SMRCD_RAT
ID SMRCD_RAT Reviewed; 1024 AA.
AC D3Z9Z9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1;
DE EC=3.6.4.12;
GN Name=Smarcad1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127 AND SER-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC nucleosome-remodeling activity and is both required for DNA repair and
CC heterochromatin organization. Promotes DNA end resection of double-
CC strand breaks (DSBs) following DNA damage: probably acts by weakening
CC histone DNA interactions in nucleosomes flanking DSBs. Required for the
CC restoration of heterochromatin organization after replication. Acts at
CC replication sites to facilitate the maintenance of heterochromatin by
CC directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation
CC (H3K9me3) and restoration of silencing (By similarity). {ECO:0000250}.
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; EC=3.6.4.12;
CC -!- SUBUNIT: Binds to DNA preferentially in the vicinity of transcriptional
CC start sites. Interacts with MSH2 and TRIM28. Part of a complex composed
CC of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PCNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Colocalizes with PCNA at replication forks during S phase.
CC Recruited to double-strand breaks (DSBs) sites of DNA damage (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AABR03032021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101334.2; NM_001107864.2.
DR RefSeq; XP_006236661.1; XM_006236599.2.
DR RefSeq; XP_006236662.1; XM_006236600.3.
DR AlphaFoldDB; D3Z9Z9; -.
DR SMR; D3Z9Z9; -.
DR STRING; 10116.ENSRNOP00000008585; -.
DR iPTMnet; D3Z9Z9; -.
DR PhosphoSitePlus; D3Z9Z9; -.
DR PaxDb; D3Z9Z9; -.
DR PeptideAtlas; D3Z9Z9; -.
DR PRIDE; D3Z9Z9; -.
DR Ensembl; ENSRNOT00000008585; ENSRNOP00000008585; ENSRNOG00000006391.
DR GeneID; 312398; -.
DR KEGG; rno:312398; -.
DR UCSC; RGD:1309640; rat.
DR CTD; 56916; -.
DR RGD; 1309640; Smarcad1.
DR eggNOG; KOG0389; Eukaryota.
DR GeneTree; ENSGT00910000144252; -.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; D3Z9Z9; -.
DR OMA; HNKYEDY; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; D3Z9Z9; -.
DR TreeFam; TF105768; -.
DR PRO; PR:D3Z9Z9; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000006391; Expressed in thymus and 20 other tissues.
DR Genevisible; D3Z9Z9; RN.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0043596; C:nuclear replication fork; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0051304; P:chromosome separation; ISS:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR GO; GO:0000018; P:regulation of DNA recombination; ISO:RGD.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51140; CUE; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chromatin regulator; Chromosome; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1024
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A containing DEAD/H box 1"
FT /id="PRO_0000416934"
FT DOMAIN 156..198
FT /note="CUE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 250..293
FT /note="CUE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 507..675
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 856..1008
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 626..629
FT /note="DEGH box"
FT /evidence="ECO:0000250"
FT MOTIF 719..736
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1003..1006
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 44..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519..527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 895..902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 722
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 994
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
SQ SEQUENCE 1024 AA; 116788 MW; 0378D83371B66539 CRC64;
MNLFNLDRFR FEKRSKIEEA PEAAPQPSQP GPSSPISLSA EEENAEGEVS RANTPDSDVT
EKTEDSSVPE PPDNESKASL SCFQNQRTIQ EYIDLSSDSE DVSPNCSSTV QEKKFSKDTV
IIVSEPSEDE ESHDLPSATR RNDISELEDL SELEDLKDAK LQTLKELFPQ RSDSDLLKLI
DSTSTMDGAI AAALLKFGDA GGGPRKRKLS SSSEAYEEDE ANDDQSLKKP RGDRREESNE
SAEASSNWEK QESIVLKLQK EFPNFDKQEL REVLKEHEWM YTEALESLKV FAEDQDVQCA
SQSEVTNGKE VARNQNYSKN AAKIKMKQKI SMKPQNGFNK KRKKNVFNPK KAVEDSEYDS
GSDAGSSLDE DYSSCEEVME DGYKGKILHF LQDASIGELT LIPKCSQKKA QKIIELRPFN
NWETLFTKMS KINGLSEDLI WNCKTVIQER DVVIRLMNKC EDISNKLTKQ VTMLTGNGGG
WNIEQPSLLN QSLSLKPYQK VGLNWLALVH KHGLNGILAD EMGLGKTIQA IAFLAYLFQE
GNKGPHLIVV PASTIDNWLR EVNLWCPTLN VLCYYGSQEE RKQIRFNIHN KYEDYNVIVT
TYNCAISSSD DRSLFRRLKL NYAIFDEGHM LKNMGSIRYQ HLMTINARNR LLLTGTPVQN
NLLELMSLLN FVMPHMFSSS TSEIRRMFSS KTKPADEQSI YEKERIAHAK QIIKPFILRR
VKEEVLKLLP PKKDQIELCA MSEKQEQLYS GLFNRLKKSI NNLEKNTEMC NVMMQLRKMA
NHPLLHRQYY TAEKLKEMSQ LMLKEPTHCE ANPDLIFEDM EVMTDFELHV LCKQYQHINS
YQLDMDLILD SGKFRTLGCI LSELKQKGDR VVLFSQFTMM LDILEVLLKH HQHRYLRLDG
KTQISERIHL IDEFNTDMDI FVFLLSTKAG GLGINLTSAN VVILHDIDCN PYNDKQAEDR
CHRVGQTKEV LVIKLISQGT IEESMLKINQ QKLKLEQDMT TVDEADEGSM PADIATLLKT
SMGL
