SMC6_MOUSE
ID SMC6_MOUSE Reviewed; 1097 AA.
AC Q924W5; Q3UFI5; Q3UX54; Q499E1; Q5DTN2; Q8BFU9; Q8R0T4; Q9CSK7; Q9CV94;
AC Q9CZZ5; Q9D169; Q9D6B2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Structural maintenance of chromosomes protein 6;
DE Short=SMC protein 6;
DE Short=SMC-6;
DE Short=mSMC6;
GN Name=Smc6; Synonyms=Kiaa4103, Smc6l1;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=11408570; DOI=10.1091/mbc.12.6.1583;
RA Taylor E.M., Moghraby J.S., Lees J.H., Smit B., Moens P.B., Lehmann A.R.;
RT "Characterization of a novel human SMC heterodimer homologous to the
RT Schizosaccharomyces pombe Rad18/Spr18 complex.";
RL Mol. Biol. Cell 12:1583-1594(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-767 AND 797-1097 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Egg, Extraembryonic tissue, Liver, Pancreas, Placenta, Thymus, and
RC Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Egg;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-1097 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and 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).
CC -!- FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved
CC in repair of DNA double-strand breaks by homologous recombination. The
CC complex may promote sister chromatid homologous recombination by
CC recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The
CC complex is required for telomere maintenance via recombination and
CC mediates sumoylation of shelterin complex (telosome) components (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC5. Component of the SMC5-SMC6
CC complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A
CC or EID3 and NSMCE3. Interacts with NSMCE1. Interacts with NSMCE2.
CC Interacts with SLF1. Interacts with SLF2. Interacts with RAD18.
CC {ECO:0000250|UniProtKB:Q96SB8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11408570}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q96SB8}. Chromosome
CC {ECO:0000269|PubMed:11408570}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q96SB8}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q96SB8}. Note=Localizes to PML nuclear bodies in
CC ALT cell lines. Associates with chromatin. Accumulates with RAD18 and
CC the SLF1-SLF2 complex at replication-coupled DNA interstrand repair and
CC DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-
CC dependent manner. Localizes in interchromatin granule clusters (By
CC similarity). Colocalizes with SMC5 on the X-Y chromosome pair within
CC the sex vesicle during late pachytene/diplotene (PubMed:11408570).
CC {ECO:0000250|UniProtKB:Q96SB8, ECO:0000269|PubMed:11408570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q924W5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924W5-2; Sequence=VSP_022254, VSP_022255;
CC -!- DOMAIN: The flexible hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC5, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Sumoylated by NSMCE2/MMS21. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ310552; CAC39250.1; -; mRNA.
DR EMBL; AK003872; BAB23051.1; ALT_INIT; mRNA.
DR EMBL; AK009009; BAB26022.3; -; mRNA.
DR EMBL; AK011982; BAB27956.1; -; mRNA.
DR EMBL; AK012626; BAB28365.1; -; mRNA.
DR EMBL; AK014442; BAB29353.2; -; mRNA.
DR EMBL; AK050341; BAC34200.2; -; mRNA.
DR EMBL; AK088002; BAC40087.2; -; mRNA.
DR EMBL; AK135873; BAE22709.1; -; mRNA.
DR EMBL; AK148478; BAE28576.1; -; mRNA.
DR EMBL; BC026429; AAH26429.1; -; mRNA.
DR EMBL; BC048790; AAH48790.1; -; mRNA.
DR EMBL; BC090630; AAH90630.1; -; mRNA.
DR EMBL; BC099955; AAH99955.1; -; mRNA.
DR EMBL; AK220488; BAD90287.1; -; mRNA.
DR CCDS; CCDS25815.1; -. [Q924W5-1]
DR CCDS; CCDS88313.1; -. [Q924W5-2]
DR RefSeq; NP_001311405.1; NM_001324476.1.
DR RefSeq; NP_079971.2; NM_025695.4. [Q924W5-1]
DR AlphaFoldDB; Q924W5; -.
DR SMR; Q924W5; -.
DR BioGRID; 212040; 12.
DR IntAct; Q924W5; 9.
DR STRING; 10090.ENSMUSP00000020931; -.
DR iPTMnet; Q924W5; -.
DR PhosphoSitePlus; Q924W5; -.
DR EPD; Q924W5; -.
DR MaxQB; Q924W5; -.
DR PaxDb; Q924W5; -.
DR PeptideAtlas; Q924W5; -.
DR PRIDE; Q924W5; -.
DR ProteomicsDB; 261521; -. [Q924W5-1]
DR ProteomicsDB; 261522; -. [Q924W5-2]
DR Antibodypedia; 27034; 171 antibodies from 27 providers.
DR DNASU; 67241; -.
DR Ensembl; ENSMUST00000020931; ENSMUSP00000020931; ENSMUSG00000020608. [Q924W5-1]
DR Ensembl; ENSMUST00000218866; ENSMUSP00000151976; ENSMUSG00000020608. [Q924W5-2]
DR GeneID; 67241; -.
