SMC4_MOUSE
ID SMC4_MOUSE Reviewed; 1286 AA.
AC Q8CG47; Q8BTS7; Q8BTY9; Q99K21;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE Short=SMC protein 4;
DE Short=SMC-4;
DE AltName: Full=Chromosome-associated polypeptide C;
DE AltName: Full=XCAP-C homolog;
GN Name=Smc4; Synonyms=Capc, Smc4l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-602.
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-379, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC2. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three non
CC SMC subunits that probably regulate the complex: BRRN1/CAPH,
CC CNAP1/CAPD2 and CAPG (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8CG47; Q00899: Yy1; NbExp=2; IntAct=EBI-6921575, EBI-6921536;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the
CC condensin complex is found in the cytoplasm, while a minority of the
CC complex is associated with chromatin. A subpopulation of the complex
CC however remains associated with chromosome foci in interphase cells.
CC During mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDC2, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC2, forming a
CC V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; AJ534940; CAD59183.1; -; mRNA.
DR EMBL; BC005507; AAH05507.1; -; mRNA.
DR EMBL; BC062939; AAH62939.1; -; mRNA.
DR EMBL; AK088350; BAC40297.1; -; mRNA.
DR EMBL; AK088846; BAC40608.2; -; mRNA.
DR CCDS; CCDS17401.1; -.
DR RefSeq; NP_598547.1; NM_133786.3.
DR RefSeq; XP_006502109.1; XM_006502046.2.
DR PDB; 3L51; X-ray; 1.51 A; B=595-752.
DR PDBsum; 3L51; -.
DR AlphaFoldDB; Q8CG47; -.
DR SMR; Q8CG47; -.
DR BioGRID; 213863; 22.
DR ComplexPortal; CPX-980; Condensin I complex.
DR ComplexPortal; CPX-986; Condensin II complex.
DR CORUM; Q8CG47; -.
DR IntAct; Q8CG47; 11.
DR MINT; Q8CG47; -.
DR STRING; 10090.ENSMUSP00000047872; -.
DR iPTMnet; Q8CG47; -.
DR PhosphoSitePlus; Q8CG47; -.
DR SwissPalm; Q8CG47; -.
DR EPD; Q8CG47; -.
DR jPOST; Q8CG47; -.
DR MaxQB; Q8CG47; -.
DR PaxDb; Q8CG47; -.
DR PeptideAtlas; Q8CG47; -.
DR PRIDE; Q8CG47; -.
DR ProteomicsDB; 261520; -.
DR Antibodypedia; 18504; 260 antibodies from 35 providers.
DR DNASU; 70099; -.
DR Ensembl; ENSMUST00000042901; ENSMUSP00000047872; ENSMUSG00000034349.
DR GeneID; 70099; -.
DR KEGG; mmu:70099; -.
DR UCSC; uc008pma.1; mouse.
DR CTD; 10051; -.
DR MGI; MGI:1917349; Smc4.
DR VEuPathDB; HostDB:ENSMUSG00000034349; -.
DR eggNOG; KOG0996; Eukaryota.
DR GeneTree; ENSGT00900000141094; -.
DR InParanoid; Q8CG47; -.
DR OMA; QIYIDEC; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; Q8CG47; -.
DR TreeFam; TF101158; -.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
DR BioGRID-ORCS; 70099; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Smc4; mouse.
DR EvolutionaryTrace; Q8CG47; -.
DR PRO; PR:Q8CG47; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8CG47; protein.
DR Bgee; ENSMUSG00000034349; Expressed in late embryo and 279 other tissues.
DR ExpressionAtlas; Q8CG47; baseline and differential.
DR Genevisible; Q8CG47; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:ComplexPortal.
DR GO; GO:0000796; C:condensin complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; TAS:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051383; P:kinetochore organization; IMP:MGI.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:MGI.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; ISO:MGI.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:ComplexPortal.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IMP:ComplexPortal.
DR GO; GO:0000012; P:single strand break repair; TAS:MGI.
