SMC1B_MOUSE
ID SMC1B_MOUSE Reviewed; 1248 AA.
AC Q920F6;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Structural maintenance of chromosomes protein 1B;
DE Short=SMC protein 1B;
DE Short=SMC-1-beta;
DE Short=SMC-1B;
GN Name=Smc1b; Synonyms=Smc1l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION
RP WITH SMC3, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=11564881; DOI=10.1128/mcb.21.20.6984-6998.2001;
RA Revenkova E., Eijpe M., Heyting C., Gross B., Jessberger R.;
RT "Novel meiosis-specific isoform of mammalian SMC1.";
RL Mol. Cell. Biol. 21:6984-6998(2001).
RN [2]
RP PROTEIN SEQUENCE OF 847-854, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP FUNCTION.
RX PubMed=15146193; DOI=10.1038/ncb1135;
RA Revenkova E., Eijpe M., Heyting C., Hodges C.A., Hunt P.A., Liebe B.,
RA Scherthan H., Jessberger R.;
RT "Cohesin SMC1 beta is required for meiotic chromosome dynamics, sister
RT chromatid cohesion and DNA recombination.";
RL Nat. Cell Biol. 6:555-562(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24287868; DOI=10.1007/s00412-013-0444-7;
RA Visnes T., Giordano F., Kuznetsova A., Suja J.A., Lander A.D., Calof A.L.,
RA Stroem L.;
RT "Localisation of the SMC loading complex Nipbl/Mau2 during mammalian
RT meiotic prophase I.";
RL Chromosoma 123:239-252(2014).
CC -!- FUNCTION: Meiosis-specific component of cohesin complex. Required for
CC the maintenance of meiotic cohesion, but not, or only to a minor
CC extent, for its establishment. Contributes to axial element (AE)
CC formation and the organization of chromatin loops along the AE. Plays a
CC key role in synapsis, recombination and chromosome movements. The
CC cohesin complex is required for the cohesion of sister chromatids after
CC DNA replication. The cohesin complex apparently forms a large
CC proteinaceous ring within which sister chromatids can be trapped. At
CC anaphase, the complex is cleaved and dissociates from chromatin,
CC allowing sister chromatids to segregate. The meiosis-specific cohesin
CC complex probably replaces mitosis specific cohesin complex when it
CC dissociates from chromatin during prophase I.
CC {ECO:0000269|PubMed:11564881, ECO:0000269|PubMed:15146193}.
CC -!- SUBUNIT: Forms a heterodimer with SMC3. Component of a meiosis-specific
CC cohesin complex, probably composed of the SMC1B and SMC3 heterodimer
CC attached via their SMC hinge domain, RAD21 (or its meiosis-specific
CC related protein REC8), which link them, and STAG3, which interacts with
CC RAD21 or REC8. {ECO:0000269|PubMed:11564881}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564881}. Chromosome
CC {ECO:0000269|PubMed:11564881, ECO:0000269|PubMed:24287868}. Chromosome,
CC centromere {ECO:0000269|PubMed:11564881}. Note=Associates with
CC chromatin. In prophase I stage of meiosis, localizes along the AE of
CC synaptonemal complexes. In late-pachytene-diplotene, the bulk of
CC protein dissociates from the chromosome arms probably because of
CC phosphorylation by PLK, except at centromeres, where cohesin complexes
CC remain. Remains chromatin associated at the centromeres up to metaphase
CC II. At anaphase II, dissociates from centromeres, allowing chromosomes
CC segregation. {ECO:0000269|PubMed:11564881}.
CC -!- TISSUE SPECIFICITY: Spermatocytes (at protein level). Testis and ovary
CC specific. Not expressed in somatic cells. {ECO:0000269|PubMed:11564881,
CC ECO:0000269|PubMed:24287868}.
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 or REC8 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; AF303827; AAL09333.1; -; mRNA.
DR CCDS; CCDS27718.1; -.
DR RefSeq; NP_536718.1; NM_080470.1.
DR AlphaFoldDB; Q920F6; -.
DR SMR; Q920F6; -.
DR BioGRID; 228280; 4.
DR CORUM; Q920F6; -.
DR IntAct; Q920F6; 8.
DR MINT; Q920F6; -.
DR STRING; 10090.ENSMUSP00000023068; -.
DR iPTMnet; Q920F6; -.
DR PhosphoSitePlus; Q920F6; -.
DR EPD; Q920F6; -.
DR MaxQB; Q920F6; -.
DR PaxDb; Q920F6; -.
DR PRIDE; Q920F6; -.
DR ProteomicsDB; 257204; -.
DR Antibodypedia; 233; 126 antibodies from 23 providers.
DR DNASU; 140557; -.
