SMC3

SMC3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSMC3, BAM, BMH, CDLS3, CSPG6, HCAP, SMC3L1, structural maintenance of chromosomes 3
External IDsMGI: 1339795 HomoloGene: 3974 GeneCards: SMC3
Gene location (Human)
Chr.Chromosome 10 (human)[1]
Band10q25.2Start110,567,691 bp[1]
End110,604,636 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

9126

13006

Ensembl

ENSG00000108055

ENSMUSG00000024974

UniProt

Q9UQE7

Q9CW03

RefSeq (mRNA)

NM_005445

NM_007790

RefSeq (protein)

NP_005436

NP_031816

Location (UCSC)Chr 10: 110.57 – 110.6 MbChr 19: 53.6 – 53.65 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Structural maintenance of chromosomes protein 3 (SMC-3) is a nuclear protein that in humans is encoded by the SMC3 gene.[5] A post-translated modified form that is excreted is known as basement membrane-associated chondroitin proteoglycan (bamacan).

Function

This gene belongs to the SMC3 subfamily of SMC proteins. The encoded protein occurs in certain cell types as either an intracellular, nuclear protein or a secreted protein. The nuclear form, known as structural maintenance of chromosomes 3, is a component of the multimeric cohesin complex that holds together sister chromatids during mitosis, enabling proper chromosome segregation. Post-translational modification of the encoded protein by the addition of chondroitin sulfate chains gives rise to the secreted proteoglycan bamacan, an abundant basement membrane protein.[5]

SMC3 protein appears to participate with other cohesins REC8, STAG3 and SMC1ß in sister-chromatid cohesion throughout the whole meiotic process in human oocytes.[6]

Model organisms

Model organisms have been used in the study of SMC3 function. A conditional knockout mouse line, called Smc3tm1a(EUCOMM)Wtsi[14][15] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[16][17][18]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[12][19] Twenty two tests were carried out on mutant mice and six significant abnormalities were observed.[12] No homozygous mutant embryos were identified during gestation, and thus none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice. Females had a higher than normal incidence of pre-wean death in their offspring, and also had a decreased body weight. Males heterozygotes displayed a shortened, upturned snout.[12][19]

Cornelia de Lange syndrome

Cornelia de Lange syndrome (CdLS) is a rare genetic disorder that presents with variable clinical abnormalities including dysmorphic features, severe growth retardation, global developmental delay, and intellectual disability. SMC3 is one of five genes that have been implicated in CdLS.[20] In one case report, a novel SMC3 gene duplication was detected in a child with failure to thrive, hypotonia and facial dysmorphic features of CdLS.[20] The same duplication was also observed in the mother, who had milder dysmorphic facies.

Interactions

SMC3 (gene) has been shown to interact with:

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000108055 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024974 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 "Entrez Gene: SMC3 structural maintenance of chromosomes 3".
  6. ↑ Garcia-Cruz R, Brieño MA, Roig I, Grossmann M, Velilla E, Pujol A, Cabero L, Pessarrodona A, Barbero JL, Garcia Caldés M (2010). "Dynamics of cohesin proteins REC8, STAG3, SMC1 beta and SMC3 are consistent with a role in sister chromatid cohesion during meiosis in human oocytes". Hum. Reprod. 25 (9): 2316–27. doi:10.1093/humrep/deq180. PMID 20634189.
  7. ↑ "Body weight data for Smc3". Wellcome Trust Sanger Institute.
  8. ↑ "Dysmorphology data for Smc3". Wellcome Trust Sanger Institute.
  9. ↑ "DEXA data for Smc3". Wellcome Trust Sanger Institute.
  10. ↑ "Salmonella infection data for Smc3". Wellcome Trust Sanger Institute.
  11. ↑ "Citrobacter infection data for Smc3". Wellcome Trust Sanger Institute.
  12. 1 2 3 4 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  13. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  14. ↑ "International Knockout Mouse Consortium".
  15. ↑ "Mouse Genome Informatics".
  16. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  17. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  18. ↑ Collins FS, Rossant J, Wurst W (2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  19. 1 2 van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  20. 1 2 Infante E, Alkorta-Aranburu G, El-Gharbawy A (2017). "Rare form of autosomal dominant familial Cornelia de Lange syndrome due to a novel duplication in SMC3". Clin Case Rep. 5 (8): 1277–1283. doi:10.1002/ccr3.1010. PMC 5538066. PMID 28781842.
  21. ↑ Shimizu K, Shirataki H, Honda T, Minami S, Takai Y (March 1998). "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide". J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
  22. 1 2 Gupta K, Anand G, Yin X, Grove L, Prochownik EV (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
  23. 1 2 Lee J, Iwai T, Yokota T, Yamashita M (July 2003). "Temporally and spatially selective loss of Rec8 protein from meiotic chromosomes during mammalian meiosis". J. Cell Sci. 116 (Pt 13): 2781–90. doi:10.1242/jcs.00495. PMID 12759374.
  24. ↑ Kim ST, Xu B, Kastan MB (March 2002). "Involvement of the cohesin protein, Smc1, in Atm-dependent and independent responses to DNA damage". Genes Dev. 16 (5): 560–70. doi:10.1101/gad.970602. PMC 155347. PMID 11877376.
  25. ↑ Schmiesing JA, Ball AR, Gregson HC, Alderton JM, Zhou S, Yokomori K (October 1998). "Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 12906–11. doi:10.1073/pnas.95.22.12906. PMC 23650. PMID 9789013.
  26. ↑ Gregson HC, Schmiesing JA, Kim JS, Kobayashi T, Zhou S, Yokomori K (Dec 2001). "A potential role for human cohesin in mitotic spindle aster assembly". J. Biol. Chem. 276 (50): 47575–82. doi:10.1074/jbc.M103364200. PMID 11590136.

