SCC4_YEAST
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 03-AUG-2022, entry version 163.
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}.
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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; 337.
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; P40090; -.
DR PRIDE; P40090; -.
DR EnsemblFungi; YER147C_mRNA; YER147C; YER147C.
DR GeneID; 856890; -.
DR KEGG; sce:YER147C; -.
DR SGD; S000000949; SCC4.
DR VEuPathDB; FungiDB:YER147C; -.
DR eggNOG; ENOG502QQXI; Eukaryota.
DR HOGENOM; CLU_409364_0_0_1; -.
DR InParanoid; P40090; -.
DR OMA; SYLVNCY; -.
DR BioCyc; YEAST:G3O-30308-MON; -.
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:1905309; P:positive regulation of cohesin loading; IDA:ComplexPortal.
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; A-
FT 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; D-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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