DR Ensembl; ENSMUST00000023068; ENSMUSP00000023068; ENSMUSG00000022432.
DR GeneID; 140557; -.
DR KEGG; mmu:140557; -.
DR UCSC; uc007xcx.1; mouse.
DR CTD; 27127; -.
DR MGI; MGI:2154049; Smc1b.
DR VEuPathDB; HostDB:ENSMUSG00000022432; -.
DR eggNOG; KOG0018; Eukaryota.
DR GeneTree; ENSGT00940000157633; -.
DR HOGENOM; CLU_001042_0_2_1; -.
DR InParanoid; Q920F6; -.
DR OMA; GIDNHEG; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; Q920F6; -.
DR TreeFam; TF101156; -.
DR BioGRID-ORCS; 140557; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Smc1b; mouse.
DR PRO; PR:Q920F6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q920F6; protein.
DR Bgee; ENSMUSG00000022432; Expressed in spermatid and 28 other tissues.
DR ExpressionAtlas; Q920F6; baseline and differential.
DR Genevisible; Q920F6; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IPI:MGI.
DR GO; GO:0007062; P:sister chromatid cohesion; IDA:MGI.
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; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Centromere; Chromosome; Coiled coil;
KW Direct protein sequencing; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1248
FT /note="Structural maintenance of chromosomes protein 1B"
FT /id="PRO_0000118994"
FT DOMAIN 514..629
FT /note="SMC hinge"
FT REGION 1219..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..502
FT /evidence="ECO:0000255"
FT COILED 666..912
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 648
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 713
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 1032
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CU62"
SQ SEQUENCE 1248 AA; 144513 MW; 6C31DB46217BC94D CRC64;
MGHLELLLVE NFKSWRGRQV IGPFKRFTCI IGPNGSGKSN VMDALSFVMG EKTTNLRVKN
IQELIHGAHT GKPVSSSASV TIIYIEDSGE EKTFTRIIRG GCSEYHFGDK PVSRSVYVAQ
LENIGIIVKA QNCLVFQGTV ESISMKKPKE RTQFFEEIST SGEFIGEYEA KKKKLQKAEE
DAQFHFNVKK NVAAERKHAK IEKEEAEHYQ NLLEELKINK IQLMLFQLYY NEEKINVLNT
ELEQMDGNLS VVKDTLSHHE NIFKAKKKDY GMLTRQLQQT AKELKSVEAI LNQKRPQYIK
AKENTSHHLK KLDLSKKLIT DNEKQCSKQE DGIRALVAEL ADLDRAWKSF EKQMEEKILQ
KGRDIELENS QLDRYKLLKE QVRRKVGIMT QQLEKLQWEQ KAEKERLAFE KRRHGDTQGN
LKQIKEQIEE HKKRIEKLEE YTKTCMDCLE DKKQQEEALK KEIENTKSRM SEVNEELSLI
RNELQNAGID NHEGKRQQKR AEVLEHLKRL YPDSVFGRLL DLCHPIHKKY QLAVTKLFGR
YMVAIVVASE KIAKDCIRFL KAERAEPETF LALDYLDIKP INERLREIKG CKMMIDVIKT
QFPQLKKVIQ FVCGNGLVCE TVEEARHIAF GGPERRKAVA LDGTLFLKSG VISGGSSDLK
HKALCWDEKE LHNLRDKRSQ LVQELKELMK TLRKETDLKQ IQTLVQGTNT RLKYSQNELE
MIKKKHLATF YREQSQLQSE LLNIDSQCTM LSEGINKQQQ KIEEFQDKID EVEDDIFQDF
CEEIGVENIR EFENKHVKQQ QENDQKRLEF EKQKTRLNIQ LEYSRNQLKK KLNNIDTLKT
TIQKGKEDID NLKKTEEECL KIVEELMVKQ EQIKEVLATQ SSNIEKIHIQ IEEERKKVLA
VDREVGKLQK EVVIIQGSLE QKLLEKHNLL LDCKVQDIDI SLVLGSLEDI IEMELTETES
TQATADIYEK EASIQIDYSP LREDLKALQS DKEVEAHLTL LLQQVASQEN TLLKTTAPNL
RAQENLKTVR DKFQESADVF EASRKEARIC RQEFEQVKRR RYDAFSQCFE HISVSIDQIY
KKLCRNNSAQ AFLSPENPEE PYLDGISYNC VAPGKRFMPM DNLSGGEKCV AALALLFAVH
SFRPAPFFVL DEVDAALDNT NIGKVSSYIK EQSQEQFQMI IISLKEEFYS KADALIGVYP
EHNECMFSHV LTLDLSKYPD TEDQEGSRSH RKPRVPRVSM SPKSPQSR
