SMC3_SCHPO
ID SMC3_SCHPO Reviewed; 1194 AA.
AC O42649;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE AltName: Full=Cohesin complex Psm3 subunit;
GN Name=psm3; Synonyms=smc3; ORFNames=SPAC10F6.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COHESIN COMPLEX
RP WITH PSM1 AND RAD21.
RX PubMed=11069892; DOI=10.1101/gad.832000;
RA Tomonaga T., Nagao K., Kawasaki Y., Furuya K., Murakami A., Morishita J.,
RA Yuasa T., Sutani T., Kearsey S.E., Uhlmann F., Nasmyth K., Yanagida M.;
RT "Characterization of fission yeast cohesin: essential anaphase proteolysis
RT of Rad21 phosphorylated in the S phase.";
RL Genes Dev. 14:2757-2770(2000).
CC -!- FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA
CC repair. Central component of cohesin complex. The cohesin complex is
CC required for the cohesion of sister chromatids after DNA replication.
CC The cohesin complex apparently forms a large proteinaceous ring within
CC which sister chromatids can be trapped. At anaphase, the complex is
CC cleaved and dissociates from chromatin, allowing sister chromatids to
CC segregate. {ECO:0000269|PubMed:11069892}.
CC -!- SUBUNIT: Cohesin complexes are composed of the psm1/smc1 and psm3/smc3
CC heterodimer attached via their SMC hinge domain, rad21/scc1 which link
CC them, and psc3/scc3, which interacts with rad21.
CC {ECO:0000269|PubMed:11069892}.
CC -!- INTERACTION:
CC O42649; Q09725: mis4; NbExp=3; IntAct=EBI-1151879, EBI-16083239;
CC O42649; O94383: psm1; NbExp=3; IntAct=EBI-1151879, EBI-1151900;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11069892}. Chromosome
CC {ECO:0000269|PubMed:11069892}. Note=Associates with chromatin. Before
CC prophase it is scattered along chromosome arms. At anaphase, the rad21
CC subunit of the cohesin complex is cleaved, leading to the dissociation
CC of the complex from chromosomes, allowing chromosome separation.
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 psm1, 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-105 and Lys-106 by ECO1 is important for genome
CC stability 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; CU329670; CAA15722.1; -; Genomic_DNA.
DR PIR; T37503; T37503.
DR RefSeq; NP_593260.1; NM_001018657.2.
DR PDB; 6YUF; EM; 3.94 A; C=1-1194.
DR PDBsum; 6YUF; -.
DR AlphaFoldDB; O42649; -.
DR SMR; O42649; -.
DR BioGRID; 279448; 24.
DR DIP; DIP-35366N; -.
DR IntAct; O42649; 3.
DR STRING; 4896.SPAC10F6.09c.1; -.
DR iPTMnet; O42649; -.
DR MaxQB; O42649; -.
DR PaxDb; O42649; -.
DR PRIDE; O42649; -.
DR EnsemblFungi; SPAC10F6.09c.1; SPAC10F6.09c.1:pep; SPAC10F6.09c.
DR GeneID; 2543010; -.
DR KEGG; spo:SPAC10F6.09c; -.
DR PomBase; SPAC10F6.09c; psm3.
DR VEuPathDB; FungiDB:SPAC10F6.09c; -.
DR eggNOG; KOG0964; Eukaryota.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; O42649; -.
DR OMA; DQHQSMR; -.
DR PhylomeDB; O42649; -.
DR Reactome; R-SPO-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-SPO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:O42649; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0008278; C:cohesin complex; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0030892; C:mitotic cohesin complex; IDA:PomBase.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0140588; P:chromatin looping; IDA:PomBase.
DR GO; GO:0061780; P:mitotic cohesin loading; IDA:PomBase.
DR GO; GO:0062022; P:mitotic cohesin ssDNA (lagging strand) loading; IDA:PomBase.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP: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 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Chromosome; Coiled coil; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1194
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000119014"
FT DOMAIN 522..634
FT /note="SMC hinge"
FT COILED 176..497
FT /evidence="ECO:0000255"
FT COILED 668..908
FT /evidence="ECO:0000255"
FT COILED 970..1006
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1194 AA; 136850 MW; FD4D1E81A9E2E423 CRC64;
MYITKIVIQG FKSYKDYTVI EPLSPHHNVI VGRNGSGKSN FFAAIRFVLS DAYTHLSREE
RQALLHEGPG ATVMSAYVEV TFANADNRFP TGKSEVVLRR TIGLKKDEYS LDKKTVSKTE
VINLLESAGF SRSNPYYIVP QGRVTSLTNA KDSERLELLK EVAGTQIYEN RRAESNKIMD
ETIQKSEKID ELLQYIEERL RELEEEKNDL AVYHKKDNER RCLEYAIYSR EHDEINSVLD
ALEQDRIAAL ERNDDDSGAF IQREERIERI KAEITELNHS LELLRVEKQQ NDEDYTNIMK
SKVALELQSS QLSRQIEFSK KDESSKLNIL SELESKISEK ENELSEILPK YNAIVSEADD
LNKRIMLLKN QKQSLLDKQS RTSQFTTKKE RDEWIRNQLL QINRNINSTK ENSDYLKTEY
DEMENELKAK LSRKKEIEIS LESQGDRMSQ LLANITSINE RKENLTDKRK SLWREEAKLK
SSIENVKDDL SRSEKALGTT MDRNTSNGIR AVKDIAERLK LEGYYGPLCE LFKVDNRFKV
AVEATAGNSL FHIVVDNDET ATQILDVIYK ENAGRVTFMP LNKLRPKAVT YPDASDALPL
IQYLEFDPKF DAAIKQVFSK TIVCPSIETA SQYARSHQLN GITLSGDRSD KKGALTAGYR
DYRNSRLDAI KNVKTYQIKF SDLQESLEKC RSEIESFDQK ITACLDDLQK AQLSLKQFER
DHIPLKDELV TITGETTDLQ ESMHHKSRML ELVVLELHTL EQQANDLKSE LSSEMDELDP
KDVEALKSLS GQIENLSHEF DAIIKERAHI EARKTALEYE LNTNLYLRRN PLKAEIGSDN
RIDESELNSV KRSLLKYENK LQIIKSSSSG LEEQMQRINS EISDKRNELE SLEELQHEVA
TRIEQDAKIN ERNAAKRSLL LARKKECNEK IKSLGVLPEE AFIKYVSTSS NAIVKKLHKI
NEALKDYGSV NKKAYEQFNN FTKQRDSLLA RREELRRSQE SISELTTVLD QRKDEAIERT
FKQVAKSFSE IFVKLVPAGR GELVMNRRSE LSQSIEQDIS MDIDTPSQKS SIDNYTGISI
RVSFNSKDDE QLNINQLSGG QKSLCALTLI FAIQRCDPAP FNILDECDAN LDAQYRSAIA
AMVKEMSKTS QFICTTFRPE MVKVADNFYG VMFNHKVSTV ESISKEEAMA FVEG
