ID   SETD7_MOUSE             Reviewed;         366 AA.
AC   Q8VHL1; Q6ZPJ6; Q80UU3; Q8C7Y6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE            EC=2.1.1.364 {ECO:0000250|UniProtKB:Q8WTS6};
DE   AltName: Full=Histone H3-K4 methyltransferase SETD7;
DE            Short=H3-K4-HMTase SETD7;
DE   AltName: Full=SET domain-containing protein 7;
DE   AltName: Full=SET7/9;
GN   Name=Setd7; Synonyms=Kiaa1717, Set7, Set9;
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].
RC   TISSUE=Pancreas;
RX   PubMed=11779497; DOI=10.1016/s1097-2765(01)00405-1;
RA   Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P.,
RA   Zhang Y.;
RT   "Purification and functional characterization of a histone H3-lysine 4-
RT   specific methyltransferase.";
RL   Mol. Cell 8:1207-1217(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain, and Cerebellum;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
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   [5]
RP   FUNCTION.
RX   PubMed=12711597; DOI=10.1074/jbc.m303423200;
RA   Chakrabarti S.K., Francis J., Ziesmann S.M., Garmey J.C., Mirmira R.G.;
RT   "Covalent histone modifications underlie the developmental regulation of
RT   insulin gene transcription in pancreatic beta cells.";
RL   J. Biol. Chem. 278:23617-23623(2003).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15975555; DOI=10.1016/j.bbrc.2005.06.003;
RA   Jeong K.S., Park J.H., Lee S.;
RT   "The analysis of X-chromosome inactivation-related gene expression from
RT   single mouse embryo with sex-determination.";
RL   Biochem. Biophys. Res. Commun. 333:803-807(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, and Spleen;
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-297.
RX   PubMed=35210392; DOI=10.1038/s41413-022-00194-0;
RA   Xiao Y., Li J., Liao X., He Y., He T., Yang C., Jiang L., Jeon S.M.,
RA   Lee J.H., Chen Y., Liu R., Chen Q.;
RT   "RIOX1-demethylated cGAS regulates ionizing radiation-elicited DNA
RT   repair.";
RL   Bone Res. 10:19-19(2022).
CC   -!- FUNCTION: Histone methyltransferase that specifically monomethylates
CC       'Lys-4' of histone H3 (By similarity). H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional activation (By
CC       similarity). Plays a central role in the transcriptional activation of
CC       genes such as collagenase or insulin (PubMed:12711597). Recruited by
CC       IPF1/PDX-1 to the insulin promoter, leading to activate transcription
CC       (By similarity). Has also methyltransferase activity toward non-histone
CC       proteins such as CGAS, p53/TP53, TAF10, and possibly TAF7 by
CC       recognizing and binding the [KR]-[STA]-K in substrate proteins
CC       (PubMed:35210392). Monomethylates 'Lys-189' of TAF10, leading to
CC       increase the affinity of TAF10 for RNA polymerase II (By similarity).
CC       Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and
CC       increasing p53/TP53-mediated transcriptional activation (By
CC       similarity). Monomethylates 'Lys-491' of CGAS, promoting interaction
CC       between SGF29 and CGAS (PubMed:35210392).
CC       {ECO:0000250|UniProtKB:Q8WTS6, ECO:0000269|PubMed:12711597,
CC       ECO:0000269|PubMed:35210392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC         Evidence={ECO:0000250|UniProtKB:Q8WTS6, ECO:0000255|PROSITE-
CC         ProRule:PRU00910};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC         methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC         Evidence={ECO:0000269|PubMed:35210392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC         Evidence={ECO:0000269|PubMed:35210392};
CC   -!- SUBUNIT: Interacts with IPF1/PDX-1. {ECO:0000250|UniProtKB:Q8WTS6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WTS6}.
CC       Chromosome {ECO:0000250|UniProtKB:Q8WTS6}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during all pre-implementation stages in
CC       both male and female embryos. {ECO:0000269|PubMed:15975555}.
CC   -!- DOMAIN: The SET domain is necessary but not sufficient for histone
CC       methyltransferase activity. {ECO:0000250|UniProtKB:Q8WTS6}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. SET7 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00910}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF448509; AAL56578.1; -; mRNA.
DR   EMBL; AK129428; BAC98238.1; ALT_INIT; mRNA.
DR   EMBL; AK048924; BAC33493.1; -; mRNA.
DR   EMBL; AK147422; BAE27903.1; -; mRNA.
DR   EMBL; AK147413; BAE27897.1; -; mRNA.
DR   EMBL; AK147667; BAE28059.1; -; mRNA.
DR   EMBL; AK170161; BAE41607.1; -; mRNA.
DR   EMBL; BC050190; AAH50190.1; -; mRNA.
