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Q8CG47 (SMC4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 4

Short name=SMC protein 4
Short name=SMC-4
Alternative name(s):
Chromosome-associated polypeptide C
XCAP-C homolog
Gene names
Name:Smc4
Synonyms:Capc, Smc4l1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases By similarity.

Subunit structure

Forms a heterodimer with SMC2. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRRN1/CAPH, CNAP1/CAPD2 and CAPG By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Chromosome By similarity. Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase By similarity.

Domain

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC2, forming a V-shaped heterodimer By similarity.

Sequence similarities

Belongs to the SMC family. SMC4 subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Yy1Q008992EBI-6921575,EBI-6921536

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12861286Structural maintenance of chromosomes protein 4
PRO_0000119008

Regions

Nucleotide binding111 – 1188ATP Potential
Region590 – 767178Flexible hinge
Coiled coil270 – 589320 Potential
Coiled coil768 – 1018251 Potential
Coiled coil1068 – 113366 Potential
Compositional bias64 – 696Poly-Pro
Compositional bias1189 – 122436Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue211Phosphoserine By similarity
Modified residue271Phosphoserine By similarity
Modified residue401Phosphoserine By similarity
Modified residue1411Phosphoserine By similarity
Modified residue3791N6-acetyllysine Ref.4
Modified residue6771N6-acetyllysine By similarity

Experimental info

Sequence conflict4541E → V in BAC40608. Ref.2

Secondary structure

................................. 1286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CG47 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: CFEAD84199C3CEB5

FASTA1,286146,895
        10         20         30         40         50         60 
MRRKGTKPST ACHQEEGPPP SQDGAHSDEE MEQPAGEAES AAPAKPPGEE LDNRSLEEIL 

        70         80         90        100        110        120 
NSIPPPPPPA MASEAGAPRL MITHIVNQNF KSYAGEKVLG PFHKRFSCII GPNGSGKSNV 

       130        140        150        160        170        180 
IDSMLFVFGY RAQKIRSKKL SVLIHNSDEH KDIQSCTVEV HFQKIIDKEG DDYEVLPNSN 

       190        200        210        220        230        240 
FYVSRTAYRD STSVYHISGK KKTFKDVGNL LRSHGIDLDH NRFLILQGEV EQIAMMKPKG 

       250        260        270        280        290        300 
QTEHDEGMLE YLEDIIGCGR LNEPIKVLCR RVEILNEHRG EKLNRVKMVE KEKDALEGEK 

       310        320        330        340        350        360 
NIAIEFLTLE NEMFKKKNHI CQYYIYDLQN RIAEITTQKE KIHEDTKEIT EKSNVLSNEM 

       370        380        390        400        410        420 
KAKNSAVKDV EKKLNKVTKF IEQNKEKFTQ LDLEDVQVRE KLKHATSKAK KLEKQLQKDK 

       430        440        450        460        470        480 
EKVEELKSVP AKSKTVINET TTRNNSLEKE REKEEKKLKE VMDSLKQETQ GLQKEKEIQE 

       490        500        510        520        530        540 
KELMGFNKSV NEARSKMEVA QSELDIYLSR HNTAVSQLSK AKEALITASE TLKERKAAIK 

       550        560        570        580        590        600 
DINTKLPQTQ QELKEKEKEL QKLTQEEINL KSLVHDLFQK VEEAKSSLAM NRSRGKVLDA 

       610        620        630        640        650        660 
IIQEKKSGRI PGIYGRLGDL GAIDEKYDIA ISSCCHALDY IVVDSIDTAQ ECVNFLKKHN 

       670        680        690        700        710        720 
IGIATFIGLD KMTVWAKKMS KIQTPENTPR LFDLVKVKNE EIRQAFYFAL RDTLVANNLD 

       730        740        750        760        770        780 
QATRVAYQRD RRWRVVTLQG QIIEQSGTMS GGGSKVMRGR MGSSVIDEIS VEEVNKMESQ 

