ID SCC4_YEAST Reviewed; 624 AA. AC P40090; D3DM54; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=MAU2 chromatid cohesion factor homolog; DE AltName: Full=Sister chromatid cohesion protein 4; GN Name=SCC4; OrderedLocusNames=YER147C; 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=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(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 PROTEIN SEQUENCE OF 390-398, FUNCTION, INTERACTION WITH SCC2, AND RP SUBCELLULAR LOCATION. RX PubMed=10882066; DOI=10.1016/s1097-2765(00)80420-7; RA Ciosk R., Shirayama M., Shevchenko A., Tanaka T., Toth A., Shevchenko A., RA Nasmyth K.; RT "Cohesin's binding to chromosomes depends on a separate complex consisting RT of Scc2 and Scc4 proteins."; RL Mol. Cell 5:243-254(2000). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:25173104}; RX PubMed=25173104; DOI=10.1038/ng.3080; RA Lopez-Serra L., Kelly G., Patel H., Stewart A., Uhlmann F.; RT "The Scc2-Scc4 complex acts in sister chromatid cohesion and RT transcriptional regulation by maintaining nucleosome-free regions."; RL Nat. Genet. 46:1147-1151(2014). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) IN COMPLEX WITH SCC2, AND RP MUTAGENESIS OF LEU-256; TYR-298; LYS-299; TYR-313; PHE-324; LYS-327; RP LYS-331; LYS-540 AND LYS-541. RX PubMed=26038942; DOI=10.7554/elife.06057; RA Hinshaw S.M., Makrantoni V., Kerr A., Marston A.L., Harrison S.C.; RT "Structural evidence for Scc4-dependent localization of cohesin loading."; RL Elife 4:E06057-E06057(2015). CC -!- FUNCTION: Involved in sister chromatid cohesion (PubMed:10882066). CC Forms a complex with SCC2, which is required for the association of the CC cohesin complex with chromosomes (PubMed:10882066, PubMed:26038942). CC Binds to the nucleosome-free promoter regions of ribosomal protein CC genes and tRNA genes (PubMed:25173104). {ECO:0000269|PubMed:10882066, CC ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26038942}. CC -!- SUBUNIT: Interacts with SCC2 to form the cohesin loading complex. CC {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:26038942}. CC -!- INTERACTION: CC P40090; Q04002: SCC2; NbExp=5; IntAct=EBI-16679, EBI-16662; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10882066, CC ECO:0000269|PubMed:25173104}. Note=Associates with chromatin. CC {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:25173104}. CC -!- MISCELLANEOUS: Present with 907 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the SCC4/mau-2 family. {ECO:0000305}. 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; U18917; AAB64674.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07808.1; -; Genomic_DNA. DR PIR; S50650; S50650. DR RefSeq; NP_011074.3; NM_001179037.3. DR PDB; 4XDN; X-ray; 2.08 A; A=1-624. DR PDB; 5W94; X-ray; 3.19 A; A/C=1-624. DR PDBsum; 4XDN; -. DR PDBsum; 5W94; -. DR AlphaFoldDB; P40090; -. DR SMR; P40090; -. DR BioGRID; 36896; 346. DR ComplexPortal; CPX-1868; SCC2-SCC4 cohesin loader complex. DR DIP; DIP-5627N; -. DR IntAct; P40090; 3. DR MINT; P40090; -. DR STRING; 4932.YER147C; -. DR iPTMnet; P40090; -. DR MaxQB; P40090; -. DR PaxDb; 4932-YER147C; -. DR PeptideAtlas; P40090; -. DR EnsemblFungi; YER147C_mRNA; YER147C; YER147C. DR GeneID; 856890; -. DR KEGG; sce:YER147C; -. DR AGR; SGD:S000000949; -. DR SGD; S000000949; SCC4. DR VEuPathDB; FungiDB:YER147C; -. DR eggNOG; ENOG502QQXI; Eukaryota. DR HOGENOM; CLU_409364_0_0_1; -. DR InParanoid; P40090; -. DR OMA; KIASRNC; -. DR OrthoDB; 2016806at2759; -. DR BioCyc; YEAST:G3O-30308-MONOMER; -. DR BioGRID-ORCS; 856890; 9 hits in 10 CRISPR screens. DR PRO; PR:P40090; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P40090; Protein. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0032116; C:SMC loading complex; IPI:SGD. DR GO; GO:0043515; F:kinetochore binding; IDA:SGD. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006302; P:double-strand break repair; IMP:SGD. DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IDA:ComplexPortal. DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:SGD. DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD. DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD. DR InterPro; IPR019440; MAU2. DR Pfam; PF10345; Cohesin_load; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Chromosome partition; KW Direct protein sequencing; Mitosis; Nucleus; Reference proteome. FT CHAIN 1..624 FT /note="MAU2 chromatid cohesion factor homolog" FT /id="PRO_0000193217" FT MUTAGEN 256 FT /note="L->K: In scc4m7; eliminates centromeric localization FT of SCC2 in mitotic cells and reduces association of the FT cohesin subunit SCC1 with the centromere and FT pericentromere; when associated with A-298; D-299; A-313; FT A-324; D-327; and D-331." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 298 FT /note="Y->A: In scc4m7; eliminates centromeric localization FT of SCC2 in mitotic cells and reduces association of the FT cohesin subunit SCC1 with the centromere and FT pericentromere; when associated with K-256; D-299; A-313; FT A-324; D-327; and D-331." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 299 FT /note="K->D: In scc4m7; eliminates centromeric localization FT of SCC2 in mitotic cells and reduces association of the FT cohesin subunit SCC1 with the centromere and FT pericentromere; when associated with K-256; A-298; A-313; FT A-324; D-327; and D-331." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 313 FT /note="Y->A: In scc4m7; eliminates centromeric localization FT of SCC2 in mitotic cells and reduces association of the FT cohesin subunit SCC1 with the centromere and FT pericentromere; when associated with K-256; A-298; D-299; FT A-324; D-327; and D-331." