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Protein

Structural maintenance of chromosomes protein 3

Gene

Smc3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: MGI
  • dynein binding Source: UniProtKB
  • mediator complex binding Source: MGI
  • protein heterodimerization activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-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.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1339795. Smc3.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication
  • Chromosomecentromere 1 Publication

  • 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.

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • chromosome, centromeric region Source: UniProtKB-SubCell
  • cohesin core heterodimer Source: InterPro
  • cytoplasm Source: UniProtKB
  • lateral element Source: MGI
  • meiotic cohesin complex Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nuclear meiotic cohesin complex Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • spindle pole Source: UniProtKB
Complete GO annotation...

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

Widely expressed, with higher expression in testis and brain.

Gene expression databases

BgeeiENSMUSG00000024974.
CleanExiMM_SMC3.
ExpressionAtlasiQ9CW03. baseline and differential.
GenevisibleiQ9CW03. MM.

Interactioni

Subunit structurei

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/SCC-112 and PDS5B/APRIN. Interacts with PDS5A and WAPL; 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). Interacts (via central hinge region) with KIAA1328 (via N- and C-terminal domains) (By similarity). Interacts with DDX11 (By similarity).By similarity

Binary interactionsi

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

GO - Molecular functioni

  • dynein binding Source: UniProtKB
  • mediator complex binding Source: MGI
  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi198951. 46 interactors.
DIPiDIP-57028N.
IntActiQ9CW03. 45 interactors.
MINTiMINT-4134864.
STRINGi10090.ENSMUSP00000025930.

Structurei

Secondary structure

11217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi495 – 498Combined sources4
Turni499 – 501Combined sources3
Helixi502 – 522Combined sources21
Helixi526 – 529Combined sources4
Beta strandi532 – 535Combined sources4
Helixi536 – 538Combined sources3
Beta strandi539 – 541Combined sources3
Helixi544 – 546Combined sources3
Helixi547 – 554Combined sources8
Helixi557 – 559Combined sources3
Beta strandi561 – 564Combined sources4
Helixi566 – 578Combined sources13
Beta strandi585 – 589Combined sources5
Turni590 – 592Combined sources3
Beta strandi604 – 608Combined sources5
Helixi609 – 612Combined sources4
Helixi617 – 619Combined sources3
Helixi620 – 627Combined sources8
Beta strandi630 – 635Combined sources6
Helixi636 – 645Combined sources10
Beta strandi649 – 651Combined sources3
Beta strandi664 – 666Combined sources3
Helixi676 – 685Combined sources10

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...

Miscellaneous databases

EvolutionaryTraceiQ9CW03.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni505 – 667Flexible hingeAdd BLAST163

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 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.
OMAiSKRETCG.
OrthoDBiEOG091G011B.
PhylomeDBiQ9CW03.
TreeFamiTF105602.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF8. PTHR18937:SF8. 3 hits.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
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.

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. 46 interactors.
DIPiDIP-57028N.
IntActiQ9CW03. 45 interactors.
MINTiMINT-4134864.
STRINGi10090.ENSMUSP00000025930.

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.
OMAiSKRETCG.
OrthoDBiEOG091G011B.
PhylomeDBiQ9CW03.
TreeFamiTF105602.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-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.
PROiQ9CW03.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024974.
CleanExiMM_SMC3.
ExpressionAtlasiQ9CW03. baseline and differential.
GenevisibleiQ9CW03. MM.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF8. PTHR18937:SF8. 3 hits.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
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 historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: November 30, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.