CHP1_SCHPO
ID CHP1_SCHPO Reviewed; 960 AA.
AC Q10103;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Chromo domain-containing protein 1 {ECO:0000303|PubMed:9722643};
GN Name=chp1 {ECO:0000303|PubMed:9722643};
GN ORFNames=SPAC18G6.02c {ECO:0000312|PomBase:SPAC18G6.02c};
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 SUBCELLULAR LOCATION.
RX PubMed=9722643; DOI=10.1093/nar/26.18.4222;
RA Doe C.L., Wang G., Chow C.-M., Fricker M.D., Singh P.B., Mellor E.J.;
RT "The fission yeast chromo domain encoding gene chp1(+) is required for
RT chromosome segregation and shows a genetic interaction with alpha-
RT tubulin.";
RL Nucleic Acids Res. 26:4222-4229(1998).
RN [3]
RP FUNCTION.
RX PubMed=10835380; DOI=10.1093/genetics/155.2.551;
RA Thon G., Verhein-Hansen J.;
RT "Four chromo-domain proteins of Schizosaccharomyces pombe differentially
RT repress transcription at various chromosomal locations.";
RL Genetics 155:551-568(2000).
RN [4]
RP FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15607976; DOI=10.1016/j.cell.2004.11.034;
RA Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P.,
RA Moazed D.;
RT "Two RNAi complexes, RITS and RDRC, physically interact and localize to
RT noncoding centromeric RNAs.";
RL Cell 119:789-802(2004).
RN [5]
RP FUNCTION, COMPOSITION OF THE RITS COMPLEX, AND INTERACTION WITH TAS3.
RX PubMed=14704433; DOI=10.1126/science.1093686;
RA Verdel A., Jia S., Gerber S., Sugiyama T., Gygi S.P., Grewal S.I.S.,
RA Moazed D.;
RT "RNAi-mediated targeting of heterochromatin by the RITS complex.";
RL Science 303:672-676(2004).
RN [6]
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 [7]
RP INTERACTION WITH DRI1.
RX PubMed=33693625; DOI=10.1093/genetics/iyab032;
RA Ban H., Sun W., Chen Y.H., Chen Y., Li F.;
RT "Dri1 mediates heterochromatin assembly via RNAi and histone
RT deacetylation.";
RL Genetics 217:iyab032-iyab032(2021).
CC -!- FUNCTION: Component of the kinetochore which plays a role in
CC stabilizing microtubules and so allowing accurate chromosome
CC segregation. Has a role in the RNA interference (RNAi) pathway which is
CC important for heterochromatin formation and accurate chromosome
CC segregation. A member of the RNA-induced transcriptional silencing
CC (RITS) complex which is involved in the biosynthesis of dsRNA from
CC primer siRNAs provided by the RNA-directed RNA polymerase (RDRC)
CC complex. {ECO:0000269|PubMed:10835380, ECO:0000269|PubMed:14704433,
CC ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:9722643}.
CC -!- SUBUNIT: Ago1, chp1 and tas3 interact to form the core of the RNA-
CC induced transcriptional silencing (RITS) complex. The RITS complex
CC interacts with the RDRC complex via interaction between ago1 and hrr1.
CC Clr4 has a role in mediating this interaction (PubMed:14704433).
CC Interacts with dri1 (PubMed:33693625). {ECO:0000269|PubMed:14704433,
CC ECO:0000269|PubMed:33693625}.
CC -!- INTERACTION:
CC Q10103; Q10426: rik1; NbExp=2; IntAct=EBI-421832, EBI-1111936;
CC Q10103; O94687: tas3; NbExp=10; IntAct=EBI-421832, EBI-423002;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15607976,
CC ECO:0000269|PubMed:9722643}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:9722643}.
CC Note=Associates with telomeric and mating-type region heterochromatin
CC (PubMed:15607976).
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DR EMBL; CU329670; CAA92382.1; -; Genomic_DNA.
DR PIR; T37916; T37916.
DR RefSeq; NP_593666.1; NM_001019098.2.
DR PDB; 2RSN; NMR; -; A=1-75.
DR PDB; 3G7L; X-ray; 2.20 A; A=15-75.
DR PDB; 3TIX; X-ray; 2.90 A; B/D=504-960.
DR PDBsum; 2RSN; -.
DR PDBsum; 3G7L; -.
DR PDBsum; 3TIX; -.
DR AlphaFoldDB; Q10103; -.
DR BMRB; Q10103; -.
DR SMR; Q10103; -.
DR BioGRID; 278711; 120.
DR DIP; DIP-29301N; -.
DR IntAct; Q10103; 5.
DR STRING; 4896.SPAC18G6.02c.1; -.
DR iPTMnet; Q10103; -.
DR MaxQB; Q10103; -.
DR PaxDb; Q10103; -.