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 324 FT /note="F->A: In scc4m35; eliminates centromeric FT localization of SCC2 in mitotic cells and reduces FT association of the cohesin subunit SCC1 with the centromere FT and pericentromere; when associated with A-327; A-331; FT A-540 and A-541. In scc4m7; eliminates centromeric FT localization of SCC2 in mitotic cells and reduces FT association of the cohesin subunit SCC1 with the centromere FT and pericentromere; when associated with K-256; A-298; FT D-299; A-313; D-327; and D-331." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 327 FT /note="K->A: In scc4m35; eliminates centromeric FT localization of SCC2 in mitotic cells and reduces FT association of the cohesin subunit SCC1 with the centromere FT and pericentromere; when associated with A-324; A-331; FT A-540 and A-541." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 327 FT /note="K->D: In scc4m7; eliminates centromeric localization FT of SCC2 in mitotic cells and reduces association of the FT cohesin subunit SCC1 with the centromere and FT pericentromere; when associated with K-256; A-298; D-299; FT A-313; A-324 and D-331." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 331 FT /note="K->A: In scc4m35; eliminates centromeric FT localization of SCC2 in mitotic cells and reduces FT association of the cohesin subunit SCC1 with the centromere FT and pericentromere; when associated with A-324; A-327; FT A-540 and A-541." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 331 FT /note="K->D: In scc4m7; eliminates centromeric localization FT of SCC2 in mitotic cells and reduces association of the FT cohesin subunit SCC1 with the centromere and FT pericentromere; when associated with K-256; A-298; D-299; FT A-313; A-324 and D-327." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 540 FT /note="K->A: In scc4m35; eliminates centromeric FT localization of SCC2 in mitotic cells and reduces FT association of the cohesin subunit SCC1 with the centromere FT and pericentromere; when associated with A-324; A-327; FT A-331 and A-541." FT /evidence="ECO:0000269|PubMed:26038942" FT MUTAGEN 541 FT /note="K->A: In scc4m35; eliminates centromeric FT localization of SCC2 in mitotic cells and reduces FT association of the cohesin subunit SCC1 with the centromere FT and pericentromere; when associated with A-324; A-327; FT A-331 and A-540." FT /evidence="ECO:0000269|PubMed:26038942" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 10..26 FT /evidence="ECO:0007829|PDB:4XDN" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 34..57 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 62..79 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 83..100 FT /evidence="ECO:0007829|PDB:4XDN" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 107..118 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 120..125 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 128..146 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 151..170 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 174..187 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 193..209 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 215..222 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 231..247 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 253..272 FT /evidence="ECO:0007829|PDB:4XDN" FT TURN 273..275 FT /evidence="ECO:0007829|PDB:4XDN" FT STRAND 278..283 FT /evidence="ECO:0007829|PDB:4XDN" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 293..296 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 298..312 FT /evidence="ECO:0007829|PDB:4XDN" FT TURN 313..318 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 320..341 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 350..379 FT /evidence="ECO:0007829|PDB:4XDN" FT TURN 391..395 FT /evidence="ECO:0007829|PDB:5W94" FT HELIX 396..407 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 413..421 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 427..447 FT /evidence="ECO:0007829|PDB:4XDN" FT TURN 450..452 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 453..471 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 475..478 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 480..494 FT /evidence="ECO:0007829|PDB:4XDN" FT TURN 496..498 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 507..524 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 543..556 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 561..574 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:4XDN" FT STRAND 578..580 FT /evidence="ECO:0007829|PDB:5W94" FT HELIX 582..599 FT /evidence="ECO:0007829|PDB:4XDN" FT HELIX 602..619 FT /evidence="ECO:0007829|PDB:4XDN" SQ SEQUENCE 624 AA; 72141 MW; 1269D931C656E608 CRC64; MENLGDKLSI SQVYHLAQEY RDHAYSIANK IGSEEGLKQY YGLMNMSIQM FQLLKTKCTL SVLEDSKVTF EMVELLIQET YNFDLAELYI SSLKERLQTH QSDTDLVEEI MRCEFLLLHD LPLMRDSKFH YKIALRNCNE LVQYMVNLQD ELYQNWASVF QYVGVMLCIK LKQHRRVKTS FHGLLSQCRE KSQWKWFLNL CYVNYLLNER FPIPEDALQE LRSTELHTVG PELYAWKLAL EMVIQLCKDG NITDHLNEFK NFFDTNKQSL VTNEGKGCVI KIMPRIALKV ELPMIFHYKE LKNILLLLQS VSYIVNCYDE KGNFSRKFLP KVYSTTQKLI KNIAAGGVSM NELDSRIQTY KSILEFCEFY KVWEQTLLKG AVVTTESPKL GPSPGYVRLL QAMKVQFEGG GAVEEYTRLA QSGGTSSEVK MISLLNCYTV QAARVSRCSG DKQGELVEQC NKVWLQVEKL LQETDLQFNP IWECTVTILW LFSHFEPFSW NPLPCSDKQR AEYVSKLREF YSSNKFVAGE AVADNRFKLK KALLLQILVN YLGGRMLEHD LGEIYAISAK CFDMCRQQGG MRKVQYVIGI WHLMNCTVAM RGKDVALTNA KLEALVKQIT SVKQ //