D., Bonilla C., Trewick S.C., Boukaba A., Walfridsson J.,
RA Cauwood J., Werler P.J., Carr A.M., Kouzarides T., Murzina N.V.,
RA Allshire R.C., Ekwall K., Laue E.D.;
RT "Genome-wide studies of histone demethylation catalysed by the fission
RT yeast homologues of mammalian LSD1.";
RL PLoS ONE 2:E386-E386(2007).
CC -!- FUNCTION: Component of the SWM histone demethylase complex that
CC specifically demethylates H3K9me2, a specific tag for epigenetic
CC transcriptional activation, thereby acting as a corepressor. Has a role
CC in regulating heterochromatin propagation and euchromatic
CC transcription. {ECO:0000269|PubMed:17434129,
CC ECO:0000269|PubMed:17440621}.
CC -!- SUBUNIT: Component of the SWM histone demethylase complex composed of
CC at least lsd1, lsd2, phf1 and phf2. {ECO:0000269|PubMed:16990277,
CC ECO:0000269|PubMed:17434129, ECO:0000269|PubMed:17440621}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAB09774.1; -; Genomic_DNA.
DR PIR; T41369; T41369.
DR RefSeq; NP_587831.1; NM_001022824.2.
DR AlphaFoldDB; P87233; -.
DR SMR; P87233; -.
DR BioGRID; 275971; 6.
DR STRING; 4896.SPCC4G3.07c.1; -.
DR MaxQB; P87233; -.
DR PaxDb; P87233; -.
DR EnsemblFungi; SPCC4G3.07c.1; SPCC4G3.07c.1:pep; SPCC4G3.07c.
DR GeneID; 2539406; -.
DR KEGG; spo:SPCC4G3.07c; -.
DR PomBase; SPCC4G3.07c; phf1.
DR VEuPathDB; FungiDB:SPCC4G3.07c; -.
DR eggNOG; KOG4323; Eukaryota.
DR HOGENOM; CLU_594680_0_0_1; -.
DR InParanoid; P87233; -.
DR OMA; KENIFAW; -.
DR PRO; PR:P87233; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0033193; C:Lsd1/2 complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IPI:PomBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IPI:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..461
FT /note="SWM histone demethylase complex subunit phf1"
FT /id="PRO_0000363000"
FT ZN_FING 190..246
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 79..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 51285 MW; AFCEB88216CCE1AD CRC64;
MSQKNFFDEG KSYGVNDYAG FHFENGADSS LPQVSAQGVV RETDSSNFDA SPVASGSGIS
DVGPFGADFH QLQQHVQTPY GGMTMPASSS SGATSVPPEQ DPSLSVSFNR LPKSASTKTK
NGRIRSSRRE DDNRIPFYDL DVAEGAEDDL QEDFHVEGMK TKSGRKIQRP VAYNPNATAL
KRKSRKVDMV TLCSVCQRGH SPLSNRIVFC DGCNSPYHQL CHHPPIDDAT VQDVDAEWFC
MKCQYRRAKQ PLETGMTAQD LGLSESDKKM YLSSLPTPHL ADLILFCEKS YPSLPIYNPR
TRELLGEIRH QLLVSSERQQ ISLQERLHAK QDEAPSDEPA PVPYTASYVA NSGTLYDYPT
LIRLAIRNTL SPSKDEIFNW LAQNVPLLPT FHDSASEAIR WMVNKGQLVR SGSIYQIATV
EEYPHLQPSL LPTFQRNRKV PKLVPVSFPT DDPQNLCATV L
