SMHD1_MOUSE
ID SMHD1_MOUSE Reviewed; 2007 AA.
AC Q6P5D8; Q6PDM8; Q6PE93; Q6ZQ78; Q811H3; Q8BP09; Q9D4M7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Structural maintenance of chromosomes flexible hinge domain-containing protein 1 {ECO:0000303|PubMed:18425126};
DE Short=SMC hinge domain-containing protein 1 {ECO:0000303|PubMed:18425126};
DE EC=3.6.1.- {ECO:0000269|PubMed:26391951, ECO:0000269|PubMed:27059856};
GN Name=Smchd1 {ECO:0000303|PubMed:18425126, ECO:0000312|MGI:MGI:1921605};
GN Synonyms=Kiaa0650 {ECO:0000303|PubMed:14621295};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-272 AND 1116-2007.
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct;
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] OF 660-2007.
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Eye, and Mammary tumor;
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 942-2007.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=18425126; DOI=10.1038/ng.142;
RA Blewitt M.E., Gendrel A.V., Pang Z., Sparrow D.B., Whitelaw N., Craig J.M.,
RA Apedaile A., Hilton D.J., Dunwoodie S.L., Brockdorff N., Kay G.F.,
RA Whitelaw E.;
RT "SmcHD1, containing a structural-maintenance-of-chromosomes hinge domain,
RT has a critical role in X inactivation.";
RL Nat. Genet. 40:663-669(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, 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).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=21553025; DOI=10.1007/s00412-011-0318-9;
RA Roberts A.R., Blewitt M.E., Youngson N.A., Whitelaw E., Chong S.;
RT "Reduced dosage of the modifiers of epigenetic reprogramming Dnmt1, Dnmt3L,
RT SmcHD1 and Foxo3a has no detectable effect on mouse telomere length in
RT vivo.";
RL Chromosoma 120:377-385(2011).
RN [8]
RP FUNCTION.
RX PubMed=22841499; DOI=10.1016/j.devcel.2012.06.011;
RA Gendrel A.V., Apedaile A., Coker H., Termanis A., Zvetkova I., Godwin J.,
RA Tang Y.A., Huntley D., Montana G., Taylor S., Giannoulatou E., Heard E.,
RA Stancheva I., Brockdorff N.;
RT "Smchd1-dependent and -independent pathways determine developmental
RT dynamics of CpG island methylation on the inactive X chromosome.";
RL Dev. Cell 23:265-279(2012).
RN [9]
RP SUMOYLATION WITH SUMO1.
RX PubMed=23213215; DOI=10.1073/pnas.1215366110;
RA Tirard M., Hsiao H.H., Nikolov M., Urlaub H., Melchior F., Brose N.;
RT "In vivo localization and identification of SUMOylated proteins in the
RT brain of His6-HA-SUMO1 knock-in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21122-21127(2012).
RN [10]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-1803, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23754746; DOI=10.1128/mcb.00145-13;
RA Gendrel A.V., Tang Y.A., Suzuki M., Godwin J., Nesterova T.B.,
RA Greally J.M., Heard E., Brockdorff N.;
RT "Epigenetic functions of smchd1 repress gene clusters on the inactive X
RT chromosome and on autosomes.";
RL Mol. Cell. Biol. 33:3150-3165(2013).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23819640; DOI=10.1186/1756-8935-6-19;
RA Mould A.W., Pang Z., Pakusch M., Tonks I.D., Stark M., Carrie D.,
RA Mukhopadhyay P., Seidel A., Ellis J.J., Deakin J., Wakefield M.J.,
RA Krause L., Blewitt M.E., Kay G.F.;
RT "Smchd1 regulates a subset of autosomal genes subject to monoallelic
RT expression in addition to being critical for X inactivation.";
RL Epigenetics Chromatin 6:19-19(2013).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION
RP WITH LRIF1, AND MUTAGENESIS OF GLU-147 AND 1872-GLY--GLY-1876.
RX PubMed=26391951; DOI=10.1128/mcb.00432-15;
RA Brideau N.J., Coker H., Gendrel A.V., Siebert C.A., Bezstarosti K.,
RA Demmers J., Poot R.A., Nesterova T.B., Brockdorff N.;
RT "Independent Mechanisms Target SMCHD1 to Trimethylated Histone H3 Lysine 9-
RT Modified Chromatin and the Inactive X Chromosome.";
RL Mol. Cell. Biol. 35:4053-4068(2015).
RN [14]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ARG-1867.
RX PubMed=26091879; DOI=10.1073/pnas.1504232112;
RA Chen K., Hu J., Moore D.L., Liu R., Kessans S.A., Breslin K., Lucet I.S.,
RA Keniry A., Leong H.S., Parish C.L., Hilton D.J., Lemmers R.J.,
RA van der Maarel S.M., Czabotar P.E., Dobson R.C., Ritchie M.E., Kay G.F.,
RA Murphy J.M., Blewitt M.E.;
RT "Genome-wide binding and mechanistic analyses of Smchd1-mediated epigenetic
RT regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E3535-E3544(2015).
RN [15]
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-1867.
RX PubMed=26733688; DOI=10.1042/bj20151049;
RA Chen K., Czabotar P.E., Blewitt M.E., Murphy J.M.;
RT "The hinge domain of the epigenetic repressor Smchd1 adopts an
RT unconventional homodimeric configuration.";
RL Biochem. J. 473:733-742(2016).
RN [16]
RP FUNCTION, SUBUNIT, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=27059856; DOI=10.1042/bcj20160189;
RA Chen K., Dobson R.C., Lucet I.S., Young S.N., Pearce F.G., Blewitt M.E.,
RA Murphy J.M.;
RT "The epigenetic regulator Smchd1 contains a functional GHKL-type ATPase
RT domain.";
RL Biochem. J. 473:1733-1744(2016).
RN [17]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28067911; DOI=10.1038/ng.3765;
RA Gordon C.T., Xue S., Yigit G., Filali H., Chen K., Rosin N., Yoshiura K.I.,
RA Oufadem M., Beck T.J., McGowan R., Magee A.C., Altmueller J., Dion C.,
RA Thiele H., Gurzau A.D., Nuernberg P., Meschede D., Muehlbauer W.,
RA Okamoto N., Varghese V., Irving R., Sigaudy S., Williams D., Ahmed S.F.,
RA Bonnard C., Kong M.K., Ratbi I., Fejjal N., Fikri M., Elalaoui S.C.,
RA Reigstad H., Bole-Feysot C., Nitschke P., Ragge N., Levy N., Tuncbilek G.,
RA Teo A.S., Cunningham M.L., Sefiani A., Kayserili H., Murphy J.M.,
RA Chatdokmaiprai C., Hillmer A.M., Wattanasirichaigoon D., Lyonnet S.,
RA Magdinier F., Javed A., Blewitt M.E., Amiel J., Wollnik B., Reversade B.;
RT "De novo mutations in SMCHD1 cause Bosma arhinia microphthalmia syndrome
RT and abrogate nasal development.";
RL Nat. Genet. 49:249-255(2017).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28587678; DOI=10.1186/s13395-017-0129-7;
RA Mason A.G., Slieker R.C., Balog J., Lemmers R.J.L.F., Wong C.J., Yao Z.,
RA Lim J.W., Filippova G.N., Ne E., Tawil R., Heijmans B.T., Tapscott S.J.,
RA van der Maarel S.M.;
RT "SMCHD1 regulates a limited set of gene clusters on autosomal
RT chromosomes.";
RL Skelet. Muscle 7:12-12(2017).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29887375; DOI=10.1016/j.cell.2018.05.007;
RA Wang C.Y., Jegu T., Chu H.P., Oh H.J., Lee J.T.;
RT "SMCHD1 merges chromosome compartments and assists formation of super-
RT structures on the inactive X.";
RL Cell 0:0-0(2018).
RN [20]
RP FUNCTION, AND INDUCTION.
RX PubMed=29900695; DOI=10.1002/mrd.23001;
RA Midic U., Vincent K.A., Wang K., Lokken A., Severance A.L., Ralston A.,
RA Knott J.G., Latham K.E.;
RT "Novel key roles for Structural maintenance of chromosome flexible domain
RT containing 1 (Smchd1) during preimplantation mouse development.";
RL Mol. Reprod. Dev. 85:635-648(2018).