DR   CCDS; CCDS17341.1; -.
DR   RefSeq; NP_542983.3; NM_080793.5.
DR   AlphaFoldDB; Q8VHL1; -.
DR   SMR; Q8VHL1; -.
DR   BioGRID; 215865; 6.
DR   IntAct; Q8VHL1; 1.
DR   STRING; 10090.ENSMUSP00000043492; -.
DR   iPTMnet; Q8VHL1; -.
DR   PhosphoSitePlus; Q8VHL1; -.
DR   SwissPalm; Q8VHL1; -.
DR   EPD; Q8VHL1; -.
DR   MaxQB; Q8VHL1; -.
DR   PaxDb; 10090-ENSMUSP00000043492; -.
DR   PeptideAtlas; Q8VHL1; -.
DR   ProteomicsDB; 261171; -.
DR   Pumba; Q8VHL1; -.
DR   Antibodypedia; 16193; 604 antibodies from 40 providers.
DR   DNASU; 73251; -.
DR   Ensembl; ENSMUST00000037141.9; ENSMUSP00000043492.8; ENSMUSG00000037111.10.
DR   GeneID; 73251; -.
DR   KEGG; mmu:73251; -.
DR   UCSC; uc008peb.1; mouse.
DR   AGR; MGI:1920501; -.
DR   CTD; 80854; -.
DR   MGI; MGI:1920501; Setd7.
DR   VEuPathDB; HostDB:ENSMUSG00000037111; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   GeneTree; ENSGT00390000004827; -.
DR   HOGENOM; CLU_803117_0_0_1; -.
DR   InParanoid; Q8VHL1; -.
DR   OMA; RITHTEV; -.
DR   OrthoDB; 5304435at2759; -.
DR   PhylomeDB; Q8VHL1; -.
DR   TreeFam; TF106392; -.
DR   BRENDA; 2.1.1.364; 3474.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   BioGRID-ORCS; 73251; 3 hits in 83 CRISPR screens.
DR   ChiTaRS; Setd7; mouse.
DR   PRO; PR:Q8VHL1; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8VHL1; Protein.
DR   Bgee; ENSMUSG00000037111; Expressed in triceps brachii and 217 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR   GO; GO:0140938; F:histone H3 methyltransferase activity; ISO:MGI.
DR   GO; GO:0140945; F:histone H3K4 monomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IDA:MGI.
DR   GO; GO:0006974; P:DNA damage response; ISO:MGI.
DR   GO; GO:0070828; P:heterochromatin organization; IMP:MGI.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   CDD; cd10530; SET_SETD7; 1.
DR   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR017155; Hist-Lys_N-MeTrfase_SETD7.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044436; SETD7_SET.
DR   PANTHER; PTHR46820; HISTONE-LYSINE N-METHYLTRANSFERASE SETD7; 1.
DR   PANTHER; PTHR46820:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD7; 1.
DR   Pfam; PF02493; MORN; 4.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR   SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51577; SAM_MT43_SET7; 1.
DR   PROSITE; PS50280; SET; 1.
DR   Genevisible; Q8VHL1; MM.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..366
FT                   /note="Histone-lysine N-methyltransferase SETD7"
FT                   /id="PRO_0000186055"
FT   REPEAT          36..58
FT                   /note="MORN 1"
FT   REPEAT          59..81
FT                   /note="MORN 2"
FT   REPEAT          106..128
FT                   /note="MORN 3"
FT   DOMAIN          214..336
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         226..228
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   BINDING         297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   BINDING         356
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6,
FT                   ECO:0000255|PROSITE-ProRule:PRU00190"
FT   SITE            245
FT                   /note="Histone H3K4 binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   SITE            256
FT                   /note="Histone H3K4 binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   SITE            266
FT                   /note="Histone H3K4 binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   SITE            317
FT                   /note="Histone H3K4 binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   SITE            335
FT                   /note="Histone H3K4 binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS6"
FT   MUTAGEN         297
FT                   /note="H->A: Abolishes methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:35210392"
FT   CONFLICT        77
FT                   /note="E -> V (in Ref. 4; AAH50190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="L -> I (in Ref. 1; AAL56578)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  40506 MW;  C826EAFCB4B9D345 CRC64;
     MDSDDEVVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE
     GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDS DGRLIFKGQY KDNNRHGVCW
     IHYPDGGSLV GEVNEDGEMT GEKIAYVYPD QRTALYGKFI DGEMLEGKLA TLMATEEGRP
     HFEVTSGSSV YHFDKSTSSC ISSDALLPDP YESERVYVAD SLISSAGEGL FSKVAVGPNT
     VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
     PNCVYDLFVH PRFGPIKCIR TLRAVEAEEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF
     QATQQK
//