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Protein

Structural maintenance of chromosomes protein 3

Gene

Smc3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

Caution

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2467813 Separation of Sister Chromatids
R-MMU-2468052 Establishment of Sister Chromatid Cohesion
R-MMU-2470946 Cohesin Loading onto Chromatin
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins

Protein family/group databases

MoonProtiQ9CW03

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Smc3
Synonyms:Bam, Bmh, Cspg6, Mmip1, Smc3l1, Smcd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1339795 Smc3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi807L → P: Abolishes interaction with MXI1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190021 – 1217Structural maintenance of chromosomes protein 3Add BLAST1217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei105N6-acetyllysineCombined sources1
Modified residuei106N6-acetyllysineCombined sources1
Modified residuei140N6-acetyllysineBy similarity1
Modified residuei783PhosphothreonineBy similarity1
Modified residuei787PhosphoserineCombined sources1
Modified residuei886PhosphoserineBy similarity1
Modified residuei1013Phosphoserine1 Publication1
Modified residuei1065PhosphoserineBy similarity1
Modified residuei1067PhosphoserineCombined sources1
Modified residuei1074PhosphoserineBy similarity1
Modified residuei1083Phosphoserine1 Publication1
Modified residuei1190N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylated at Ser-1083 in a SPO11-dependent manner.2 Publications
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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CW03
MaxQBiQ9CW03
PaxDbiQ9CW03
PRIDEiQ9CW03

PTM databases

iPTMnetiQ9CW03
PhosphoSitePlusiQ9CW03

Expressioni

Tissue specificityi

Spermatocytes (at protein level). Widely expressed, with higher expression in testis and brain.2 Publications

Gene expression databases

BgeeiENSMUSG00000024974 Expressed in 280 organ(s), highest expression level in placenta
CleanExiMM_SMC3
ExpressionAtlasiQ9CW03 baseline and differential
GenevisibleiQ9CW03 MM

Interactioni

Subunit structurei

Forms a heterodimer with SMC1A or SMC1B in cohesin complexes (PubMed:11564881). Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their SMC 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. Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Interacts with PDS5A and WAPL; regulated by SMC3 acetylation. 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 and RPGR. Interacts (via SMC hinge domain) with KIAA1328 (via N- and C-terminal domains). Interacts with DDX11. Found in a cohesin complex with SMC1A, STAG1 and RAD21. The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (By similarity). Interacts with MXI1, MXD3 and MXD4 (PubMed:9528857). Interacts with STAG3 (PubMed:11483963).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Mecp2Q9Z2D63EBI-2550068,EBI-1188816

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198951, 48 interactors
CORUMiQ9CW03
DIPiDIP-57028N
IntActiQ9CW03, 51 interactors
MINTiQ9CW03
STRINGi10090.ENSMUSP00000025930

Structurei

Secondary structure

11217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9CW03
SMRiQ9CW03
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CW03

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini530 – 642SMC hingeAdd BLAST113

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili179 – 350Sequence analysisAdd BLAST172
Coiled coili393 – 503Sequence analysisAdd BLAST111
Coiled coili669 – 916Sequence analysisAdd BLAST248
Coiled coili958 – 989Sequence analysisAdd BLAST32

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1115 – 1150Ala/Asp-rich (DA-box)Add BLAST36

Domaini

The flexible SMC 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).By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC3 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0964 Eukaryota
COG1196 LUCA
GeneTreeiENSGT00580000081628
HOGENOMiHOG000166512
HOVERGENiHBG039849
InParanoidiQ9CW03
KOiK06669
OMAiSEMQKTE
OrthoDBiEOG091G011B
PhylomeDBiQ9CW03
TreeFamiTF105602

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR003395 RecF/RecN/SMC_N
IPR024704 SMC
IPR010935 SMC_hinge
IPR036277 SMC_hinge_sf
PfamiView protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit
PIRSFiPIRSF005719 SMC, 1 hit
SMARTiView protein in SMART
SM00968 SMC_hinge, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF75553 SSF75553, 2 hits

Sequencei

Sequence statusi: Complete.