DR PRIDE; Q10103; -.
DR EnsemblFungi; SPAC18G6.02c.1; SPAC18G6.02c.1:pep; SPAC18G6.02c.
DR GeneID; 2542239; -.
DR KEGG; spo:SPAC18G6.02c; -.
DR PomBase; SPAC18G6.02c; chp1.
DR VEuPathDB; FungiDB:SPAC18G6.02c; -.
DR eggNOG; KOG1911; Eukaryota.
DR HOGENOM; CLU_307797_0_0_1; -.
DR InParanoid; Q10103; -.
DR OMA; WYDNTWE; -.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR EvolutionaryTrace; Q10103; -.
DR PRO; PR:Q10103; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0034507; C:chromosome, centromeric outer repeat region; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0030958; C:RITS complex; IDA:PomBase.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0042393; F:histone binding; IDA:PomBase.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; TAS:PomBase.
DR IDEAL; IID50149; -.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR035979; RBD_domain_sf.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Chromosome partition; Cytoplasm; Cytoskeleton;
KW DNA-binding; Nucleus; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..960
FT /note="Chromo domain-containing protein 1"
FT /id="PRO_0000080238"
FT DOMAIN 22..74
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2RSN"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:3G7L"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2RSN"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3G7L"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3G7L"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3G7L"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3G7L"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:2RSN"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:3G7L"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:3TIX"
FT TURN 527..530
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 531..539
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 541..544
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 550..558
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 570..576
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 589..595
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 596..606
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 608..613
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 618..623
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 627..632
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 641..648
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 653..660
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 675..682
FT /evidence="ECO:0007829|PDB:3TIX"
FT TURN 687..691
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 707..718
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 723..727
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 731..734
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 736..744
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 745..747
FT /evidence="ECO:0007829|PDB:3TIX"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 751..753
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 757..762
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 766..771
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 804..808
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 812..816
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 818..823
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 827..837
FT /evidence="ECO:0007829|PDB:3TIX"
FT TURN 838..841
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 842..846
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 850..861
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 867..882
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 889..891
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 903..918
FT /evidence="ECO:0007829|PDB:3TIX"
FT TURN 919..921
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 923..928
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 932..934
FT /evidence="ECO:0007829|PDB:3TIX"
FT STRAND 941..944
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 946..952
FT /evidence="ECO:0007829|PDB:3TIX"
SQ SEQUENCE 960 AA; 108726 MW; E92C16BBD0D5957C CRC64;
MVSVKPLPDI DSNEGETDAD VYEVEDILAD RVNKNGINEY YIKWAGYDWY DNTWEPEQNL
FGAEKVLKKW KKRKKLIAKG LLEPFDAEDN EAKKMKREKE ILRQQRQKRK SELTQLSQKV
KEKFKKMRKK PARRIVTIAN DEEEEDDQTM DEDAFERKSM QGELKERNLT DKTSTLSTSF
GETSPDVNPF YLSEWPTVTD SILLSKSLSS DAIPLKNGEI KSTMLMPSDS DNSVPGIQNS
NNLENTGAFV ENANSPQSNT PLSTFRHSSP LSLSPVITSD NDVANSLFFS NSTPLPSSLK
IKKEAPKLET HTILVSDNSG SLTKQDILSY FAFIKGNIEV FFLKSPKKDK VCNMAYIQFD
SIEQAKLAYD KGHPSWHVTL VKGKISTDME ECKVSKSILK TTPSKKANAR SVSFTQTTTD
TLSESEKFAS NVDLDENFDF NVNVTNEDAK QLKKSVIGSS WTTVNNDWNS VSKSDQTFEN
DGASKVVPAG NITLNSDNSL HHSISESEDL SSASTLSDYF RFVLRVGKSL YYAGELSFDI
SKLKAETEHQ QLLRSLVSCK QVDVLRFVTS QYLEVFGTCL TKVLSGSLCI RSDVDMTHFK
NILNRGNGAG IVLGSNYTLL LFTEDNNALM NLYDCQGQSN SPFWMVIFEP LESILVEWSA
KNLRPKKPYH KSQSYLSYLL QLGHIDLHKI GAFQATQILI VSKQPSPEAE ELEDTFREAA
IPTFRGLEIP ESLFLSQNVF VFLNVSLEDD FDQLQFLTLA KRKSCKFFLF GLSLPLKSPN
DSHVGTDFKK NNEPLDKLTY SQYLRPMFPK GGVVSVTLSA LIKTPRLLEL ISPFLEIKKD
SWILILPPSI VDMVKSYFVT NNPDKSLLEI QNLLNTLQRY LTNPALKNVT LYQDWDIVID
DSADVSLAST LQLYQKKNYD KYRRFVLIHE LKNELTPVNG LDIVDYDEFK ETFMRAIGLK