DR KEGG; mmu:67241; -.
DR UCSC; uc007nax.1; mouse. [Q924W5-2]
DR UCSC; uc007nay.1; mouse. [Q924W5-1]
DR CTD; 79677; -.
DR MGI; MGI:1914491; Smc6.
DR VEuPathDB; HostDB:ENSMUSG00000020608; -.
DR eggNOG; KOG0250; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR HOGENOM; CLU_009063_0_1_1; -.
DR InParanoid; Q924W5; -.
DR OMA; MCHDHFY; -.
DR OrthoDB; 263113at2759; -.
DR PhylomeDB; Q924W5; -.
DR TreeFam; TF314520; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 67241; 27 hits in 108 CRISPR screens.
DR ChiTaRS; Smc6; mouse.
DR PRO; PR:Q924W5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q924W5; protein.
DR Bgee; ENSMUSG00000020608; Expressed in embryonic post-anal tail and 261 other tissues.
DR ExpressionAtlas; Q924W5; baseline and differential.
DR Genevisible; Q924W5; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0035061; C:interchromatin granule; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0000803; C:sex chromosome; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosome; Coiled coil; DNA damage;
KW DNA recombination; DNA repair; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
FT CHAIN 1..1097
FT /note="Structural maintenance of chromosomes protein 6"
FT /id="PRO_0000270957"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..667
FT /note="Flexible hinge"
FT REGION 813..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 232..348
FT /evidence="ECO:0000255"
FT COILED 376..457
FT /evidence="ECO:0000255"
FT COILED 668..920
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB8"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96SB8"
FT CROSSLNK 779
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96SB8"
FT VAR_SEQ 323..326
FT /note="RLND -> LQAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022254"
FT VAR_SEQ 327..1097
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022255"
FT CONFLICT 120
FT /note="Q -> W (in Ref. 4; BAD90287)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="E -> K (in Ref. 2; BAE22709)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="E -> A (in Ref. 3; AAH99955)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="A -> V (in Ref. 3; AAH99955)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="K -> E (in Ref. 2; BAB29353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1097 AA; 127198 MW; 7329C25A85102DE5 CRC64;
MAKRKEENFC SPENAKRPRQ EELEDFDKDG DEDECTISFT NGTSTLTAAE VGIIESIQLR
NFMCHSMLGP FKFGSNVNFV VGNNGSGKSA VLTALIVGLG GKAVATNRGS SLKGFVKAGQ
NSADISITLR NRGDDAFRAN VYGDSIVVQQ HISVDGSRSY KLKSEKGTVV STRKEELIAI
LDHFNIQVDN PVSVLTQEMS KQFLQSKNEG DKYKFFMKAT QLEQMKEDYS YIMETKERTK
EQINQGEERL TELKRQCLEK EERFQNIAGL STMKTNLEYL KHEMAWAVVN EIEKQLNAIR
DNIKIGEERA AKLDRKMEEQ QVRLNDAEKK YKDIQDKLEK ISEETNARAP ECMALKTDVI
ARTRAFNDAE VLYNRSLNEY KALKKDGEQL CKRIEELKKS TDQSLEPERL ERQKRICWLK
EKVKALQDQE HTVNQEAEQF EQAIEKDKQE HGRVRKEDIE VRHALNYNQR QLKELKDSKT
DRLKRFGPHV PALLEAIDDA YRRRQFTHKP IGPLGACIHL RDPELALAIE SCLKGLLQAY
CCHNHADERV LQSLMKKFYP PGTSRPQIIV SEFRDEVYDV RLRAAYHPEF PTVLTALEID
NAVVANSLID MRSIETVLLI KNNSVARAVM QSQKPPKNCR EAFTADGDQV FAGRYYSSES
TRPKFLSRDV DSEISDLETE IENKKGHIIT LQQRLSALEK DIKRNEELLK RCQLHYKEIK
MKIRKNISEI RELENIEEHQ SVDIATLEDE AEENKIKMQM VEKNMEQQKE NMENLKSLKI
EAENKYDTIK LKINQLSELA DPLKDELNLA DSEVDSQKRG KQHYEDKQKE HLDTLNKKRR
ELDMKEKELQ EKMSQARQIC PERIEVKKSA SILDKEINRL RQKIQAEHAS HGDREEIMKQ
YQEARETYLD LDNKVRTLRR FIKLLEEIMT HRYKTYQQFR RCLTLRCKLY FDNLLSQRAY
CGKMNFDHKN ETLSITVQPG EGNKASFNDM RALSGGERSF STVCFILSLW SIAESPFRCL
DEFDVYMDMV NRRIAMDMIL KMADSQRFRQ FILLTPQSMS SLPSSKLIRI LRMSDPERGQ
TTLPFRPVTQ EEDDSAS