Q9CW03-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS
60 70 80 90 100
DEFSHLRPEQ RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR
110 120 130 140 150
VIGAKKDQYF LDKKMVTKND VMNLLESAGF SRSNPYYIVK QGKINQMATA
160 170 180 190 200
PDSQRLKLLR EVAGTRVYDE RKEESISLMK ETEGKREKIN ELLKYIEERL
210 220 230 240 250
HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD ELSAKRETSG
260 270 280 290 300
EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK
310 320 330 340 350
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK
360 370 380 390 400
FNSVKEKEER GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK
410 420 430 440 450
SLDQAINDKK RQIAAIHKDL EDTEANKEKN LEQYNKLDQD LNEVKARVEE
460 470 480 490 500
LDRKYYEVKN KKDELQSERN YLWREENAEQ QALAAKREDL EKKQQLLRAA
510 520 530 540 550
TGKAILNGID SINKVLEHFR RKGINQHVQN GYHGIVMNNF ECEPAFYTCV
560 570 580 590 600
EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY
610 620 630 640 650
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC
660 670 680 690 700
ITLEGDQVSH RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL
710 720 730 740 750
RRNIERINNE IDQLMNQMQQ IETQQRKFKA SRDSILSEMK MLKEKRQQSE
760 770 780 790 800
KTFMPKQRSL QSLEASLHAM ESTRESLKAE LGTDLLSQLS LEDQKRVDAL
810 820 830 840 850
NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL DQVEQELNEL
860 870 880 890 900
RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS
910 920 930 940 950
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP
960 970 980 990 1000
QEAFEKYQTL SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL
1010 1020 1030 1040 1050
IKRQEELDRG YKSIMELMNV LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG
1060 1070 1080 1090 1100
GKATLVMKKG DVEGSQSQDE GEGSGESERG SGSQSSVPSV DQFTGVGIRV
1110 1120 1130 1140 1150
SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY LFDEIDQALD
1160 1170 1180 1190 1200
AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV
1210
ITAEMAKDFV EDDTTHG
Length:1,217
Mass (Da):141,556
Last modified:March 25, 2003 - v2
Checksum:i11FF55165BE6A88E
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti999K → R in CAA75400 (PubMed:9528857).Curated1
Sequence conflicti1175F → L (PubMed:9528857).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF141294 mRNA Translation: AAD42073.1
AF047601 mRNA Translation: AAD27754.1
Y15128 mRNA Translation: CAA75400.1 Frameshift.
AK005647 mRNA Translation: BAB24167.1
CCDSiCCDS38025.1
RefSeqiNP_031816.2, NM_007790.3
UniGeneiMm.14910

Genome annotation databases

EnsembliENSMUST00000025930; ENSMUSP00000025930; ENSMUSG00000024974
GeneIDi13006
KEGGimmu:13006
UCSCiuc008hwy.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF141294 mRNA Translation: AAD42073.1
AF047601 mRNA Translation: AAD27754.1
Y15128 mRNA Translation: CAA75400.1 Frameshift.
AK005647 mRNA Translation: BAB24167.1
CCDSiCCDS38025.1
RefSeqiNP_031816.2, NM_007790.3
UniGeneiMm.14910

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70B484-696[»]
ProteinModelPortaliQ9CW03
SMRiQ9CW03
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198951, 48 interactors
CORUMiQ9CW03
DIPiDIP-57028N
IntActiQ9CW03, 51 interactors
MINTiQ9CW03
STRINGi10090.ENSMUSP00000025930

Protein family/group databases

MoonProtiQ9CW03

PTM databases

iPTMnetiQ9CW03
PhosphoSitePlusiQ9CW03

Proteomic databases

EPDiQ9CW03
MaxQBiQ9CW03
PaxDbiQ9CW03
PRIDEiQ9CW03

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025930; ENSMUSP00000025930; ENSMUSG00000024974
GeneIDi13006
KEGGimmu:13006
UCSCiuc008hwy.2 mouse

Organism-specific databases

CTDi9126
MGIiMGI:1339795 Smc3

Phylogenomic databases

eggNOGiKOG0964 Eukaryota
COG1196 LUCA
GeneTreeiENSGT00580000081628
HOGENOMiHOG000166512
HOVERGENiHBG039849
InParanoidiQ9CW03
KOiK06669
OMAiSEMQKTE
OrthoDBiEOG091G011B
PhylomeDBiQ9CW03
TreeFamiTF105602

Enzyme and pathway databases

ReactomeiR-MMU-2467813 Separation of Sister Chromatids
R-MMU-2468052 Establishment of Sister Chromatid Cohesion
R-MMU-2470946 Cohesin Loading onto Chromatin
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins

Miscellaneous databases

ChiTaRSiSmc3 mouse
EvolutionaryTraceiQ9CW03
PROiPR:Q9CW03
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024974 Expressed in 280 organ(s), highest expression level in placenta
CleanExiMM_SMC3
ExpressionAtlasiQ9CW03 baseline and differential
GenevisibleiQ9CW03 MM

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR003395 RecF/RecN/SMC_N
IPR024704 SMC
IPR010935 SMC_hinge
IPR036277 SMC_hinge_sf
PfamiView protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit
PIRSFiPIRSF005719 SMC, 1 hit
SMARTiView protein in SMART
SM00968 SMC_hinge, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF75553 SSF75553, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiSMC3_MOUSE
AccessioniPrimary (citable) accession number: Q9CW03
Secondary accession number(s): O35667, Q9QUS3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: September 12, 2018
This is version 164 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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