RIF1_SCHPO
ID RIF1_SCHPO Reviewed; 1400 AA.
AC Q96UP3; O14247; Q9P7P5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Telomere length regulator protein rif1;
GN Name=rif1; ORFNames=SPAC6F6.17, SPAPJ736.01;
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 [MRNA], FUNCTION, INTERACTION WITH TAZ1, AND
RP SUBCELLULAR LOCATION.
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 [2]
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).
CC -!- FUNCTION: Negatively regulates telomere length. Appears to play no role
CC in transcriptional silencing of telomeric loci.
CC {ECO:0000269|PubMed:11676925}.
CC -!- SUBUNIT: Recruited to telomeres by interaction with taz1. Does not
CC interact with rap1, unlike the orthologous protein of budding yeast.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11676925}.
CC Chromosome, telomere {ECO:0000269|PubMed:11676925}. Note=Localized to
CC telomeres. This interaction may be increased by perturbation of
CC telomere structure, for instance by loss of the rap1 protein.
CC -!- SIMILARITY: Belongs to the RIF1 family. {ECO:0000305}.
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DR EMBL; AY034033; AAK57741.1; -; mRNA.
DR EMBL; CU329670; CAB11739.2; -; Genomic_DNA.
DR PIR; T39050; T39050.
DR PIR; T50299; T50299.
DR RefSeq; NP_593910.2; NM_001019340.2.
DR AlphaFoldDB; Q96UP3; -.
DR BioGRID; 278620; 17.
DR STRING; 4896.SPAC6F6.17.1; -.
DR iPTMnet; Q96UP3; -.
DR MaxQB; Q96UP3; -.
DR PaxDb; Q96UP3; -.
DR PRIDE; Q96UP3; -.
DR EnsemblFungi; SPAC6F6.17.1; SPAC6F6.17.1:pep; SPAC6F6.17.
DR GeneID; 2542144; -.
DR KEGG; spo:SPAC6F6.17; -.
DR PomBase; SPAC6F6.17; rif1.
DR VEuPathDB; FungiDB:SPAC6F6.17; -.
DR eggNOG; ENOG502QSZW; Eukaryota.
DR HOGENOM; CLU_005497_0_0_1; -.
DR InParanoid; Q96UP3; -.
DR OMA; HVPQIWS; -.
DR PhylomeDB; Q96UP3; -.
DR PRO; PR:Q96UP3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0140463; F:chromatin-protein adaptor; EXP:PomBase.
DR GO; GO:0051880; F:G-quadruplex DNA binding; EXP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0101018; P:negative regulation of mitotic DNA replication initiation from late origin; IMP:PomBase.
DR GO; GO:0062212; P:regulation of mitotic DNA replication initiation from early origin; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028566; Rif1.
DR InterPro; IPR022031; Rif1_N.
DR PANTHER; PTHR22928; PTHR22928; 1.
DR Pfam; PF12231; Rif1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..1400
FT /note="Telomere length regulator protein rif1"
FT /id="PRO_0000097335"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 155835 MW; C279D8168CC940F0 CRC64;
MTKEIAVKEA SNMLLQEPST PSSQAVGLSS SPSSSIRKKK VNFSSELENS PGGNRPSFGL
PKRGILKTST PLSSIKQPNF QSFEGNESEK ETSLQELQSS FCSGIENLQH VEKSARIETY
SKLSSFLKIY TPSLPEDPIF PLLNQLCNFL LSDRCSNNSE GSPDFQLNTQ ANKLLSILLW
HPTISSHIQP ETATVFIEQS LNFLEGPKLT KALAAQHLHL LSCQKCPLSI HPLCNRILDV
CFNISFPSLV IGQERLAVLT KILSQFPLEF SRRVVDWAPY LLACLVDASR PIREKALLLA
LDLSKHLYHD KLVARTILAN FRSDIKGTAF VLIMTEQFEK LVIEEDDGVY VAHAWAAIIS
VLGGARISSW EYFNTWLKII QLCFNSMNPL TKCAAQTSWI RLIHEFSLSE TLTQATKRLT
LLCQPISMVL GSRNLPTVKN AAMTTLIALI YACLRPGISD AMLSLLWDSV IVNILEKCAL
KNEVTIFESS NILLALFNTL SNGVWKDDRL VCRESVEAKE LPKLNPVWVR ANCSRTIEPV
KTLLLLAKPD HTVKTTTPAR KQHIRGLSYE QSSSVWSTYI KCLASAGQKE IKRSVETGRA
ICCICSSLHK FLYSKSIRKD ELYVERVSRF ALMVKSAIEA FGINTFVEAS YLVSDNQLVL
IDQTKAIDSY DHVPISPLIY LLHSLALLTN GTLFSTVHAA YSSILSSIEE YHLRFGLKLM
LLWDCVSPLS DDGTLVLARV LVSHEVSRLT SEALLSELKS RNGNNSVEEG FSEEERSILL
KLLSWNVKFC SISDAGSVNN LLQQYFTAIY KFEGCGSVFP FVVDPFTTIL DDVLSFEANK
VYSFAISLMK VSTFESCTKE LPPVTLPENI RQHLDSYNHM VELYNTLLQR LSSSDQVDLQ
CRYLHELSEF IKKIPKEFIF HTICKLSKGL IPCFLMNAFP QLEKSTTLQK SCTNFCILIL
QLLLNSTATA SNILESLSPL LTSGLKSISK EVVLAAIKFW NQVFGKFESE EYPIELQKTI
SYLSKTYIIL LPFQSLCPGG KQANHQSSEK MSDILKGVDE LRSVSKNGPY ASSQDKGEKT
TEFSGPGKPN NDNYIQIASV QELDDSSKGK AGKMPASKKN KRQKGDVKKI DETKNEATDM
EESLTTPSGK VNKEVIVDDT SLRDEAIVPD KAIDVADNSN ALLKENISSQ SNRKADNNGT
PSVNNSFTTA NNDECSKENS QIEPEGQTAS REGVLSTPRS TRKKRKLGRK SQSSNVNKEV
AISEVSATLE NVEVIERHGI SEQGQNLDES ACVLTNESSL SQTEIPEEKT ENETTAVNGF
ENSKKRQFSS LLSGSIDTNN ESNKVSSVEF DKSGPQDIIQ SMTEATFEIE KNIQDLKSEE
VQKLSDLLMR LQRAILSRIA
