SMC3_BOVIN
ID SMC3_BOVIN Reviewed; 1218 AA.
AC O97594;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE Short=SMC protein 3;
DE Short=SMC-3;
DE AltName: Full=Chondroitin sulfate proteoglycan 6;
GN Name=SMC3; Synonyms=CSPG6, SMC3L1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INTERACTION WITH SMC1A.
RX PubMed=10072753; DOI=10.1016/s0378-1119(99)00021-9;
RA Stursberg S., Riwar B., Jessberger R.;
RT "Cloning and characterization of mammalian SMC1 and SMC3 genes and
RT proteins, components of the DNA recombination complexes RC-1.";
RL Gene 228:1-12(1999).
RN [2]
RP INTERACTION WITH RPGR.
RX PubMed=16043481; DOI=10.1074/jbc.m505827200;
RA Khanna H., Hurd T.W., Lillo C., Shu X., Parapuram S.K., He S., Akimoto M.,
RA Wright A.F., Margolis B., Williams D.S., Swaroop A.;
RT "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with
RT SMC1, SMC3, and microtubule transport proteins.";
RL J. Biol. Chem. 280:33580-33587(2005).
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.
CC -!- SUBUNIT: Forms a heterodimer with SMC1A or SMC1B in cohesin complexes
CC (PubMed:10072753). Cohesin complexes are composed of the SMC1 (SMC1A or
CC meiosis-specific SMC1B) and SMC3 heterodimer attached via their SMC
CC hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2
CC or STAG3), which interacts with RAD21. Also found in meiosis-specific
CC cohesin complexes. Found in a complex with SMC1A, CDCA5 and RAD21,
CC PDS5A/SCC-112 and PDS5B/APRIN. Interacts with MXI1, MXD3 and MXD4.
CC Interacts with NUMA1, and forms a ternary complex with KIF3B and
CC KIFAP3, suggesting a function in tethering the chromosomes to the
CC spindle pole and a function in chromosome movement. Interacts with
CC PDS5A and WAPL; regulated by SMC3 acetylation. Interacts (via SMC hinge
CC domain) with KIAA1328 (via N- and C-terminal domains). Interacts with
CC DDX11, SYCP2 and STAG3. Found in a cohesin complex with SMC1A, RAD21
CC and STAG1. The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2
CC heterodimer (By similarity). Interacts with RPGR (PubMed:16043481).
CC Interacts with the NuRD complex component HDAC2; the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:P97690,
CC ECO:0000250|UniProtKB:Q9CW03, ECO:0000250|UniProtKB:Q9UQE7,
CC ECO:0000269|PubMed:10072753, ECO:0000269|PubMed:16043481}.
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. The phosphorylated form at Ser-1082 is
CC preferentially associated with unsynapsed chromosomal regions (By
CC similarity). {ECO:0000250|UniProtKB:Q9CW03}.
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-1082 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: Was originally isolated as a proteoglycan protein (explaining
CC its name). Although not excluded, such secreted function is not clear.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF072713; AAD13142.1; -; mRNA.
DR RefSeq; NP_776720.1; NM_174295.1.
DR BioGRID; 159045; 2.
DR STRING; 9913.ENSBTAP00000043550; -.
DR PaxDb; O97594; -.
DR PRIDE; O97594; -.
DR GeneID; 281729; -.
DR KEGG; bta:281729; -.
DR CTD; 9126; -.
DR eggNOG; KOG0964; Eukaryota.
DR InParanoid; O97594; -.
DR OrthoDB; 119789at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
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:0034990; C:nuclear mitotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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: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:0006275; P:regulation of DNA replication; ISS:UniProtKB.
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; DNA damage; DNA repair; Meiosis; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1218
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000119000"
FT DOMAIN 530..642
FT /note="SMC hinge"
FT REGION 239..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..350
FT /evidence="ECO:0000255"
FT COILED 393..503
FT /evidence="ECO:0000255"
FT COILED 669..916
FT /evidence="ECO:0000255"
FT COILED 958..989
FT /evidence="ECO:0000255"
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 1191
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
SQ SEQUENCE 1218 AA; 142024 MW; 2C7870C6D40A671E 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 SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKR RXERQSGLRM KEKGVVKGER
GSGPQSSVPS VDQFTGVGIR VSFTGKQGEM REMQQLSGGQ KSLVALALIF AIQKCDPAPF
YLFDEIDQAL DAQHRKAVSD MIMELAVHAQ FITTTFRPEL LESADKFYGV KFRNKVSHID
VITAEMAKDF VEDDTTHG
