SMC1_SCHPO
ID SMC1_SCHPO Reviewed; 1228 AA.
AC O94383;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Structural maintenance of chromosomes protein 1;
DE AltName: Full=Chromosome segregation protein smc1;
DE AltName: Full=Cohesin complex subunit psm1;
GN Name=psm1; Synonyms=smc1; ORFNames=SPBC29A10.04;
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 [GENOMIC DNA], CHARACTERIZATION, AND SUBCELLULAR
RP LOCATION.
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).
RN [2] {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 [3]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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.
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 -!- INTERACTION:
CC O94383; O42649: psm3; NbExp=3; IntAct=EBI-1151900, EBI-1151879;
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 psm3, 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 -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA22432.2; -; Genomic_DNA.
DR PIR; T40059; T40059.
DR RefSeq; NP_596049.2; NM_001021960.2.
DR PDB; 6YUF; EM; 3.94 A; A=1-1228.
DR PDBsum; 6YUF; -.
DR AlphaFoldDB; O94383; -.
DR SMR; O94383; -.
DR BioGRID; 277084; 30.
DR IntAct; O94383; 2.
DR STRING; 4896.SPBC29A10.04.1; -.
DR iPTMnet; O94383; -.
DR MaxQB; O94383; -.
DR PaxDb; O94383; -.
DR PRIDE; O94383; -.
DR EnsemblFungi; SPBC29A10.04.1; SPBC29A10.04.1:pep; SPBC29A10.04.
DR GeneID; 2540557; -.
DR KEGG; spo:SPBC29A10.04; -.
DR PomBase; SPBC29A10.04; psm1.
DR VEuPathDB; FungiDB:SPBC29A10.04; -.
DR eggNOG; KOG0018; Eukaryota.
DR HOGENOM; CLU_001042_0_1_1; -.
DR InParanoid; O94383; -.
DR OMA; YIRDHTT; -.
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:O94383; -.
DR Proteomes; UP000002485; Chromosome II.
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:0030892; C:mitotic cohesin complex; IDA:PomBase.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; 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; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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 GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR CDD; cd03275; ABC_SMC1_euk; 2.
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; IPR028468; Smc1_ABC.
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; ATP-binding; Cell cycle; Cell division; Chromosome;
KW Coiled coil; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1228
FT /note="Structural maintenance of chromosomes protein 1"
FT /id="PRO_0000119010"
FT DOMAIN 522..635
FT /note="SMC hinge"
FT COILED 197..510
FT /evidence="ECO:0000255"
FT COILED 710..783
FT /evidence="ECO:0000255"
FT COILED 814..926
FT /evidence="ECO:0000255"
FT COILED 984..1068
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1228 AA; 140522 MW; 915817D9AF404CEC CRC64;
MGRLLRLEVE NFKSYRGHQI IGPFEDFTSI IGPNGAGKSN LMDAISFVLG VKSSHLRSTN
VKELIYRGKI LQRDNTDFTD SSNPTTAYVK LMYELDNGEQ REYKRAITPS GATEYKIDEE
IVTFSEYCGS LQKENILVRA RNFLVFQGDV ETIASQSPLE LSKLVEQISG SLEYKSEYDK
SKDEQDKAVN LSAHSFNKKR GINAELRQYQ EQKTEAERYQ SQKEKRDSAQ LVYLLWKLFH
LEKSISSNMA EVTRLKADSI QLIERRDENT KEIEKLKEKE GSIRRNLLAF DRKVRKQEKL
IASKRPELIS IAEKALESKS NLRKIQRKAA EIEKDYSDQA STLQVLENQL TSLSAAEKEF
LKDMQEKEQL KGLRLLPEDK EEYEGLRSEA DKLNSNLLFK LQTLNRNIKV TSQSKDSLTS
IVGDLESKIK SLHESVSSLD TERADLLAKI NEKIESLELE KHDQQKKRLT YSELFHKTQE
LNEELQSCLQ KILEASADRN ESKQDAKKRE ALYALKRIYP EVKGRIIDLC TPTQKKYESA
IAAALGKNFD AIVVETQAVA KECIDYIKEQ RIGIMTFFPM DTIAASPVNQ KFRGTHKGAR
LAIDVLNFES EYERVMISAV GNTLICDSMT VARDLSYNKR LNAKTVTLEG TVIHKTGLIT
GGSSNNRSAK HWDDHDFDLL TQTKDRLMHQ IGEIEYQKSS CVITESDTVK LHSLESEISL
LKDKYTVVSR SVEDKKKEIG HYESLIKEKQ PHLSELEMEL RNFVKSRDEL QIQVEKVEEK
IFSGFCKRIG ISDIHTYDEI HRTFTQSFTQ KQLEFTKQKS LLENRISFEK QRVSDTRLRL
ERMHKFIEKD QESIDNYEQN REALESEVAT AEAELELLKE DFASENSKTE KILLAASEKK
LVGKRLVSEL TKLSGNITLL ESEIDRYVSE WHAILRKCKL EDIDVPLREG SLTSIPIDDV
SNSGDITMGE EPSEPVINFE KFGVEVDYDE LDEELRNDGS ESMASVLQEK LREYSEELDQ
MSPNLRAIER LETVETRLAK LDEEFAAARK AAKNAKERFN AVKQKRLQKF QAAFSHISEQ
IDPIYKELTK SPAFPLGGTA YLTLDDLDEP YLGGIKFHAM PPMKRFRDMD QLSGGEKTMA
ALALLFAIHS YQPSPFFVLD EIDAALDQTN VTKIANYIRQ HASSGFQFVV ISLKNQLFSK
SEALVGIYRD QQENSSRTLS INLEGYVE
