SMC3_RAT
ID SMC3_RAT Reviewed; 1191 AA.
AC P97690;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE Short=SMC protein 3;
DE Short=SMC-3;
DE AltName: Full=Basement membrane-associated chondroitin proteoglycan;
DE Short=Bamacan;
DE AltName: Full=Chondroitin sulfate proteoglycan 6;
DE AltName: Full=Chromosome segregation protein SmcD;
GN Name=Smc3; Synonyms=Bam, Bmh, Cspg6, Smc3l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Yolk sac carcinoma;
RX PubMed=9015313; DOI=10.1083/jcb.136.2.433;
RA Wu R.-R., Couchman J.R.;
RT "cDNA cloning of the basement membrane chondroitin sulfate proteoglycan
RT core protein, bamacan: a five domain structure including coiled-coil
RT motifs.";
RL J. Cell Biol. 136:433-444(1997).
RN [2]
RP PROTEIN SEQUENCE OF 437-447 AND 462-469, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH SYCP2.
RX PubMed=10652260; DOI=10.1242/jcs.113.4.673;
RA Eijpe M., Heyting C., Gross B., Jessberger R.;
RT "Association of mammalian SMC1 and SMC3 proteins with meiotic chromosomes
RT and synaptonemal complexes.";
RL J. Cell Sci. 113:673-682(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067 AND SER-1074, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Central component of cohesin, a complex required for
CC chromosome cohesion during the cell cycle. The cohesin complex may form
CC a large proteinaceous ring within which sister chromatids can be
CC trapped. At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate. Cohesion is coupled
CC to DNA replication and is involved in DNA repair. The cohesin complex
CC also plays an important role in spindle pole assembly during mitosis
CC and in chromosomes movement (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC1A or SMC1B in cohesin complexes.
CC Cohesin complexes are composed of the SMC1 (SMC1A or meiosis-specific
CC SMC1B) and SMC3 heterodimer attached via their SMC hinge domain, RAD21
CC which link them, and one STAG protein (STAG1, STAG2 or STAG3), which
CC interacts with RAD21. Also found in meiosis-specific cohesin complexes.
CC Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/SCC-112 and
CC PDS5B/APRIN. Interacts with MXI1, MXD3 and MXD4. Interacts with NUMA1,
CC and forms a ternary complex with KIF3B and KIFAP3, suggesting a
CC function in tethering the chromosomes to the spindle pole and a
CC function in chromosome movement. Interacts with PDS5A and WAPL;
CC regulated by SMC3 acetylation. Interacts (via SMC hinge domain) with
CC KIAA1328 (via N- and C-terminal domains). Interacts with DDX11, RPGR
CC and STAG3. Found in a cohesin complex with SMC1A, RAD21 and STAG1. The
CC SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (By
CC similarity). Interacts with SYCP2 (PubMed:10652260). Interacts with the
CC NuRD complex component HDAC2; the interaction is direct (By
CC similarity). {ECO:0000250|UniProtKB:O97594,
CC ECO:0000250|UniProtKB:Q9CW03, ECO:0000250|UniProtKB:Q9UQE7,
CC ECO:0000269|PubMed:10652260}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CW03}.
CC Chromosome {ECO:0000250|UniProtKB:Q9CW03}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q9CW03}. Note=Associates with chromatin. Before
CC prophase it is scattered along chromosome arms. During prophase, most
CC of cohesin complexes dissociate from chromatin probably because of
CC phosphorylation by PLK, except at centromeres, where cohesin complexes
CC remain. At anaphase, the RAD21 subunit of the cohesin complex is
CC cleaved, leading to the dissociation of the complex from chromosomes,
CC allowing chromosome separation (By similarity). The phosphorylated form
CC at Ser-1083 is preferentially associated with unsynapsed chromosomal
CC regions (By similarity). {ECO:0000250|UniProtKB:Q9CW03}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC1A or SMC1B, forming a V-shaped
CC heterodimer. The two heads of the heterodimer are then connected by
CC different ends of the cleavable RAD21 protein, forming a ring structure
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-1083 in a SPO11-dependent manner.
CC {ECO:0000250|UniProtKB:Q9CW03}.
CC -!- PTM: Acetylation at Lys-105 and Lys-106 by ESCO1 is important for
CC genome stability and S phase sister chromatid cohesion. Regulated by
CC DSCC1, it is required for processive DNA synthesis, coupling sister
CC chromatid cohesion establishment during S phase to DNA replication (By
CC similarity). Deacetylation by HDAC8, regulates release of the cohesin
CC complex from chromatin (By similarity). {ECO:0000250|UniProtKB:Q9UQE7}.
CC -!- PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its
CC degradation. {ECO:0000250|UniProtKB:Q9UQE7}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000305}.
CC -!- CAUTION: PubMed:9015313 originally reported this protein to be a
CC proteoglycan (thus explaining its name). Although not excluded, such
CC secreted function is not clear. {ECO:0000305}.
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DR EMBL; U82626; AAB96342.1; -; mRNA.
DR AlphaFoldDB; P97690; -.
DR SMR; P97690; -.
DR IntAct; P97690; 2.
DR STRING; 10116.ENSRNOP00000019560; -.
DR iPTMnet; P97690; -.
DR PhosphoSitePlus; P97690; -.
DR jPOST; P97690; -.
DR PaxDb; P97690; -.
DR PeptideAtlas; P97690; -.
DR PRIDE; P97690; -.
DR UCSC; RGD:62006; rat.
DR RGD; 62006; Smc3.
DR eggNOG; KOG0964; Eukaryota.
DR InParanoid; P97690; -.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:P97690; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; ISO:RGD.
DR GO; GO:0000800; C:lateral element; ISO:RGD.
DR GO; GO:0030893; C:meiotic cohesin complex; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; ISO:RGD.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0061775; F:cohesin loading activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR GO; GO:0036033; F:mediator complex binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISO:RGD.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Direct protein sequencing; DNA damage; DNA repair;
KW Meiosis; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1191
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000119004"
FT DOMAIN 530..642
FT /note="SMC hinge"
FT REGION 242..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..357
FT /evidence="ECO:0000255"
FT COILED 389..504
FT /evidence="ECO:0000255"
FT COILED 668..1022
FT /evidence="ECO:0000255"
FT COMPBIAS 1067..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 783
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CW03"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
SQ SEQUENCE 1191 AA; 138448 MW; 1F33AEF05E9198A2 CRC64;
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK
ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD
ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL
EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLDHFR RKGINQHVQN GYHGIVMNNF
ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH
RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ
IETQQRKFKA SRDSTLSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE
LGTDLPSQLS LEDQKRVDAL NDEIRQLQQK NRQLLNERIK LEGIITRVET YLNENLRKRL
DQVEQELNEL RETEGGTVLT ATTSQLEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG AKATLVMKKG DVEGSQSQDE GEGSGESERG
SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY
LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKSSGKS E
