CST9_YEAST
ID CST9_YEAST Reviewed; 482 AA.
AC Q06032; D6VZ29;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Chromosome stability protein 9;
DE AltName: Full=Molecular zipper protein 3;
GN Name=CST9; Synonyms=ZIP3; OrderedLocusNames=YLR394W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=10454593; DOI=10.1093/nar/27.15.3001;
RA Ouspenski I.I., Elledge S.J., Brinkley B.R.;
RT "New yeast genes important for chromosome integrity and segregation
RT identified by dosage effects on genome stability.";
RL Nucleic Acids Res. 27:3001-3008(1999).
RN [4]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SIC
RP COMPLEX, AND INTERACTION WITH ZIP1; MRE11; RAD51 AND RAD57.
RX PubMed=10943844; DOI=10.1016/s0092-8674(00)00029-5;
RA Agarwal S., Roeder G.S.;
RT "Zip3 provides a link between recombination enzymes and synaptonemal
RT complex proteins.";
RL Cell 102:245-255(2000).
RN [5]
RP FUNCTION OF THE SIC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15035982; DOI=10.1016/s0092-8674(04)00249-1;
RA Fung J.C., Rockmill B., Odell M., Roeder G.S.;
RT "Imposition of crossover interference through the nonrandom distribution of
RT synapsis initiation complexes.";
RL Cell 116:795-802(2004).
RN [6]
RP FUNCTION OF THE SIC COMPLEX.
RX PubMed=15070750; DOI=10.1073/pnas.0400843101;
RA Henderson K.A., Keeney S.;
RT "Tying synaptonemal complex initiation to the formation and programmed
RT repair of DNA double-strand breaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4519-4524(2004).
RN [7]
RP FUNCTION OF THE SIC COMPLEX.
RX PubMed=15805472; DOI=10.1101/gad.1293605;
RA Peoples-Holst T.L., Burgess S.M.;
RT "Multiple branches of the meiotic recombination pathway contribute
RT independently to homolog pairing and stable juxtaposition during meiosis in
RT budding yeast.";
RL Genes Dev. 19:863-874(2005).
CC -!- FUNCTION: Component of the synapsis initiation complex (SIC) necessary
CC for the synaptonemal complex assembly. Stabilizes the ZIP2 component to
CC the chromosomes. The SIC complex loads onto chromosomes and nucleates
CC ZIP1 polymerization, a molecular zipper that acts to bring homologous
CC chromosomes in close apposition, which is required for meiotic
CC crossover. May also be involved in double strand break repair.
CC {ECO:0000269|PubMed:10454593, ECO:0000269|PubMed:10943844,
CC ECO:0000269|PubMed:15035982, ECO:0000269|PubMed:15070750,
CC ECO:0000269|PubMed:15805472}.
CC -!- SUBUNIT: Component of the synapsis initiation complex composed of at
CC least ZIP2, ZIP3, MSH4 and MSH5. Interacts also with ZIP1, MRE11, RAD51
CC and RAD53. {ECO:0000269|PubMed:10943844}.
CC -!- INTERACTION:
CC Q06032; P25301: RAD57; NbExp=2; IntAct=EBI-30044, EBI-14744;
CC Q06032; P31111: ZIP1; NbExp=3; IntAct=EBI-30044, EBI-29645;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Synapsed meiotic
CC chromosomes.
CC -!- INDUCTION: Expressed during meiosis. {ECO:0000269|PubMed:10943844}.
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DR EMBL; U19729; AAB82346.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09695.1; -; Genomic_DNA.
DR PIR; S55950; S55950.
DR RefSeq; NP_013498.3; NM_001182282.3.
DR AlphaFoldDB; Q06032; -.
DR SMR; Q06032; -.
DR BioGRID; 31653; 240.
DR ComplexPortal; CPX-1386; Synapsis initiation complex.
DR DIP; DIP-5875N; -.
DR IntAct; Q06032; 8.
DR STRING; 4932.YLR394W; -.
DR PaxDb; Q06032; -.
DR PRIDE; Q06032; -.
DR EnsemblFungi; YLR394W_mRNA; YLR394W; YLR394W.
DR GeneID; 851110; -.
DR KEGG; sce:YLR394W; -.
DR SGD; S000004386; CST9.
DR VEuPathDB; FungiDB:YLR394W; -.
DR eggNOG; KOG4739; Eukaryota.
DR HOGENOM; CLU_051887_0_0_1; -.
DR InParanoid; Q06032; -.
DR OMA; AHILCSQ; -.
DR BioCyc; YEAST:G3O-32459-MON; -.
DR PRO; PR:Q06032; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06032; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR GO; GO:0106069; C:synapsis initiation complex; IC:ComplexPortal.
DR GO; GO:0000795; C:synaptonemal complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR GO; GO:0035825; P:homologous recombination; IC:ComplexPortal.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0090173; P:regulation of synaptonemal complex assembly; IC:ComplexPortal.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
DR InterPro; IPR042123; Zip3/RNF212-like.
DR PANTHER; PTHR22663; PTHR22663; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..482
FT /note="Chromosome stability protein 9"
FT /id="PRO_0000232995"
FT REGION 239..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 53863 MW; DC806A8F9B5EA952 CRC64;
MGGYLAIVFI PQTNTKSMRE KKQKCLKQVR RLSLISPKKY IMPDSIFEQP FVYCGVCHRR
TSHGDPLRLT SCAHILCSQH SPLTSKVCPI CRSSDISIIN LVESKQLPTD IRIFFEPLPP
LLESLYNVSQ FQLNGLSKQC QYYQNHCLKL REKCARQQQL LYQAKIELDS MAILKKRIQE
LESVLNHNNV SSMSVGVLPT RNSHQNHYQP PPTVDLTVDD NSLEEFEAKS FIKKLKKNSS
LRNSSKNNNG TVTPSTSGRV NKNQPLFMET LNNPNRNSIP PPGMNPNANS NLPNISTIAE
STNLNRFSFS PVRVAKGFDG KLPNLDILTN NGSVSSKNIS RLSSASLQPS SPLSSSSNRL
ILPNSNLKEL HHSNTPLTST STQFPSALEK LKITRKRNNT ISGSNRITHN LSSHVRSSGL
AFSSSSNSLQ QSKLPKSNIL KRSNSTQQLT NTHLKSDNHL PPRSSNTVLG SSKKNNKFRR
IR