DR CDD; cd03274; ABC_SMC4_euk; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041738; SMC4_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Chromosome; Coiled coil; Cytoplasm; DNA condensation; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1286
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000119008"
FT DOMAIN 611..725
FT /note="SMC hinge"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..589
FT /evidence="ECO:0000255"
FT COILED 768..1018
FT /evidence="ECO:0000255"
FT COILED 1068..1133
FT /evidence="ECO:0000255"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 677
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT CONFLICT 454
FT /note="E -> V (in Ref. 2; BAC40608)"
FT /evidence="ECO:0000305"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 628..634
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 640..644
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 646..658
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 691..694
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 700..710
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 714..718
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 719..726
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:3L51"
SQ SEQUENCE 1286 AA; 146895 MW; CFEAD84199C3CEB5 CRC64;
MRRKGTKPST ACHQEEGPPP SQDGAHSDEE MEQPAGEAES AAPAKPPGEE LDNRSLEEIL
NSIPPPPPPA MASEAGAPRL MITHIVNQNF KSYAGEKVLG PFHKRFSCII GPNGSGKSNV
IDSMLFVFGY RAQKIRSKKL SVLIHNSDEH KDIQSCTVEV HFQKIIDKEG DDYEVLPNSN
FYVSRTAYRD STSVYHISGK KKTFKDVGNL LRSHGIDLDH NRFLILQGEV EQIAMMKPKG
QTEHDEGMLE YLEDIIGCGR LNEPIKVLCR RVEILNEHRG EKLNRVKMVE KEKDALEGEK
NIAIEFLTLE NEMFKKKNHI CQYYIYDLQN RIAEITTQKE KIHEDTKEIT EKSNVLSNEM
KAKNSAVKDV EKKLNKVTKF IEQNKEKFTQ LDLEDVQVRE KLKHATSKAK KLEKQLQKDK
EKVEELKSVP AKSKTVINET TTRNNSLEKE REKEEKKLKE VMDSLKQETQ GLQKEKEIQE
KELMGFNKSV NEARSKMEVA QSELDIYLSR HNTAVSQLSK AKEALITASE TLKERKAAIK
DINTKLPQTQ QELKEKEKEL QKLTQEEINL KSLVHDLFQK VEEAKSSLAM NRSRGKVLDA
IIQEKKSGRI PGIYGRLGDL GAIDEKYDIA ISSCCHALDY IVVDSIDTAQ ECVNFLKKHN
IGIATFIGLD KMTVWAKKMS KIQTPENTPR LFDLVKVKNE EIRQAFYFAL RDTLVANNLD
QATRVAYQRD RRWRVVTLQG QIIEQSGTMS GGGSKVMRGR MGSSVIDEIS VEEVNKMESQ
LERHSKQAMQ IQEQKVQHEE AVVKLRHSER DMRNTLEKFA ASIQGLSEQE EYLCVQIKEL
EANVLTTAPD RKQQKLLEEN VSVFKKEYDA VAEKAGKVEA EIKRLHNTII DINNRKLKAQ
QNKLDTINKQ LDECASAITK AQVAIKTADR NLKKAQDSVC RTEKEIKDTE KEINDLKTEL
KNIEDKAEEV INNTKTAETS LPEIQKEHRN LLQELKVIQE NEHALQKDAL SIKLKLEQID
GHISEHNSKI KYWQKEISKI KLHPVEDNPV ETVAVLSQEE LEAIKNPESI TNEIALLEAQ
CREMKPNLGA IAEYKKKEDL YLQRVAELDK ITSERDNFRQ AYEDLRKQRL NEFMAGFYVI
TNKLKENYQM LTLGGDAELE LVDSLDPFSE GIMFSVRPPK KSWKKIFNLS GGEKTLSSLA
LVFALHHYKP TPLYFMDEID AALDFKNVSI VAFYIYEQTK NAQFIIISLR NNMFEISDRL
IGIYKTYNST KSVAVNPKQI ASKGLC