       790        800        810        820        830        840 
LERHSKQAMQ IQEQKVQHEE AVVKLRHSER DMRNTLEKFA ASIQGLSEQE EYLCVQIKEL 

       850        860        870        880        890        900 
EANVLTTAPD RKQQKLLEEN VSVFKKEYDA VAEKAGKVEA EIKRLHNTII DINNRKLKAQ 

       910        920        930        940        950        960 
QNKLDTINKQ LDECASAITK AQVAIKTADR NLKKAQDSVC RTEKEIKDTE KEINDLKTEL 

       970        980        990       1000       1010       1020 
KNIEDKAEEV INNTKTAETS LPEIQKEHRN LLQELKVIQE NEHALQKDAL SIKLKLEQID 

      1030       1040       1050       1060       1070       1080 
GHISEHNSKI KYWQKEISKI KLHPVEDNPV ETVAVLSQEE LEAIKNPESI TNEIALLEAQ 

      1090       1100       1110       1120       1130       1140 
CREMKPNLGA IAEYKKKEDL YLQRVAELDK ITSERDNFRQ AYEDLRKQRL NEFMAGFYVI 

      1150       1160       1170       1180       1190       1200 
TNKLKENYQM LTLGGDAELE LVDSLDPFSE GIMFSVRPPK KSWKKIFNLS GGEKTLSSLA 

      1210       1220       1230       1240       1250       1260 
LVFALHHYKP TPLYFMDEID AALDFKNVSI VAFYIYEQTK NAQFIIISLR NNMFEISDRL 

      1270       1280 
IGIYKTYNST KSVAVNPKQI ASKGLC 

« Hide

References

« Hide 'large scale' references
[1]"The evolution of SMC proteins: phylogenetic analysis and structural implications."
Cobbe N., Heck M.M.S.
Mol. Biol. Evol. 21:332-347(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and C57BL/6J.
Tissue: Brain and Mammary tumor.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-602.
Strain: NOD.
Tissue: Thymus.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ534940 mRNA. Translation: CAD59183.1.
BC005507 mRNA. Translation: AAH05507.1.
BC062939 mRNA. Translation: AAH62939.1.
AK088350 mRNA. Translation: BAC40297.1.
AK088846 mRNA. Translation: BAC40608.2.
RefSeqNP_598547.1. NM_133786.3.
XP_006502108.1. XM_006502045.1.
XP_006502109.1. XM_006502046.1.
UniGeneMm.206841.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51B595-752[»]
ProteinModelPortalQ8CG47.
SMRQ8CG47. Positions 595-752.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CG47. 1 interaction.

PTM databases

PhosphoSiteQ8CG47.

Proteomic databases

PaxDbQ8CG47.
PRIDEQ8CG47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042901; ENSMUSP00000047872; ENSMUSG00000034349.
GeneID70099.
KEGGmmu:70099.
UCSCuc008pma.1. mouse.

Organism-specific databases

CTD10051.
MGIMGI:1917349. Smc4.

Phylogenomic databases

eggNOGCOG1196.
GeneTreeENSGT00580000081617.
HOGENOMHOG000184777.
HOVERGENHBG106696.
InParanoidQ8CG47.
KOK06675.
OMAIAIEFLT.
OrthoDBEOG7RJPQJ.
PhylomeDBQ8CG47.
TreeFamTF101158.

Gene expression databases

ArrayExpressQ8CG47.
BgeeQ8CG47.
CleanExMM_SMC4.
GenevestigatorQ8CG47.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSMC4. mouse.
EvolutionaryTraceQ8CG47.
NextBio330998.
PROQ8CG47.
SOURCESearch...

Entry information

Entry nameSMC4_MOUSE
AccessionPrimary (citable) accession number: Q8CG47
Secondary accession number(s): Q8BTS7, Q8BTY9, Q99K21
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot