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Database: UniProt
Entry: Q9W3U1
LinkDB: Q9W3U1
Original site: Q9W3U1 
ID   SETD3_DROME             Reviewed;         537 AA.
AC   Q9W3U1;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   13-FEB-2019, entry version 148.
DE   RecName: Full=Actin-histidine N-methyltransferase {ECO:0000305};
DE            EC=2.1.1.85 {ECO:0000250|UniProtKB:Q86TU7};
DE   AltName: Full=SET domain-containing protein 3 homolog {ECO:0000305};
DE            Short=dSETD3 {ECO:0000303|PubMed:30067821};
GN   ORFNames=CG32732 {ECO:0000312|FlyBase:FBgn0052732};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=30067821; DOI=10.1371/journal.pone.0201609;
RA   Tiebe M., Lutz M., Levy D., Teleman A.A.;
RT   "Phenotypic characterization of SETD3 knockout Drosophila.";
RL   PLoS ONE 13:E0201609-E0201609(2018).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=30526847; DOI=10.7554/eLife.37921;
RA   Kwiatkowski S., Seliga A.K., Vertommen D., Terreri M., Ishikawa T.,
RA   Grabowska I., Tiebe M., Teleman A.A., Jagielski A.K.,
RA   Veiga-da-Cunha M., Drozak J.;
RT   "SETD3 protein is the actin-specific histidine N-methyltransferase.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC       mediates methylation of actin at 'His-74'.
CC       {ECO:0000269|PubMed:30526847}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC         Evidence={ECO:0000250|UniProtKB:Q86TU7};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30526847}.
CC       Nucleus {ECO:0000269|PubMed:30526847}. Note=Localizes mainly in
CC       the cytoplasm. {ECO:0000269|PubMed:30526847}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:30067821).
CC       Cells show complete loss of actin histidine methylation
CC       (PubMed:30526847). {ECO:0000269|PubMed:30067821,
CC       ECO:0000269|PubMed:30526847}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SETD3 subfamily. {ECO:0000305}.
DR   EMBL; AE014298; AAF46222.2; -; Genomic_DNA.
DR   EMBL; BT003482; AAO39485.1; -; mRNA.
DR   RefSeq; NP_727144.1; NM_167100.3.
DR   UniGene; Dm.7994; -.
DR   SMR; Q9W3U1; -.
DR   IntAct; Q9W3U1; 1.
DR   STRING; 7227.FBpp0070998; -.
DR   EnsemblMetazoa; FBtr0071039; FBpp0070998; FBgn0052732.
DR   GeneID; 31638; -.
DR   KEGG; dme:Dmel_CG32732; -.
DR   UCSC; CG32732-RA; d. melanogaster.
DR   FlyBase; FBgn0052732; CG32732.
DR   eggNOG; KOG1337; Eukaryota.
DR   eggNOG; ENOG410Y7DR; LUCA.
DR   GeneTree; ENSGT00940000153577; -.
DR   KO; K19199; -.
DR   OMA; CERADPN; -.
DR   OrthoDB; EOG091G087D; -.
DR   GenomeRNAi; 31638; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0052732; Expressed in 29 organ(s), highest expression level in cleaving embryo.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.90.1420.10; -; 1.
DR   InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR   InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; SSF81822; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Complete proteome; Cytoplasm; Methyltransferase;
KW   Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    537       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000446384.
FT   DOMAIN      133    364       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      143    145       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   REGION      325    329       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   REGION      375    377       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   BINDING     114    114       S-adenosyl-L-methionine.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   BINDING     299    299       S-adenosyl-L-methionine.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
SQ   SEQUENCE   537 AA;  61158 MW;  F12FBFAAEAF8304B CRC64;
     MGKNTKRNKK TKQQQQQPQQ NGVTASASGT AVEDFEDQQA ASSLPSLNGK KRSQLNKLVE
     ELLDLVEKQP ANPNEEWKQY GQLQELLKQI MILEEPLSQA VCPQISDSPD DQTRLAKVEA
     FSAWAKDGGV HSEGLEIAIF PGYQLGLRAT RPLAKDELVL SVPRKLILSE ENNSDCRLFG
     KMTQATHLNL AYDLVIEKIR GEFSEWRPYI DVLPAKYNTV LYFTTKQMEL LRGTAAAALA
     MRQCRVIAKQ YAFLYKYAHT MTEPSTGNRS HPGERGLFFT QHGLCYKLYR WAVSTVMTRQ
     NLVPSEKQES EDGPKLISAL IPYWDMANHR PGKITSFYAT VSRQLECTAQ EAVNTGEQFF
     IYYGDRSNTD LLVHNGFVDP NNTKDYVNIR VGLSLTDALA AKRASILDKL NIRHTAELRV
     LPAPDFISKE LLAFVRVFKM SAEQLDHWCS DLDRAGDLLH IDCALETDHE TRTWQFLEDR
     LKLLLAVFNK EMHEADEVKE LELKDGQEIE LMLFLYRRLE RSILAGALQY AQEHRKV
//
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