Further reading

  • Wu RR, Couchman JR (1997). "cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs". J. Cell Biol. 136 (2): 433–44. doi:10.1083/jcb.136.2.433. PMC 2134808. PMID 9015313.
  • Shimizu K, Shirataki H, Honda T, Minami S, Takai Y (1998). "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide". J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
  • Gupta K, Anand G, Yin X, Grove L, Prochownik EV (1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
  • Schmiesing JA, Ball AR, Gregson HC, Alderton JM, Zhou S, Yokomori K (1998). "Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 12906–11. doi:10.1073/pnas.95.22.12906. PMC 23650. PMID 9789013.
  • Ghiselli G, Iozzo RV (2000). "Overexpression of bamacan/SMC3 causes transformation". J. Biol. Chem. 275 (27): 20235–8. doi:10.1074/jbc.C000213200. PMID 10801778.
  • Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
  • Sumara I, Vorlaufer E, Gieffers C, Peters BH, Peters JM (2000). "Characterization of vertebrate cohesin complexes and their regulation in prophase". J. Cell Biol. 151 (4): 749–62. doi:10.1083/jcb.151.4.749. PMC 2169443. PMID 11076961.
  • Revenkova E, Eijpe M, Heyting C, Gross B, Jessberger R (2001). "Novel meiosis-specific isoform of mammalian SMC1". Mol. Cell. Biol. 21 (20): 6984–98. doi:10.1128/MCB.21.20.6984-6998.2001. PMC 99874. PMID 11564881.
  • Gregson HC, Schmiesing JA, Kim JS, Kobayashi T, Zhou S, Yokomori K (2001). "A potential role for human cohesin in mitotic spindle aster assembly". J. Biol. Chem. 276 (50): 47575–82. doi:10.1074/jbc.M103364200. PMID 11590136.
  • Kim ST, Xu B, Kastan MB (2002). "Involvement of the cohesin protein, Smc1, in Atm-dependent and independent responses to DNA damage". Genes Dev. 16 (5): 560–70. doi:10.1101/gad.970602. PMC 155347. PMID 11877376.
  • James RD, Schmiesing JA, Peters AH, Yokomori K, Disteche CM (2002). "Differential association of SMC1alpha and SMC3 proteins with meiotic chromosomes in wild-type and SPO11-deficient male mice". Chromosome Res. 10 (7): 549–60. doi:10.1023/A:1020910601858. PMID 12498344.
  • Ghiselli G, Coffee N, Munnery CE, Koratkar R, Siracusa LD (2003). "The cohesin SMC3 is a target for the beta-catenin/TCF4 transactivation pathway". J. Biol. Chem. 278 (22): 20259–67. doi:10.1074/jbc.M209511200. PMID 12651860.
  • Lee J, Iwai T, Yokota T, Yamashita M (2003). "Temporally and spatially selective loss of Rec8 protein from meiotic chromosomes during mammalian meiosis". J. Cell Sci. 116 (Pt 13): 2781–90. doi:10.1242/jcs.00495. PMID 12759374.
  • Prieto I, Tease C, Pezzi N, Buesa JM, Ortega S, Kremer L, Martínez A, Martínez-A C, Hultén MA, Barbero JL (2004). "Cohesin component dynamics during meiotic prophase I in mammalian oocytes". Chromosome Res. 12 (3): 197–213. doi:10.1023/B:CHRO.0000021945.83198.0e. PMID 15125634.
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
  • Patel CA, Ghiselli G (2005). "Hinderin, a five-domains protein including coiled-coil motifs that binds to SMC3". BMC Cell Biol. 6 (1): 3. doi:10.1186/1471-2121-6-3. PMC 547899. PMID 15656913.
  • Rankin S, Ayad NG, Kirschner MW (2005). "Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates". Mol. Cell. 18 (2): 185–200. doi:10.1016/j.molcel.2005.03.017. PMID 15837422.
  • Khanna H, Hurd TW, Lillo C, Shu X, Parapuram SK, He S, Akimoto M, Wright AF, Margolis B, Williams DS, Swaroop A (2005). "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with SMC1, SMC3, and microtubule transport proteins". J. Biol. Chem. 280 (39): 33580–7. doi:10.1074/jbc.M505827200. PMC 1249479. PMID 16043481.
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