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   27-MAR-2024, entry version 170.
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; 23.
DR   ComplexPortal; CPX-980; Condensin I complex.
DR   ComplexPortal; CPX-986; Condensin II complex.
DR   CORUM; Q8CG47; -.
DR   IntAct; Q8CG47; 12.
DR   MINT; Q8CG47; -.
DR   STRING; 10090.ENSMUSP00000047872; -.
DR   GlyGen; Q8CG47; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8CG47; -.
DR   PhosphoSitePlus; Q8CG47; -.
DR   SwissPalm; Q8CG47; -.
DR   EPD; Q8CG47; -.
DR   jPOST; Q8CG47; -.
DR   MaxQB; Q8CG47; -.
DR   PaxDb; 10090-ENSMUSP00000047872; -.
DR   PeptideAtlas; Q8CG47; -.
DR   ProteomicsDB; 261520; -.
DR   Pumba; Q8CG47; -.
DR   Antibodypedia; 18504; 281 antibodies from 35 providers.
DR   DNASU; 70099; -.
DR   Ensembl; ENSMUST00000042901.15; ENSMUSP00000047872.9; ENSMUSG00000034349.15.
DR   GeneID; 70099; -.
DR   KEGG; mmu:70099; -.
DR   UCSC; uc008pma.1; mouse.
DR   AGR; MGI:1917349; -.
DR   CTD; 10051; -.
DR   MGI; MGI:1917349; Smc4.
DR   VEuPathDB; HostDB:ENSMUSG00000034349; -.
DR   eggNOG; KOG0996; Eukaryota.
DR   GeneTree; ENSGT00900000141094; -.
DR   InParanoid; Q8CG47; -.
DR   OMA; CPALDNM; -.
DR   OrthoDB; 231904at2759; -.
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 80 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 283 other cell types or tissues.
DR   ExpressionAtlas; Q8CG47; baseline and differential.
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   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   Genevisible; Q8CG47; MM.
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
//