HIR1_SCHPO
ID HIR1_SCHPO Reviewed; 932 AA.
AC P87314; Q9US78;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein hir1;
DE AltName: Full=Histone transcription regulator 1 homolog;
GN Name=hip1; Synonyms=hir1; ORFNames=SPBC31F10.13c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 758-920, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, INTERACTION WITH SLM9, AND SUBCELLULAR LOCATION.
RX PubMed=15121850; DOI=10.1128/mcb.24.10.4309-4320.2004;
RA Blackwell C., Martin K.A., Greenall A., Pidoux A., Allshire R.C.,
RA Whitehall S.K.;
RT "The Schizosaccharomyces pombe HIRA-like protein Hip1 is required for the
RT periodic expression of histone genes and contributes to the function of
RT complex centromeres.";
RL Mol. Cell. Biol. 24:4309-4320(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH HIP3.
RX PubMed=16428807; DOI=10.1074/jbc.m512170200;
RA Greenall A., Williams E.S., Martin K.A., Palmer J.M., Gray J., Liu C.,
RA Whitehall S.K.;
RT "Hip3 interacts with the HIRA proteins Hip1 and Slm9 and is required for
RT transcriptional silencing and accurate chromosome segregation.";
RL J. Biol. Chem. 281:8732-8739(2006).
RN [5]
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: Probably required for replication-independent chromatin
CC assembly. Required for transcriptional silencing in the outer repeat
CC (otr) centromeric repeats and the Tf2 long terminal repeat
CC retrotransposons. Repressor of histone gene transcription in G1
CC arrested cells. Required for repression of htb1 gene expression outside
CC of S phase. {ECO:0000269|PubMed:15121850, ECO:0000269|PubMed:16428807}.
CC -!- SUBUNIT: Interacts with his3 and slm9. {ECO:0000269|PubMed:15121850,
CC ECO:0000269|PubMed:16428807}.
CC -!- INTERACTION:
CC P87314; P87315: hip3; NbExp=2; IntAct=EBI-1556094, EBI-1556159;
CC P87314; O74309: slm9; NbExp=4; IntAct=EBI-1556094, EBI-1556117;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB10089.1; -; Genomic_DNA.
DR EMBL; AB027992; BAA87296.1; -; Genomic_DNA.
DR PIR; T40216; T40216.
DR RefSeq; NP_596575.1; NM_001022496.2.
DR PDB; 2Z34; X-ray; 2.40 A; C/D=469-497.
DR PDBsum; 2Z34; -.
DR AlphaFoldDB; P87314; -.
DR SMR; P87314; -.
DR BioGRID; 276752; 299.
DR IntAct; P87314; 2.
DR STRING; 4896.SPBC31F10.13c.1; -.
DR iPTMnet; P87314; -.
DR MaxQB; P87314; -.
DR PaxDb; P87314; -.
DR PRIDE; P87314; -.
DR EnsemblFungi; SPBC31F10.13c.1; SPBC31F10.13c.1:pep; SPBC31F10.13c.
DR GeneID; 2540219; -.
DR KEGG; spo:SPBC31F10.13c; -.
DR PomBase; SPBC31F10.13c; hip1.
DR VEuPathDB; FungiDB:SPBC31F10.13c; -.
DR eggNOG; KOG0973; Eukaryota.
DR HOGENOM; CLU_004372_3_0_1; -.
DR InParanoid; P87314; -.
DR OMA; RGSWDGD; -.
DR PhylomeDB; P87314; -.
DR PRO; PR:P87314; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000417; C:HIR complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; EXP:PomBase.
DR GO; GO:0034728; P:nucleosome organization; IMP:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 2.
DR IDEAL; IID50259; -.
DR InterPro; IPR031120; HIR1.
DR InterPro; IPR011494; Hira.
DR InterPro; IPR019015; HIRA_B_motif.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13831; PTHR13831; 1.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF09453; HIRA_B; 1.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Cytoplasm; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..932
FT /note="Protein hir1"
FT /id="PRO_0000051023"
FT REPEAT 16..55
FT /note="WD 1"
FT REPEAT 72..111
FT /note="WD 2"
FT REPEAT 132..171
FT /note="WD 3"
FT REPEAT 174..213
FT /note="WD 4"
FT REPEAT 222..265
FT /note="WD 5"
FT REPEAT 268..316
FT /note="WD 6"
FT REPEAT 320..361
FT /note="WD 7"
FT REGION 405..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:2Z34"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:2Z34"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:2Z34"
SQ SEQUENCE 932 AA; 103686 MW; 09D527CDB9003D3E CRC64;
MKIKKIPWLG HFDDRGHRLS IFSIHIHPDG SRIATGGLDG TIRIWSTEAI NRENENENEN
EDLPKQLCCM STHTGTVTSV RFSPNGQYLA SGSDDRVVII WHKEEAIPGL GSTFGSGEKH
TENWRSYRRL LGHDNDIQDL CWSYDSQLVV SVGLDSSIIV WNGTTFERLK RIEAHQSHVK
GITFDPAGKY FATESDDRTI KVWRVSDFSI EKTITGPFNN SPLSTYFRRP SWSPDGKHIA
APNAMNGPVS CVSIIERGTW TSEINLIGHE GPVEVTAFNP KLFRDKNDKL VCILACGGQD
RSLSIWSSAL PRPLLSCQNV FQKSIGDVCW SPDGLSLFLC SYDGNVLVCT FEKEEFGDMV
SDEEISKALA KYGHGRHGIV LPESAKQLEL EETAYAILKK PSSLSTTDPT LVPQSSSTPK
SAQKTPQKLP AFLPNRLTAE TVDTNKLTAS KEQIASPKRP GPSDNGNEIP TKFVQKVTIT
KEGKKRVAPQ LLTTLSATPS TSRLASTQLQ HTGSSQLPPQ QFSQPINSLP KGGVPILIVG
NKTKVNHEND ESDQALQEEK IEEGLLKNYY SSLIDSSTSI SNINFEAPRY KTNIVHSLNN
EQKYVLEVKN GTSEKNPTRI VALENGNTKW MDYLPRPVIL VTGSIHFWSI ACDDGSLHLY
SLTGSRLLPP IMIESKASFL HCNNAYLLCI SSSGMVYAWN VVNKTALFTA NSLAPILSRV
SNNVTIENNS TDIPHVVIAS ISKEGVPSVT LSTGETYVYS STMLCWQRIT EPWWAIGSRE
WDSSGLLQSN TQTESQPLKI YEHRTNNVLM DSGRGKLLQK MVADAITEEG YDDFETIVTI
NHLENKIASA RLLKLDDEFL VTSEVYVRLL MHHGLWQKLE EFLGELRTQT KCSIKLSGRE
VVAKMLVVLR QAVQTDNEFD RANKLIEKYA ST
