PHP4_SCHPO
ID PHP4_SCHPO Reviewed; 295 AA.
AC O14318; Q9HFE3;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=CCAAT-binding factor complex subunit php4;
GN Name=php4; ORFNames=SPBC16E9.01c, SPBP16F5.09c;
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 FUNCTION, AND INDUCTION.
RX PubMed=16963626; DOI=10.1128/ec.00199-06;
RA Mercier A., Pelletier B., Labbe S.;
RT "A transcription factor cascade involving Fep1 and the CCAAT-binding factor
RT Php4 regulates gene expression in response to iron deficiency in the
RT fission yeast Schizosaccharomyces pombe.";
RL Eukaryot. Cell 5:1866-1881(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 FUNCTION, AND INDUCTION.
RX PubMed=18223116; DOI=10.1128/ec.00446-07;
RA Mercier A., Watt S., Bahler J., Labbe S.;
RT "Key function for the CCAAT-binding factor Php4 to regulate gene expression
RT in response to iron deficiency in fission yeast.";
RL Eukaryot. Cell 7:493-508(2008).
RN [5]
RP INDUCTION, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH
RP CRM1 AND GRX4.
RX PubMed=19502236; DOI=10.1074/jbc.m109.009563;
RA Mercier A., Labbe S.;
RT "Both Php4 function and subcellular localization are regulated by iron via
RT a multistep mechanism involving the glutaredoxin Grx4 and the exportin
RT Crm1.";
RL J. Biol. Chem. 284:20249-20262(2009).
CC -!- FUNCTION: Component of the transcription regulatory CCAAT-binding
CC complex. Required for the reprogramming of the cell for iron use. Down-
CC regulates pcl1, sdh4, and isa1 underlow-iron conditions.
CC {ECO:0000269|PubMed:16963626, ECO:0000269|PubMed:18223116,
CC ECO:0000269|PubMed:19502236}.
CC -!- SUBUNIT: Component of tha CCAAT-binding complex composed of at least
CC php2, php3, php4 and php5 (By similarity). Interacts with crm1 and
CC grx4. {ECO:0000250, ECO:0000269|PubMed:19502236}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19502236}. Nucleus
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19502236}. Cytoplasm,
CC cytoskeleton, spindle pole. Note=Iron starvation induces nuclear
CC accumulation and iron induces relocalization to the cytoplasm, in
CC association with exportin crm1. {ECO:0000269|PubMed:19502236}.
CC -!- INDUCTION: Expressed is under the control of the iton-regulatory
CC transcription factor fep1. Expression is repressed under iron-replete
CC conditions and induced under conditions of iron starvation.
CC {ECO:0000269|PubMed:16963626, ECO:0000269|PubMed:18223116,
CC ECO:0000269|PubMed:19502236}.
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DR EMBL; CU329671; CAC08548.1; -; Genomic_DNA.
DR RefSeq; NP_595783.2; NM_001021683.3.
DR AlphaFoldDB; O14318; -.
DR SMR; O14318; -.
DR BioGRID; 276199; 7.
DR IntAct; O14318; 1.
DR STRING; 4896.SPBC16E9.01c.1; -.
DR iPTMnet; O14318; -.
DR MaxQB; O14318; -.
DR PaxDb; O14318; -.
DR PRIDE; O14318; -.
DR EnsemblFungi; SPBC16E9.01c.1; SPBC16E9.01c.1:pep; SPBC16E9.01c.
DR GeneID; 2539644; -.
DR KEGG; spo:SPBC16E9.01c; -.
DR PomBase; SPBC16E9.01c; php4.
DR VEuPathDB; FungiDB:SPBC16E9.01c; -.
DR HOGENOM; CLU_921838_0_0_1; -.
DR OMA; KQWVVPP; -.
DR PRO; PR:O14318; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016602; C:CCAAT-binding factor complex; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:PomBase.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:PomBase.
DR GO; GO:0090375; P:negative regulation of transcription from RNA polymerase II promoter in response to iron ion starvation; IMP:PomBase.
DR InterPro; IPR018287; Hap4_TF_heteromerisation.
DR Pfam; PF10297; Hap4_Hap_bind; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..295
FT /note="CCAAT-binding factor complex subunit php4"
FT /id="PRO_0000116506"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..111
FT /evidence="ECO:0000255"
FT MOTIF 93..100
FT /note="Nuclear export signal"
SQ SEQUENCE 295 AA; 32726 MW; 51B614844EC8D8E2 CRC64;
MESSKSPSEV EKSSSASPAP QKPMIRVSKQ WVVPPRPKPG RKPALDALGR RKAPIKPRPG
PTSALSVEEA KFRVREKQYQ DTIGKLQKEN NELLEQLEML QAQLKNSTLD SPKEVEVNSE
VVKPDSATTE NENRYVNQYN YPVEPPCAKN AVYTEIPIEL DPHAFLGDSA KRIRVDSDSK
DAKSVPSENG RIRVSMSPQN EINFTPENPA VMEKIRKRGV CNSVEGCLYS GSPKSVKRVR
ESEETKVYAQ LLIDLHKSSK SAPMLKAGPS IAFKLPTMEP NFNDVRPVTS ISSSS