CC -!- FUNCTION: Non-canonical member of the structural maintenance of
CC chromosomes (SMC) protein family that plays a key role in epigenetic
CC silencing by regulating chromatin architecture (PubMed:26091879,
CC PubMed:29887375). Promotes heterochromatin formation in both autosomes
CC and chromosome X, probably by mediating the merge of chromatin
CC compartments (PubMed:23754746, PubMed:23819640, PubMed:26391951,
CC PubMed:28587678, PubMed:29887375). Plays a key role in chromosome X
CC inactivation in females by promoting the spreading of heterochromatin
CC (PubMed:18425126, PubMed:22841499, PubMed:26391951, PubMed:29887375).
CC Recruited to inactivated chromosome X by Xist RNA and acts by mediating
CC the merge of chromatin compartments: promotes random chromatin
CC interactions that span the boundaries of existing structures, leading
CC to create a compartment-less architecture typical of inactivated
CC chromosome X (PubMed:29887375). Required to facilitate Xist RNA
CC spreading (PubMed:29887375). Also required for silencing of a subset of
CC clustered autosomal loci in somatic cells, such as the DUX4 locus
CC (PubMed:23754746, PubMed:23819640, PubMed:28587678). Has ATPase
CC activity; may participate in structural manipulation of chromatin in an
CC ATP-dependent manner as part of its role in gene expression regulation
CC (PubMed:26391951, PubMed:27059856). Also plays a role in DNA repair:
CC localizes to sites of DNA double-strand breaks in response to DNA
CC damage to promote the repair of DNA double-strand breaks (By
CC similarity). Acts by promoting non-homologous end joining (NHEJ) and
CC inhibiting homologous recombination (HR) repair (By similarity).
CC Required during preimplantation development, probably acts by
CC regulating chromatin architecture (PubMed:29900695).
CC {ECO:0000250|UniProtKB:A6NHR9, ECO:0000269|PubMed:18425126,
CC ECO:0000269|PubMed:22841499, ECO:0000269|PubMed:23754746,
CC ECO:0000269|PubMed:23819640, ECO:0000269|PubMed:26091879,
CC ECO:0000269|PubMed:26391951, ECO:0000269|PubMed:27059856,
CC ECO:0000269|PubMed:28587678, ECO:0000269|PubMed:29887375,
CC ECO:0000269|PubMed:29900695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:26391951, ECO:0000269|PubMed:27059856};
CC -!- SUBUNIT: Homodimer; homodimerizes via its SMC hinge domain
CC (PubMed:26391951, PubMed:26733688, PubMed:27059856). Interacts with
CC LRIF1 (PubMed:26391951). {ECO:0000269|PubMed:26391951,
CC ECO:0000269|PubMed:26733688, ECO:0000269|PubMed:27059856}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:18425126,
CC ECO:0000269|PubMed:26391951, ECO:0000269|PubMed:29887375}.
CC Note=Recruited to inactivated chromosome X in females by Xist RNA
CC (PubMed:29887375). Localizes at sites of DNA damage at double-strand
CC breaks (DSBs) (By similarity). {ECO:0000250|UniProtKB:A6NHR9,
CC ECO:0000269|PubMed:29887375}.
CC -!- TISSUE SPECIFICITY: During embryogenesis, specifically expressed in
CC immature olfactory sensory neurons. {ECO:0000269|PubMed:28067911}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the nasal placodes and optic vesicles
CC at day 9.5 dpc and in the nasal epithelium at 12.5 dpc
CC (PubMed:28067911). Expressed in the nasal cavity in 14.5 dpc animals
CC (PubMed:28067911). {ECO:0000269|PubMed:28067911}.
CC -!- INDUCTION: Expression is repressed by CDX2.
CC {ECO:0000269|PubMed:29900695}.
