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Q9CW03 (SMC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 3

Short name=SMC protein 3
Short name=SMC-3
Alternative name(s):
Basement membrane-associated chondroitin proteoglycan
Short name=Bamacan
Chondroitin sulfate proteoglycan 6
Chromosome segregation protein SmcD
Mad member-interacting protein 1
Gene names
Name:Smc3
Synonyms:Bam, Bmh, Cspg6, Mmip1, Smc3l1, Smcd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement. Ref.2

Subunit structure

Interacts with NUMA1, and forms a ternary complex with KIF3B and KIFAP3, suggesting a function in tethering the chromosomes to the spindle pole and a function in chromosome movement. Interacts with SYCP2. Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/APRIN and PDS5B/SCC-112. Interacts with PDS5A and WAPAL; regulated by SMC3 acetylation By similarity. Forms a heterodimer with SMC1A or SMC1B in cohesin complexes. Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. Also found in meiosis-specific cohesin complexes. Interacts with MXI1, MXD3 and MXD4. Interacts with RPGR By similarity. Ref.2 Ref.3 Ref.5 Ref.6

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. The phosphorylated form at Ser-1083 is preferentially associated with unsynapsed chromosomal regions. Ref.9

Tissue specificity

Widely expressed, with higher expression in testis and brain.

Domain

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1A or SMC1B, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 protein, forming a ring structure By similarity.

Post-translational modification

Phosphorylated at Ser-1083 in a SPO11-dependent manner. Ref.7 Ref.9

Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion. Regulated by DSCC1, it is required for processive DNA synthesis, coupling sister chromatid cohesion establishment during S phase to DNA replication By similarity. Deacetylation by HDAC8, regulates release of the cohesin complex from chromatin By similarity.

Sequence similarities

Belongs to the SMC family. SMC3 subfamily.

Caution

Was originally isolated as a proteoglycan protein (explaining its name). Although not excluded, such secreted function is not clear.

Sequence caution

The sequence CAA75400.1 differs from that shown. Reason: Frameshift at positions 522, 1018 and 1144.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Meiosis
Mitosis
   Cellular componentCentromere
Chromosome
Nucleus
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome organization

Inferred from electronic annotation. Source: InterPro

meiotic nuclear division

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of DNA endoreduplication

Inferred from electronic annotation. Source: Ensembl

regulation of DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

stem cell maintenance

Inferred from mutant phenotype PubMed 20720539. Source: MGI

   Cellular_componentchromatin

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

lateral element

Inferred from direct assay PubMed 15870106PubMed 22711701. Source: MGI

meiotic cohesin complex

Inferred from direct assay PubMed 21527826. Source: UniProtKB

nuclear matrix

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear meiotic cohesin complex

Inferred from direct assay PubMed 21743440PubMed 22164254. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12759374. Source: MGI

spindle pole

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from direct assay PubMed 20720539PubMed 22415368. Source: MGI

dynein binding

Inferred from sequence or structural similarity. Source: UniProtKB

mediator complex binding

Inferred from direct assay PubMed 20720539. Source: MGI

protein binding

Inferred from physical interaction PubMed 12759374. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12171217Structural maintenance of chromosomes protein 3
PRO_0000119002

Regions

Nucleotide binding32 – 398ATP Potential
Region505 – 667163Flexible hinge
Coiled coil179 – 350172 Potential
Coiled coil393 – 503111 Potential
Coiled coil669 – 916248 Potential
Coiled coil958 – 98932 Potential
Compositional bias1115 – 115036Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue1051N6-acetyllysine Ref.10
Modified residue1061N6-acetyllysine Ref.10
Modified residue1401N6-acetyllysine By similarity
Modified residue7831Phosphothreonine By similarity
Modified residue7871Phosphoserine Ref.8
Modified residue10131Phosphoserine Ref.7
Modified residue10651Phosphoserine By similarity
Modified residue10671Phosphoserine By similarity
Modified residue10831Phosphoserine Ref.9
Modified residue11901N6-acetyllysine By similarity

Experimental info

Mutagenesis8071L → P: Abolishes interaction with MXI1. Ref.3
Sequence conflict9991K → R in CAA75400. Ref.3
Sequence conflict11751F → L Ref.3

Secondary structure

...................................... 1217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CW03 [UniParc].

