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Protein

Structural maintenance of chromosomes protein 3

Gene

Smc3

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPSequence analysis

GO - Molecular functioni

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

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
Gene namesi
Name:Smc3
Synonyms:Bam, Bmh, Cspg6, Smc3l1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62006. Smc3.

Subcellular locationi

  • Nucleus By similarity
  • Chromosome By similarity

  • 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 (By similarity). The phosphorylated form at Ser-1083 is preferentially associated with unsynapsed chromosomal regions (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11911191Structural maintenance of chromosomes protein 3PRO_0000119004Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-acetyllysineBy similarity
Modified residuei140 – 1401N6-acetyllysineBy similarity
Modified residuei783 – 7831PhosphothreonineBy similarity
Modified residuei787 – 7871PhosphoserineBy similarity
Modified residuei886 – 8861PhosphoserineBy similarity
Modified residuei1013 – 10131PhosphoserineBy similarity
Modified residuei1065 – 10651PhosphoserineBy similarity
Modified residuei1067 – 10671PhosphoserineCombined sources
Modified residuei1074 – 10741PhosphoserineCombined sources
Modified residuei1083 – 10831PhosphoserineBy similarity

Post-translational modificationi

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

PaxDbiP97690.
PeptideAtlasiP97690.
PRIDEiP97690.

PTM databases

iPTMnetiP97690.
PhosphoSiteiP97690.

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Subunit structurei

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 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 MXI1, MXD3 and MXD4. 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). Interacts with RPGR (By similarity). Interacts with SYCP2 (PubMed:10652260). Interacts (via central hinge region) with KIAA1328 (via N- and C-terminal domains) (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019560.

Structurei

3D structure databases

ProteinModelPortaliP97690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni505 – 667163Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili173 – 357185Sequence analysisAdd
BLAST
Coiled coili389 – 504116Sequence analysisAdd
BLAST
Coiled coili668 – 1022355Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1115 – 115036Ala/Asp-rich (DA-box)Add
BLAST

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.
HOGENOMiHOG000166512.
HOVERGENiHBG039849.
InParanoidiP97690.

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.

P97690-1 [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 SINKVLDHFR 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 SRDSTLSEMK MLKEKRQQSE
760 770 780 790 800
KTFMPKQRSL QSLEASLHAM ESTRESLKAE LGTDLPSQLS LEDQKRVDAL
810 820 830 840 850
NDEIRQLQQK NRQLLNERIK LEGIITRVET YLNENLRKRL DQVEQELNEL
860 870 880 890 900
RETEGGTVLT ATTSQLEAIN 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
AKATLVMKKG DVEGSQSQDE GEGSGESERG SGSQSSVPSV DQFTGVGIRV
1110 1120 1130 1140 1150
SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY LFDEIDQALD
1160 1170 1180 1190
AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKSSGKS E
Length:1,191
Mass (Da):138,448
Last modified:May 1, 1997 - v1
Checksum:i1F33AEF05E9198A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82626 mRNA. Translation: AAB96342.1.
UniGeneiRn.11074.

Genome annotation databases

UCSCiRGD:62006. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82626 mRNA. Translation: AAB96342.1.
UniGeneiRn.11074.

3D structure databases

ProteinModelPortaliP97690.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019560.

PTM databases

iPTMnetiP97690.
PhosphoSiteiP97690.

Proteomic databases

PaxDbiP97690.
PeptideAtlasiP97690.
PRIDEiP97690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:62006. rat.

Organism-specific databases

RGDi62006. Smc3.

Phylogenomic databases

eggNOGiKOG0964. Eukaryota.
COG1196. LUCA.
HOGENOMiHOG000166512.
HOVERGENiHBG039849.
InParanoidiP97690.

Miscellaneous databases

PROiP97690.

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...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs."
    Wu R.-R., Couchman J.R.
    J. Cell Biol. 136:433-444(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Yolk sac carcinoma.
  2. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 437-447 AND 462-469, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Association of mammalian SMC1 and SMC3 proteins with meiotic chromosomes and synaptonemal complexes."
    Eijpe M., Heyting C., Gross B., Jessberger R.
    J. Cell Sci. 113:673-682(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYCP2.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067 AND SER-1074, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSMC3_RAT
AccessioniPrimary (citable) accession number: P97690
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 1, 1997
Last modified: July 6, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

PubMed:9015313 originally reported this protein to be a proteoglycan (thus explaining its name). Although not excluded, such secreted function is not clear.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.