CC -!- DOMAIN: Atypical member of the structural maintenance of chromosomes
CC (SMC) protein family (PubMed:26733688, PubMed:27059856). Like other
CC members of the SMC family, has ATPase activity, which is probably
CC necessary for its engagement with chromatin, and a SMC hinge domain
CC (PubMed:26733688, PubMed:27059856). However, the SMC hinge domain
CC adopts an unconventional homodimeric arrangement augmented by an
CC intermolecular coiled coil formed between the two monomers. This
CC suggests that protein may assemble as a head-to-head parallel dimer
CC without adopting a hairpin shape at the hinge domain, unlike the
CC dimeric arrangement conventionally found in other members of the SMC
CC protein family (PubMed:26733688). The SMC hinge domain binds DNA and
CC RNA (PubMed:26091879). {ECO:0000269|PubMed:26091879,
CC ECO:0000269|PubMed:26733688, ECO:0000269|PubMed:27059856}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}.
CC -!- DISRUPTION PHENOTYPE: Defects in Smchd1 are the cause of the MommeD1
CC (modifier of murine metastable epialleles) phenotype, a semi-dominant
CC suppressor of variegation (PubMed:18425126, PubMed:21553025). Mice
CC display female-specific mid-gestation lethality and hypomethylation of
CC the X-linked gene Hprt1, due to defects in X inactivation
CC (PubMed:18425126, PubMed:21553025, PubMed:23754746). Mice do not show
CC defects on telomeres length (PubMed:18425126, PubMed:21553025). Male
CC mice are less affected, with some surviving to become fertile adults on
CC the FVB/n genetic background (PubMed:18425126). On other genetic
CC backgrounds, all males lacking die perinatally (PubMed:18425126). A
CC subset of clustered autosomal loci display hypomethylation and
CC derepression (PubMed:23754746, PubMed:23819640, PubMed:28587678).
CC {ECO:0000269|PubMed:18425126, ECO:0000269|PubMed:21553025,
CC ECO:0000269|PubMed:23754746, ECO:0000269|PubMed:23819640,
CC ECO:0000269|PubMed:28587678}.
CC -!- SIMILARITY: Belongs to the SMC family. Highly divergent. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44905.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB30222.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC107664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK016419; BAB30222.1; ALT_FRAME; mRNA.
DR EMBL; AK078494; BAC37307.1; -; mRNA.
DR EMBL; BC044905; AAH44905.1; ALT_INIT; mRNA.
DR EMBL; BC058205; AAH58205.1; -; mRNA.
DR EMBL; BC058618; AAH58618.1; -; mRNA.
DR EMBL; BC062946; AAH62946.1; -; mRNA.
DR EMBL; AK129181; BAC97991.1; -; mRNA.
DR CCDS; CCDS28958.2; -.
DR RefSeq; NP_083163.3; NM_028887.3.
DR PDB; 6N64; X-ray; 3.30 A; A/B/C/D/E/F=1683-1899.
DR PDBsum; 6N64; -.
DR AlphaFoldDB; Q6P5D8; -.
DR SMR; Q6P5D8; -.
DR BioGRID; 216686; 24.
DR IntAct; Q6P5D8; 20.
DR MINT; Q6P5D8; -.
DR STRING; 10090.ENSMUSP00000121835; -.
DR iPTMnet; Q6P5D8; -.
DR PhosphoSitePlus; Q6P5D8; -.
DR EPD; Q6P5D8; -.
DR jPOST; Q6P5D8; -.
DR MaxQB; Q6P5D8; -.
DR PaxDb; Q6P5D8; -.
DR PeptideAtlas; Q6P5D8; -.
DR PRIDE; Q6P5D8; -.
DR ProteomicsDB; 261270; -.
DR Antibodypedia; 49899; 84 antibodies from 20 providers.
DR Ensembl; ENSMUST00000127430; ENSMUSP00000121835; ENSMUSG00000024054.
DR GeneID; 74355; -.
DR KEGG; mmu:74355; -.
DR UCSC; uc008dmh.2; mouse.
DR CTD; 23347; -.
DR MGI; MGI:1921605; Smchd1.
DR VEuPathDB; HostDB:ENSMUSG00000024054; -.
DR eggNOG; ENOG502QREW; Eukaryota.
DR GeneTree; ENSGT00390000006950; -.
DR HOGENOM; CLU_002288_1_0_1; -.
DR InParanoid; Q6P5D8; -.
DR OMA; SIIMYKS; -.