Last modified March 25, 2003. Version 2.
Checksum: 11FF55165BE6A88E

FASTA1,217141,556
        10         20         30         40         50         60 
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ 

        70         80         90        100        110        120 
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND 

       130        140        150        160        170        180 
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK 

       190        200        210        220        230        240 
ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD 

       250        260        270        280        290        300 
ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK 

       310        320        330        340        350        360 
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER 

       370        380        390        400        410        420 
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL 

       430        440        450        460        470        480 
EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ 

       490        500        510        520        530        540 
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLEHFR RKGINQHVQN GYHGIVMNNF 

       550        560        570        580        590        600 
ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY 

       610        620        630        640        650        660 
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH 

       670        680        690        700        710        720 
RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ 

       730        740        750        760        770        780 
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE 

       790        800        810        820        830        840 
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL 

       850        860        870        880        890        900 
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS 

       910        920        930        940        950        960 
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL 

       970        980        990       1000       1010       1020 
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV 

      1030       1040       1050       1060       1070       1080 
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSGESERG 

      1090       1100       1110       1120       1130       1140 
SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY 

      1150       1160       1170       1180       1190       1200 
LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV 

      1210 
ITAEMAKDFV EDDTTHG 

« Hide

References

« Hide 'large scale' references
[1]"Complete cDNA cloning, genomic organization, chromosomal assignment, functional characterization of the promoter, and expression of the murine Bamacan gene."
Ghiselli G., Siracusa L.D., Iozzo R.V.
J. Biol. Chem. 274:17384-17393(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of the components of the putative mammalian sister chromatid cohesion complex."
Darwiche N., Freeman L.A., Strunnikov A.
Gene 233:39-47(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A AND RAD21.
[3]"Mmip1: a novel leucine zipper protein that reverses the suppressive effects of mad family members on C-myc."
Gupta K., Anand G., Yin X.Y., Prochownik E.V.
Oncogene 16:1149-1159(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 478-1217, INTERACTION WITH MXI1; MXD3 AND MXD4, MUTAGENESIS OF LEU-807.
Tissue: Embryo.
[4]"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 887-1217.
Strain: C57BL/6J.
Tissue: Testis.
[5]"Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis I."
Prieto I., Suja J.A., Pezzi N., Kremer L., Martinez-A C., Rufas J.S., Barbero J.L.
Nat. Cell Biol. 3:761-766(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STAG3.
[6]"Novel meiosis-specific isoform of mammalian SMC1."
Revenkova E., Eijpe M., Heyting C., Gross B., Jessberger R.
Mol. Cell. Biol. 21:6984-6998(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMC1B.
[7]"Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry."
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.
Rapid Commun. Mass Spectrom. 18:2169-2176(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1013.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[9]"Phosphorylation of chromosome core components may serve as axis marks for the status of chromosomal events during mammalian meiosis."
Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D., Hoeoeg C.
PLoS Genet. 8:E1002485-E1002485(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1083.
[10]"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-105 AND LYS-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF141294 mRNA. Translation: AAD42073.1.
AF047601 mRNA. Translation: AAD27754.1.
Y15128 mRNA. Translation: CAA75400.1. Frameshift.
AK005647 mRNA. Translation: BAB24167.1.
CCDSCCDS38025.1.
RefSeqNP_031816.2. NM_007790.3.
UniGeneMm.14910.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70B484-696[»]
ProteinModelPortalQ9CW03.
SMRQ9CW03. Positions 1-239, 493-686, 987-1206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198951. 12 interactions.
DIPDIP-57028N.
IntActQ9CW03. 13 interactions.
MINTMINT-4134864.

PTM databases

PhosphoSiteQ9CW03.

Proteomic databases

MaxQBQ9CW03.
PaxDbQ9CW03.
PRIDEQ9CW03.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025930; ENSMUSP00000025930; ENSMUSG00000024974.
GeneID13006.
KEGGmmu:13006.
UCSCuc008hwy.2. mouse.

Organism-specific databases

CTD9126.
MGIMGI:1339795. Smc3.

Phylogenomic databases

eggNOGCOG1196.
GeneTreeENSGT00580000081628.
HOGENOMHOG000166512.
HOVERGENHBG039849.
InParanoidQ9CW03.
KOK06669.
OMAASINSIV.
OrthoDBEOG73803T.
PhylomeDBQ9CW03.
TreeFamTF105602.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressQ9CW03.
BgeeQ9CW03.
CleanExMM_SMC3.
GenevestigatorQ9CW03.

Family and domain databases

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

Other

ChiTaRSSMC3. mouse.
EvolutionaryTraceQ9CW03.
NextBio282832.
PROQ9CW03.
SOURCESearch...

Entry information

Entry nameSMC3_MOUSE
AccessionPrimary (citable) accession number: Q9CW03
Secondary accession number(s): O35667, Q9QUS3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: July 9, 2014
This is version 119 of the entry and version 2 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