SMC2_MOUSE
ID SMC2_MOUSE Reviewed; 1191 AA.
AC Q8CG48; Q52KE9; Q61076; Q9CS17; Q9CSD8;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE Short=SMC protein 2;
DE Short=SMC-2;
DE AltName: Full=Chromosome-associated protein E;
DE AltName: Full=FGF-inducible protein 16;
DE AltName: Full=XCAP-E homolog;
GN Name=Smc2; Synonyms=Cape, Fin16, Smc2l1;
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] OF 1-284.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 562-570, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 801-1191.
RX PubMed=8649829;
RA Guthridge M.A., Seldin M., Basilico C.;
RT "Induction of expression of growth-related genes by FGF-4 in mouse
RT fibroblasts.";
RL Oncogene 12:1267-1278(1996).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1160, 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 SMC4. 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 Q8CG48; Q8BH43: Wasf2; NbExp=4; IntAct=EBI-643436, EBI-643162;
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 SMC4, forming a
CC V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB08867.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ534939; CAD59182.1; -; mRNA.
DR EMBL; AK013109; BAB28654.1; -; mRNA.
DR EMBL; AK019977; BAB31946.1; -; mRNA.
DR EMBL; AL732619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02299.1; -; Genomic_DNA.
DR EMBL; BC094380; AAH94380.1; -; mRNA.
DR EMBL; U42385; AAB08867.1; ALT_INIT; mRNA.
DR CCDS; CCDS18180.1; -.
DR RefSeq; NP_001288341.1; NM_001301412.1.
DR RefSeq; NP_032043.3; NM_008017.4.
DR PDB; 3L51; X-ray; 1.51 A; A=506-666.
DR PDBsum; 3L51; -.
DR AlphaFoldDB; Q8CG48; -.
DR SMR; Q8CG48; -.
DR BioGRID; 199677; 28.
DR ComplexPortal; CPX-980; Condensin I complex.
DR ComplexPortal; CPX-986; Condensin II complex.
DR CORUM; Q8CG48; -.
DR IntAct; Q8CG48; 4.
DR MINT; Q8CG48; -.
DR STRING; 10090.ENSMUSP00000099979; -.
DR iPTMnet; Q8CG48; -.
DR PhosphoSitePlus; Q8CG48; -.
DR SwissPalm; Q8CG48; -.
DR EPD; Q8CG48; -.
DR MaxQB; Q8CG48; -.
DR PaxDb; Q8CG48; -.
DR PeptideAtlas; Q8CG48; -.
DR PRIDE; Q8CG48; -.
DR ProteomicsDB; 257263; -.
DR Antibodypedia; 14701; 271 antibodies from 33 providers.
DR DNASU; 14211; -.
DR Ensembl; ENSMUST00000102915; ENSMUSP00000099979; ENSMUSG00000028312.
DR Ensembl; ENSMUST00000117280; ENSMUSP00000113940; ENSMUSG00000028312.
DR GeneID; 14211; -.
DR KEGG; mmu:14211; -.
DR UCSC; uc008swk.2; mouse.
DR CTD; 10592; -.
DR MGI; MGI:106067; Smc2.
DR VEuPathDB; HostDB:ENSMUSG00000028312; -.
DR eggNOG; KOG0933; Eukaryota.
DR GeneTree; ENSGT00550000074857; -.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; Q8CG48; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 119789at2759; -.
DR PhylomeDB; Q8CG48; -.
DR TreeFam; TF101157; -.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
DR BioGRID-ORCS; 14211; 27 hits in 79 CRISPR screens.
DR ChiTaRS; Smc2; mouse.
DR EvolutionaryTrace; Q8CG48; -.
DR PRO; PR:Q8CG48; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CG48; protein.
DR Bgee; ENSMUSG00000028312; Expressed in pharyngeal arch 2 and 278 other tissues.
DR ExpressionAtlas; Q8CG48; baseline and differential.
DR Genevisible; Q8CG48; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:ComplexPortal.
DR GO; GO:0000796; C:condensin complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO: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; ISO:MGI.
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; cd03273; ABC_SMC2_euk; 1.
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; IPR027120; Smc2_ABC.
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; Direct protein sequencing;
KW DNA condensation; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1191
FT /note="Structural maintenance of chromosomes protein 2"
FT /id="PRO_0000118996"
FT DOMAIN 521..640
FT /note="SMC hinge"
FT COILED 173..507
FT /evidence="ECO:0000255"
FT COILED 672..936
FT /evidence="ECO:0000255"
FT COILED 963..1031
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95347"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95347"
FT MOD_RES 677
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95347"
FT MOD_RES 1158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95347"
FT MOD_RES 1160
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 62
FT /note="L -> F (in Ref. 1; CAD59182)"
FT /evidence="ECO:0000305"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 538..545
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 557..566
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:3L51"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 588..598
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 617..624
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:3L51"
FT HELIX 633..641
FT /evidence="ECO:0007829|PDB:3L51"
FT TURN 643..645
FT /evidence="ECO:0007829|PDB:3L51"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:3L51"
SQ SEQUENCE 1191 AA; 134239 MW; 56CC351A7855D0BB CRC64;
MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS
NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEAHDE ITVTRQVVIG GRNKYLINGV
NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA
AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL
RAEDTKERSA GELKEMQDKI VNLQEVLSEN EKKIKALNCE IEELERRKDK ETGGKLKSLE
DACAEAQRVN TKSQSAFDLK KKNLASEETK RKELQNSMAE DSKALAAKEK EVKKITDGLH
GLQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMIACKNDIS KAQTEAKQAQ
MKLKHAQQEL KSKQAEVKKM DSGYKKDQDA FEAVKKAKEK LETEMKKLNY EENKEEKLLE
KHRQLSRDIN NLKGKHEALL AKFPNLQFAY KDPEKNWNRN SVKGLVASLI NVKDNSTATA
LEVVAGERLY NVVVDTEVTA KKLLEKGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP
DNVHVALSLV DYKPELQKGM EFVFGTTFVC NNMDNAKKVA FDKRIMTRTV TLGGDVFDPH
GTLSGGARSQ AASILTKFQE VKDVQDELRT KENELRALEE ELAGLKNVAE KYRQLKQQWE
MKTEEGDLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK STKEIQKKAE EKYEALENKM
KNAEAEREKE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHASNEQQL
DAVNEAIKAY EGQIEKMAAE VAKNKESVNK AQDELMKQKQ IITAQDNIIK DKCAEVAKHN
LQNNESQLKI KELDHSISKH KREADDAAAK VSKMLSDYDW INAEKHLFGQ PNSAYDFKTN
NPKEAGQRLQ KLQEVKEKLG RNVNLRAMNV LTEAEERYND LMKKKRIVEN DKSKILATIE
DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE
NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF
IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQSQAGKIP KEAKSRGKEP N