DR OrthoDB; 34310at2759; -.
DR PhylomeDB; Q6P5D8; -.
DR TreeFam; TF329426; -.
DR BioGRID-ORCS; 74355; 2 hits in 59 CRISPR screens.
DR ChiTaRS; Smchd1; mouse.
DR PRO; PR:Q6P5D8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6P5D8; protein.
DR Bgee; ENSMUSG00000024054; Expressed in manus and 232 other tissues.
DR ExpressionAtlas; Q6P5D8; baseline and differential.
DR Genevisible; Q6P5D8; MM.
DR GO; GO:0001740; C:Barr body; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IMP:MGI.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0060820; P:inactivation of X chromosome by heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0043584; P:nose development; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR InterPro; IPR038892; SMCHD1.
DR PANTHER; PTHR22640; PTHR22640; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromatin regulator; Chromosome; DNA damage;
KW DNA repair; DNA-binding; Hydrolase; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repressor; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A6NHR9"
FT CHAIN 2..2007
FT /note="Structural maintenance of chromosomes flexible hinge
FT domain-containing protein 1"
FT /id="PRO_0000332145"
FT DOMAIN 1721..1848
FT /note="SMC hinge"
FT /evidence="ECO:0000255"
FT REGION 111..702
FT /note="ATPase activity domain"
FT /evidence="ECO:0000269|PubMed:27059856"
FT REGION 1984..2007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:A6NHR9"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A6NHR9"
FT MOD_RES 1500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A6NHR9"
FT MOD_RES 1803
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NHR9"
FT CROSSLNK 1375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:A6NHR9"
FT MUTAGEN 147
FT /note="E->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:26391951"
FT MUTAGEN 1867
FT /note="R->G: Abolishes ability to bind DNA without altering
FT the ability of the SMC hinge domain to mediate
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:26091879,
FT ECO:0000269|PubMed:26733688"
FT MUTAGEN 1872..1876
FT /note="GKFGG->AKFAA: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:26391951"
FT CONFLICT 1120
FT /note="K -> E (in Ref. 1; BAB30222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1611
FT /note="P -> S (in Ref. 4; BAC97991)"
FT /evidence="ECO:0000305"
FT HELIX 1720..1728
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1736..1749
FT /evidence="ECO:0007829|PDB:6N64"
FT STRAND 1752..1757
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1758..1767
FT /evidence="ECO:0007829|PDB:6N64"
FT TURN 1768..1770
FT /evidence="ECO:0007829|PDB:6N64"
FT STRAND 1774..1776
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1777..1779
FT /evidence="ECO:0007829|PDB:6N64"
FT STRAND 1797..1800
FT /evidence="ECO:0007829|PDB:6N64"
FT STRAND 1809..1811
