| General Information |
| MoonProt ID | 3 |
| First appeared in release | 1.0 |
| Name(s) | Structural maintenance of chromosome protein 3
Chondroitin sulfate proteoglycan 6
Chromosome segregation protein SmcD
Basement membrane-associated chondroitin proteoglycan
Bamacan
Mad member-interacting protein 1
SMC protein 3
SMC-3
SMC3
Gene Name: Smc3
|
| UniProt ID | Q9CW03 (SMC3_MOUSE), Reviewed |
| GO terms | GO:0006275 regulation of DNA replication
GO:0006281 DNA repair
GO:0006974 cellular response to DNA damage stimulus
GO:0007049 cell cycle
GO:0007052 mitotic spindle organization
GO:0007067 mitosis
GO:0007126 meiotic nuclear division
GO:0007165 signal transduction
GO:0019827 stem cell maintenance
GO:0032876 negative regulation of DNA endoreduplication
GO:0051276 chromosome organization
GO:0051301 cell division
GO:0000166 nucleotide binding
GO:0003682 chromatin binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0036033 mediator complex binding
GO:0045502 dynein binding
GO:0046982 protein heterodimerization activity
GO:0000775 chromosome, centromeric region
GO:0000785 chromatin
GO:0000800 lateral element
GO:0000922 spindle pole
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005694 chromosome
GO:0005737 cytoplasm
GO:0016363 nuclear matrix
GO:0030893 meiotic cohesin complex
GO:0034991 nuclear meiotic cohesin complex |
| Organisms for which functions have been demonstrated | Enteamoeba histolytica (amoeba, anaerobic eukaryote, causes amebiasis) |
| Sequence length | 1217 |
| FASTA sequence | >sp|Q9CW03|SMC3_MOUSE Structural maintenance of chromosomes protein 3 OS=Mus musculus GN=Smc3 PE=1 SV=2
MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSGESERGSGSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG" |
| Structure Information |
| PDB ID | 2WD5 |
| Quaternary structure | HINGE HETERODIMER |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
Q9CW03 is 1217 residues long, with 374 residues (30.73%) predicted as disordered.The protein has 2 short (< 30 residues) disorder segments and 3 long (>= 30 residues) disorder segments.
Segment 1 - Long (>= 30 residues) disordered segment Segment is located between positions 242 and 426 in the sequence. The segment is 185 residues long (15.20 % of the total sequence length).
Segment 2 - Short (< 30 residues) disordered segment Segment is located between positions 684 and 689 in the sequence. The segment is 6 residues long (0.49 % of the total sequence length).
Segment 3 - Long (>= 30 residues) disordered segment Segment is located between positions 713 and 782 in the sequence. The segment is 70 residues long (5.75 % of the total sequence length).
Segment 4 - Long (>= 30 residues) disordered segment Segment is located between positions 846 and 933 in the sequence. The segment is 88 residues long (7.23 % of the total sequence length).
Segment 5 - Short (< 30 residues) disordered segment Segment is located between positions 1064 and 1088 in the sequence. The segment is 25 residues long (2.05 % of the total sequence length). |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | SMC3 interacts with SMC1 and other non-Smc subunits like Scc3 and Scc1 (also called Rad21) to form a cohesion complex, called "cohesin," that maintains proper sister chromatid cohesion throughout the cell cycle and during mitosis to ensure accurate chromosome segregation.
Each Smc heterodimer associates with non-Smc subunits to form functional Smc complexes. |
| References for function | Wu N, Yu H. The Smc complexes in DNA damage response. Cell Biosci. 2012 Feb 27;2:5. doi: 10.1186/2045-3701-2-5. PMID: 22369641.
Darwiche N, Freeman LA, Strunnikov A. Characterization of the components of the putative mammalian sister chromatid cohesion complex. Gene. 1999 Jun 11. PMID: 10375619. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | nucleus, associated with chromosomes |
| Comments | |
| Function 2 |
| Function description | Bamacan is a proteoglycan, and is a component of a component of the basement membrane in the Engelbreth-Holm-Swarm tumor matrix, the renal mesangial matrix, and the basement membrane of other tissues.
Bamacan is involved in the control of cell growth and transformation |
| References for function | Ghiselli G, Siracusa LD, Iozzo RV. Complete cDNA cloning, genomic organization, chromosomal assignment, functional characterization of the promoter, and expression of the murine Bamacan gene. J Biol Chem. 1999 Jun 11;274(24):17384-93.PMID: 10358101.
Couchman JR, Kapoor R, Sthanam M, Wu RR. Perlecan and basement membrane-chondroitin sulfate proteoglycan (bamacan) are two basement membrane chondroitin/dermatan sulfate proteoglycans in the Engelbreth-Holm-Swarm tumor matrix. J Biol Chem. 1996 Apr 19;271(16):9595-602. PMID: 8621634. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | basement membrane, extracellular matrix |
| Comments | Glycanation sites (Ser-Gly) are present at residues 36, 249, 1073, 1081, and 1116, where attachment of glycosaminoglycan side GAG chains is possible
There is a P-loop motif starting at residue 32 which is an ATP binding site, and a DA box motif starting at residue 1114 which is a DNA binding site. These are highly conserved in SMC proteins as well. |