SAP1_SCHPO
ID SAP1_SCHPO Reviewed; 254 AA.
AC P40847; P78961;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Switch-activating protein 1;
GN Name=sap1; ORFNames=SPCC1672.02c;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 90-102; 163-179 AND
RP 189-208, AND FUNCTION.
RX PubMed=8114737; DOI=10.1128/mcb.14.3.2058-2065.1994;
RA Arcangioli B., Copeland T.D., Klar A.J.S.;
RT "Sap1, a protein that binds to sequences required for mating-type
RT switching, is essential for viability in Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 14:2058-2065(1994).
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).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND LEVEL OF PROTEIN EXPRESSION.
RX PubMed=14555473; DOI=10.1128/ec.2.5.910-921.2003;
RA de Lahondes R., Ribes V., Arcangioli B.;
RT "Fission yeast Sap1 protein is essential for chromosome stability.";
RL Eukaryot. Cell 2:910-921(2003).
RN [4]
RP FUNCTION.
RX PubMed=16166653; DOI=10.1128/mcb.25.19.8755-8761.2005;
RA Mejia-Ramirez E., Sanchez-Gorostiaga A., Krimer D.B., Schvartzman J.B.,
RA Hernandez P.;
RT "The mating type switch-activating protein Sap1 Is required for replication
RT fork arrest at the rRNA genes of fission yeast.";
RL Mol. Cell. Biol. 25:8755-8761(2005).
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Binds to sequences required for mating-type switching. Makes
CC a simultaneous contact with both the alpha and beta domains of the
CC switch-activating site SAS1. Also binds to replication fork barrier 1
CC (RFB1) located within a 78 base pair sequence near the 3' end of the
CC rRNA coding region. This leads to replication fork blockage. It binds
CC the consensus sequence 5'-TA[AG]GCAGNTN[CT]AACG[AC]G-3'.
CC -!- FUNCTION: Has a role in chromosome organization and integrity where it
CC is involved in chromosome segregation. Has a role in sister chromatid
CC cohesion and condensation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14555473}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14555473,
CC ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The N-terminus may contain the DNA-binding domain. Last 40
CC residues of the C-terminus are required for chromosome segregation.
CC -!- MISCELLANEOUS: Present with 20000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14555473}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77578; CAA54684.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20440.1; -; Genomic_DNA.
DR PIR; A56214; A56214.
DR PIR; T45515; T45515.
DR RefSeq; NP_587873.1; NM_001022865.2.
DR PDB; 5B7J; NMR; -; A=25-135.
DR PDB; 5JDK; X-ray; 1.00 A; A=1-135.
DR PDB; 6EXT; X-ray; 1.50 A; A=18-133.
DR PDB; 6EXU; X-ray; 1.41 A; A=18-133.
DR PDBsum; 5B7J; -.
DR PDBsum; 5JDK; -.
DR PDBsum; 6EXT; -.
DR PDBsum; 6EXU; -.
DR AlphaFoldDB; P40847; -.
DR SMR; P40847; -.
DR BioGRID; 275853; 21.
DR STRING; 4896.SPCC1672.02c.1; -.
DR iPTMnet; P40847; -.
DR MaxQB; P40847; -.
DR PaxDb; P40847; -.
DR PRIDE; P40847; -.
DR EnsemblFungi; SPCC1672.02c.1; SPCC1672.02c.1:pep; SPCC1672.02c.
DR GeneID; 2539285; -.
DR KEGG; spo:SPCC1672.02c; -.
DR PomBase; SPCC1672.02c; sap1.
DR VEuPathDB; FungiDB:SPCC1672.02c; -.
DR HOGENOM; CLU_1050352_0_0_1; -.
DR OMA; IHTESAC; -.
DR PRO; PR:P40847; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0008301; F:DNA binding, bending; IDA:PomBase.
DR GO; GO:0043110; F:rDNA spacer replication fork barrier binding; IDA:PomBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR GO; GO:1902985; P:mitotic pre-replicative complex assembly; IMP:CACAO.
DR GO; GO:0031582; P:replication fork arrest at rDNA repeats; IDA:PomBase.
DR GO; GO:0071170; P:site-specific DNA replication termination; IDA:PomBase.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome partition; Direct protein sequencing; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..254
FT /note="Switch-activating protein 1"
FT /id="PRO_0000097581"
FT REPEAT 221..224
FT /note="1"
FT REPEAT 225..228
FT /note="2"
FT REPEAT 229..232
FT /note="3"
FT REPEAT 233..236
FT /note="4"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..236
FT /note="4 X 4 AA tandem repeats of G-[ATV]-N-M"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:5JDK"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5JDK"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:5JDK"
FT HELIX 78..98
FT /evidence="ECO:0007829|PDB:5JDK"
FT HELIX 107..131
FT /evidence="ECO:0007829|PDB:5JDK"
SQ SEQUENCE 254 AA; 29127 MW; 570DCE20C3C20847 CRC64;
MEAPKMELKS YKRKNASLSP SSSPAKAQRT HLSLEEKIKL MRLVVRHKHE LVDRKTSEFY
AKIARIGYED EGLAIHTESA CRNQIISIMR VYEQRLAHRQ PGMKTTPEED ELDQLCDEWK
ARLSELQQYR EKFLVGKRKC DCNDEINERL KKLTEEQQNV DMLVAKVNFL SKHLHDNEEK
LMQVNAKMDE VLAENKRLQQ LLDHNDLLSK LEPPSAYAPH GVNMGTNMGA NMGANMNAIR
GGLHSSISPN LGDH
