SMC3_DICDI
ID SMC3_DICDI Reviewed; 1437 AA.
AC Q552D9; Q75JI4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE Short=SMC protein 3;
DE Short=SMC-3;
GN Name=smc3; ORFNames=DDB_G0276101;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Central component of cohesin, a complex which is required for
CC the cohesion of sister chromatids after DNA replication. The cohesin
CC complex may form a large proteinaceous ring within which sister
CC chromatids can be trapped. Involved in chromosome cohesion during the
CC cell cycle and in DNA repair it also regulates DNA replication. At
CC anaphase, the complex is cleaved and dissociates from chromatin,
CC allowing sister chromatids to segregate. The cohesin complex may also
CC play a role in spindle pole assembly during mitosis and in chromosomes
CC movement (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the cohesin complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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 SMC3, forming a V-shaped heterodimer.
CC The two heads of the heterodimer are then connected by different ends
CC of the cleavable RAD21 protein, forming a ring structure (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylation at Lys-107 by ESCO1 is important for genome stability
CC and S phase sister chromatid cohesion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000014; EAL69350.1; -; Genomic_DNA.
DR RefSeq; XP_643274.1; XM_638182.1.
DR AlphaFoldDB; Q552D9; -.
DR SMR; Q552D9; -.
DR STRING; 44689.DDB0219934; -.
DR PaxDb; Q552D9; -.
DR PRIDE; Q552D9; -.
DR EnsemblProtists; EAL69350; EAL69350; DDB_G0276101.
DR GeneID; 8620317; -.
DR KEGG; ddi:DDB_G0276101; -.
DR dictyBase; DDB_G0276101; smc3.
DR eggNOG; KOG0964; Eukaryota.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; Q552D9; -.
DR OMA; DQHQSMR; -.
DR PhylomeDB; Q552D9; -.
DR Reactome; R-DDI-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-DDI-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-DDI-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DDI-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:Q552D9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0008278; C:cohesin complex; ISS:dictyBase.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
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:0046982; F:protein heterodimerization activity; ISS:dictyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:dictyBase.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
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; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Coiled coil; Mitosis;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1437
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000365594"
FT DOMAIN 522..636
FT /note="SMC hinge"
FT REGION 1050..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 202..503
FT /evidence="ECO:0000255"
FT COILED 672..777
FT /evidence="ECO:0000255"
FT COILED 806..888
FT /evidence="ECO:0000255"
FT COILED 952..1007
FT /evidence="ECO:0000255"
FT COMPBIAS 1330..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 107
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1437 AA; 164847 MW; B35C8FEE5F5D0B15 CRC64;
MFIKFIFIKG FRSYKDQGFT SITLHPGFNV VTGRNGAGKS NLFAAIRFLL GDLNVGNNSE
DRLKLLHSYG GNTMQTGYVE IVFDNSDHRF PIDKTEFSLR RTFGTSKDEF SIGNNKLSKA
DVRNMFEAAG FSSSNPYYIV QQGKINTLAL MKDSDRLDML KEVAGATVYE ERKRESVAIM
IESESKSIKI EEFLKYIDER IKVLDKERKE LQLYQTQIEM KKQFEAYIIH LEANESNDRI
LDLEKEKEKY LIHSSKESKK LERFTDELKK DESKFNKLLS EIKKIDNEKI MVEKLNEVFD
KQKAQLVIQQ KHFKKLLSKE QAKLEKLQKE QDLLSGSKEK LEKEIEIIKP KLEELIGQED
DIDNKLSSTE RNLQELYVKQ GMFQFKSKTE RDKYLGDESS KLEDIVNQYE QQAQSLEEDV
EDMKQIQQSK GKQFDNSMAS KDKEAEIVKT AELRVHELKL EKDQIEQRVS STFQSINEMK
SNLTEHRNEW KKAERNLQTI MNRPLSEGLT RLNQIRQEGK IKGIHGPLVE LFDIVEPEAT
LALEVVGGNG LFHVVVDTDD TASKILEILN TENIGRLSFI PLNRVRTKPP KFPILENDLV
CPLIKVISFD PIYTEAMKLV FGKTLICKDE ATAEQVRKSS HVDCITFEGD VFHSKGAVTG
GYYSKKKLKL SSYQQIKHWR QQYQQLQTQL TEKESELEKL QASLLSIQKT IRTKEDEKNK
ILSNNDNSRV ELDKIISERT MYIEILEKKQ TILKKLKIDI QNCKDTIDGY QKQINTAFNT
KLTEEESNLL LTLSESSIQL KEQKISISSD VMKLQSRKNQ MTNQLNQNYG KRLMEIEGEI
KSLNPENSKL QIELKQKEID EINIEIDGVR EKLESLVQSL NEKDAEIKPI KVSIDALKQQ
TSTIADQLVA DGKKMESLLA QIQSFNKVRD AKQLRVLSKG DRFNFEELKK YNKDQSVEEL
NKINKSLASL RHVNQKANDQ FNSFTNQYNS LEARRDELYE SNASIQLLIK TLDNKKDEAI
ARTFSGVAKN FTQVFKELIP GGSAKLVMKR QMDEDEGEGE DPKEWADGET PKGLLTFTGI
GIQVSFGEGH EPCSMRQLSG GQKTLVALAL IFALQRTDPA PFYLLDEIDA ALDHNYRVAV
SKMIRKHSRE IQFIATTFGP EFVMDANQNW IVVFNKGGSK LVPGSTEDAL NVIKQLDNGS
AFDYSYQGIT EEEFNQDRPV LGVAENKHLV AFEFKRAKKR ALKALAKAEE ACAIMVQDEA
NQDSNADSSE KLKHDKKIFE KLHKEYLLRA AEFNQVKERF IRFGGIIKQQ GDDELSQSSQ
PQDKEMENIE KEKDNNQQTS DTEMKDTDQS TTKQKSPPKR KSPSQDTSDI ETSDDESKKK
QTESNQEESD IDEETPSQRF EEALNYASQK LKQHGLQESE QSEQEEDDDD ISSDSSD