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1812..1814
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1819..1821
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1824..1832
FT /evidence="ECO:0007829|PDB:6N64"
FT STRAND 1836..1840
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1841..1851
FT /evidence="ECO:0007829|PDB:6N64"
FT TURN 1852..1854
FT /evidence="ECO:0007829|PDB:6N64"
FT STRAND 1860..1862
FT /evidence="ECO:0007829|PDB:6N64"
FT STRAND 1865..1868
FT /evidence="ECO:0007829|PDB:6N64"
FT HELIX 1877..1879
FT /evidence="ECO:0007829|PDB:6N64"
SQ SEQUENCE 2007 AA; 225648 MW; 1A41FC47C54B5415 CRC64;
MAAEGASDPA GLSEGSGRDG AVDGCRTVYL FDRRGKDSEL GDRALQVSEH ADYAGFRASV
CQTIGISSEE KFVITTTSRK EITCNNFDHT VKDGVTLYLL QSVDQSLLTA TKERIDFLPH
YDTLVKSGMY EYYASEGQNP LPFALAELID NSLSATSRNN GVRRIQIKLL FDETQGKPAV
AVVDNGRGMT SKQLNNWAVY RLSKFTRQGD FESDHSGYVR PLPVPRSLNS DISYFGVGGK
QAVFFVGQSA RMISKPIDSK DVHELVLSKE DFEKKEKNKE AIYSGYIRNR KPADSAHITN
DDERFLHNLI EEEKEKDSFT AVVITGVQPE HIQYLKNYLH LWTRQLTHIY HYYIHGPKGN
EISTAKAIGP FNNIDIEISL FEKGKTPKII NLREIQDDMQ TLYINTASDS FEFKAHVEGD
GVVEGVIRYH PFLYDRETFP DDPCFPSKLK DEDDDDDCFI SEKAARGKRP IFECFWNGRL
IPYTSVGDFD WCAPPKKRGL VPIECFNRIS GALFTNDKFQ VSTNKLTFMD LELKLKDKNT
LFTRILNGQE QRMKIDREFA LWLKDCHEKH DKQIKFTLFK GIITRPDLPT KKQGPWATFS
AIEWDGKIYK AGQLVKTIKT LPLCYGSIVR FFLHGDHDGE VYATGGEVQI AMEPQALYDE
IKTVPIAKLD RTVAEKTIRK YVEDEMARLP DRLSVTWPEG DELLPNEVRP AGTPIGALRI
EILNKKGEAM QKLPGTSHGG SKKLLVELKV ILHTSSGNKE IISHISQHGG KWPYWFKKME
NIQKLGNYTL KLQVVLNESN ADTYAGRSLP SKVIKFSVKE GKPEKFSFGL LDSPFRVGVP
FNIPLELQDE FGHTTQLLSD IEPVLEASGL SLHYEGITKG PNCVIQGVVA KGPVNSCQGK
NFNLKVILPG LKEDSQILKI RLLPGPPHQL KVKPDSEVLV IENGTAFPFQ VEVVDESDNI
TAQPKLIVHC KFLGAPNLPV YTVDCSSSGT SILTGSPIQV QNIKKDQKTL TARIEIPSCK
DVSPVEKTIK LLPSSHAACL QIFSVEEQKA IQIKHQDEVT WVAGDVIRNL IFQMYDEGER
EINITPSLAE KIKVNWTPEV NKEHLVQGLL PDVQVPTSVK DVRYCHVSFQ DDHVCLESAF
TVRPLPDDPK HLKCELKGGK TVQMGQELQG EIVVIIADQY GNQISSFSPD SLSTLSITGD
GLDSSNLKIT LEANSQSVSV QGIRFTPGPP GPKDLCFTWR EFSDFLRVQL VSGPPTKLLL
MDWPELKESI PVINGRQLEN PLIVQLCDQW DNPALVPNVK ICLIKASSLR LLPSNQQHKT
DDKGRANLGV FTVCAPRGEH TVQVKGVYNK STIEGPTIKL TILPDPEKPI RLNVKYDQDA
SFIAGDIFTD FMVSVISESG SVIKNINPTR ISMKMWKLSS GMSRPPANAE TFSCNKIKGN
DKEDGCFYFR EKTIPNKVGA YCIQFDFMID KTNILSSQQV IVDVLPNQPM KLVPDSQPAT
PAVSNVRSIA SRTLVKDLRL SITDNYGNHT GMDLVGTVVA TIKGFNEEDT DTPLFIGKVR
TLEFPFVKGS AEITTLVLAE NSPGRDSTEY FIIFEPRLST VSGTLESYSL PFMFYNDVKK
QQQMAALTKE KDELSKSITM YRSLFDANKQ LVDEMKCQAE EAKLKETQLR NELKAYNIDI
PATQQTTHIE ALLEKKITEQ NELKKRPRRL CTLPNYTKRS GDILGKIAHL AQIEDDRAAM
VISWHLASDM DCVVTLTTDA ARAIYDETQG RQQVLPLDSI YRKTLPDWKR PLPHFRNGKL
HFKPFGNPVF ARDLLTFPDN IEHCETVFGM LLGDTIILDN LDAANHYRKE VVKITHCPTL
LTRDGDRIRS NGKFGGLQNK APPMDKLRGM VFGAPVPKQC VVLGKQIDLI QQYRTALYRL
SSVNEDLDNQ LQYLHTPDMK KKKQELDEQE KSLKRIEQKL GMTPVRRCNE SLCHSPKIEV
TECPIPTKRM RRESTRQNRR PKGDVPN
