RAP1_SCHPO
ID RAP1_SCHPO Reviewed; 693 AA.
AC Q96TL7; Q9UTW1; Q9UU15;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=DNA-binding protein rap1;
GN Name=rap1; ORFNames=SPBC1778.02;
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 [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11676924; DOI=10.1016/s0960-9822(01)00457-2;
RA Chikashige Y., Hiraoka Y.;
RT "Telomere binding of the Rap1 protein is required for meiosis in fission
RT yeast.";
RL Curr. Biol. 11:1618-1623(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX PubMed=11676925; DOI=10.1016/s0960-9822(01)00503-6;
RA Kanoh J., Ishikawa F.;
RT "spRap1 and spRif1, recruited to telomeres by Taz1, are essential for
RT telomere function in fission yeast.";
RL Curr. Biol. 11:1624-1630(2001).
RN [3]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH BQT4.
RX PubMed=19948484; DOI=10.1083/jcb.200902122;
RA Chikashige Y., Yamane M., Okamasa K., Tsutsumi C., Kojidani T., Sato M.,
RA Haraguchi T., Hiraoka Y.;
RT "Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to
RT ensure chromosomal bouquet formation.";
RL J. Cell Biol. 187:413-427(2009).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 164-312.
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).
CC -!- FUNCTION: Involved in the regulation of telomere length, clustering and
CC has a specific role in telomere position effect (TPE). Unlike yeast,
CC exhibits no effect in transcription regulation.
CC {ECO:0000269|PubMed:11676924, ECO:0000269|PubMed:11676925,
CC ECO:0000269|PubMed:19948484}.
CC -!- SUBUNIT: Interacts with bqt4 and taz1. Unlike yeast does not interact
CC with rif1. {ECO:0000269|PubMed:11676924, ECO:0000269|PubMed:11676925,
CC ECO:0000269|PubMed:19948484}.
CC -!- INTERACTION:
CC Q96TL7; P79005: taz1; NbExp=5; IntAct=EBI-929794, EBI-15903288;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC Chromosome, telomere {ECO:0000269|PubMed:11676924,
CC ECO:0000269|PubMed:19948484}.
CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}.
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DR EMBL; AB061738; BAB70735.1; -; Genomic_DNA.
DR EMBL; AY034032; AAK57740.1; -; mRNA.
DR EMBL; CU329671; CAC39280.1; -; Genomic_DNA.
DR EMBL; AB027870; BAA87174.1; -; Genomic_DNA.
DR EMBL; AB027963; BAA87267.1; -; Genomic_DNA.
DR RefSeq; NP_596285.1; NM_001022207.2.
DR PDB; 2L3N; NMR; -; A=639-693.
DR PDB; 5WE0; X-ray; 2.30 A; C/F/I/L=467-496.
DR PDB; 5WE2; X-ray; 2.50 A; F=467-496.
DR PDB; 5YC2; X-ray; 2.70 A; B/D=498-512.
DR PDBsum; 2L3N; -.
DR PDBsum; 5WE0; -.
DR PDBsum; 5WE2; -.
DR PDBsum; 5YC2; -.
DR AlphaFoldDB; Q96TL7; -.
DR BMRB; Q96TL7; -.
DR SMR; Q96TL7; -.
DR BioGRID; 276652; 92.
DR DIP; DIP-35567N; -.
DR IntAct; Q96TL7; 3.
DR STRING; 4896.SPBC1778.02.1; -.
DR iPTMnet; Q96TL7; -.
DR MaxQB; Q96TL7; -.
DR PaxDb; Q96TL7; -.
DR PRIDE; Q96TL7; -.
DR EnsemblFungi; SPBC1778.02.1; SPBC1778.02.1:pep; SPBC1778.02.
DR GeneID; 2540115; -.
DR KEGG; spo:SPBC1778.02; -.
DR PomBase; SPBC1778.02; rap1.
DR VEuPathDB; FungiDB:SPBC1778.02; -.
DR HOGENOM; CLU_397488_0_0_1; -.
DR InParanoid; Q96TL7; -.
DR OMA; AESWREH; -.
DR Reactome; R-SPO-174437; Removal of the Flap Intermediate from the C-strand.
DR EvolutionaryTrace; Q96TL7; -.
DR PRO; PR:Q96TL7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0110092; C:nucleus leading edge; IDA:PomBase.
DR GO; GO:0070187; C:shelterin complex; IPI:PomBase.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0032121; P:meiotic attachment of telomeric heterochromatin to spindle pole body; IMP:PomBase.
DR GO; GO:0044820; P:mitotic telomere tethering at nuclear periphery; IMP:PomBase.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IGI:PomBase.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IBA:GO_Central.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR015280; Rap1_DNA-bd.
DR InterPro; IPR039595; TE2IP/Rap1.
DR PANTHER; PTHR16466; PTHR16466; 1.
DR Pfam; PF09197; Rap1-DNA-bind; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Telomere.
FT CHAIN 1..693
FT /note="DNA-binding protein rap1"
FT /id="PRO_0000097171"
FT DOMAIN 14..105
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 484..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:5YC2"
FT HELIX 647..662
FT /evidence="ECO:0007829|PDB:2L3N"
FT HELIX 666..676
FT /evidence="ECO:0007829|PDB:2L3N"
FT HELIX 680..688
FT /evidence="ECO:0007829|PDB:2L3N"
SQ SEQUENCE 693 AA; 79527 MW; 77C5070697D1A9CF CRC64;
MSFTFTKSDG SSILFAVSKN FEHIRGFKNA IDCFKGKIEF LSFDKVDPTK HDYYLVAEDE
RVSDLDIPKG FFERNPEFRH KMLKIAWITQ CIEQGKLLPT ESFEVELNQD DVNRTHDGFR
KRELFTLEDE KILIDHVHKN DINRFGTKVY EELARKYPQH SLESWRQHYK YMKKRLPPVS
DSDESNYCQR IIVKPYSSQK DYTQSTHEQT LSSPISKSAS VSKSENKALV NNKRYSDSYF
YFSKMRRISI DVDYVDEDLN LINAYLSQFG KKRSLNELCA LLSRRFSNRH TFSEWRALFM
HFFPFINSEG VDPAILSDRE TSAMLDETSD NEVADIDDQM IERKYLFSAS EPNTVKSTNR
LIFSERKAYA ADDSIDNTPS KVPIVNSLSD PRTNRPFFYS NPDSMYRSIS NPLHLVDSQH
LSPLNRKTHF NNPIGQPQFT CLDDHEKTLR ETSFRSLDDM SLRKSNSDNI FVKPGEDLEI
PLLSDYSDSE NISEKSSDDE EAFEKQVTSS YSSPIKVKSQ GKSSKGSSGL DVREHEGSDD
DAEVFVDRSP ESFGATKVAH TSLEGNAASH KKVEENMQQP VTKKQKKYRM VNEEAHTGPT
IIIPSDNNEK VTTLPAGHVP SEEKGKFINL AMHELQNEVS ILRSSVNHRE VDEAIDNILR
YTNSTEQQFL EAMESTGGRV RIAIAKLLSK QTS
