SETD3_HUMAN
ID SETD3_HUMAN Reviewed; 594 AA.
AC Q86TU7; A0PJU3; A5PLP0; B4DZE8; Q0VAQ2; Q659C0; Q86TU8; Q96GY9; Q9H5U5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Actin-histidine N-methyltransferase {ECO:0000305};
DE EC=2.1.1.85 {ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:31993215};
DE AltName: Full=Protein-L-histidine N-tele-methyltransferase {ECO:0000305};
DE AltName: Full=SET domain-containing protein 3 {ECO:0000305};
DE Short=hSETD3 {ECO:0000303|PubMed:28442573};
GN Name=SETD3 {ECO:0000303|PubMed:30526847, ECO:0000303|PubMed:30626964,
GN ECO:0000312|HGNC:HGNC:20493};
GN Synonyms=C14orf154 {ECO:0000312|HGNC:HGNC:20493};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Eye;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 215-594 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, UBIQUITINATION, PHOSPHORYLATION,
RP AND MUTAGENESIS OF 37-SER--GLY-42; 181-SER--THR-185; 260-THR--SER-264;
RP 373-THR--SER-378; 512-SER--SER-517 AND 565-SER--SER-569.
RX PubMed=28442573; DOI=10.1074/jbc.m117.778001;
RA Cheng X., Hao Y., Shu W., Zhao M., Zhao C., Wu Y., Peng X., Yao P.,
RA Xiao D., Qing G., Pan Z., Yin L., Hu D., Du H.N.;
RT "Cell cycle-dependent degradation of the methyltransferase SETD3 attenuates
RT cell proliferation and liver tumorigenesis.";
RL J. Biol. Chem. 292:9022-9033(2017).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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., Veiga-da-Cunha M.,
RA Drozak J.;
RT "SETD3 protein is the actin-specific histidine N-methyltransferase.";
RL Elife 7:0-0(2018).
RN [12] {ECO:0007744|PDB:3SMT}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 2-498 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RA Zeng H., Dong A., Walker J.R., Loppnau P., Bountra C., Weigelt J.,
RA Arrowsmith C.H., Edwards A.M., Min J., Wu H.;
RT "Crystal structure of human SET domain-containing protein 3.";
RL Submitted (JUN-2011) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-503 IN COMPLEX WITH ACTIN AND
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ARG-215; ASN-256; TYR-313 AND ARG-316.
RX PubMed=30785395; DOI=10.7554/elife.43676;
RA Guo Q., Liao S., Kwiatkowski S., Tomaka W., Yu H., Wu G., Tu X., Min J.,
RA Drozak J., Xu C.;
RT "Structural insights into SETD3-mediated histidine methylation on beta-
RT actin.";
RL Elife 8:0-0(2019).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 21-503 IN COMPLEX WITH ACTIN AND
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, DOMAIN, AND MUTAGENESIS OF TYR-313.
RX PubMed=30626964; DOI=10.1038/s41586-018-0821-8;
RA Wilkinson A.W., Diep J., Dai S., Liu S., Ooi Y.S., Song D., Li T.M.,
RA Horton J.R., Zhang X., Liu C., Trivedi D.V., Ruppel K.M.,
RA Vilches-Moure J.G., Casey K.M., Mak J., Cowan T., Elias J.E.,
RA Nagamine C.M., Spudich J.A., Cheng X., Carette J.E., Gozani O.;
RT "SETD3 is an actin histidine methyltransferase that prevents primary
RT dystocia.";
RL Nature 565:372-376(2019).
RN [15] {ECO:0007744|PDB:6OX0, ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2, ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4, ECO:0007744|PDB:6OX5}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ACTIN AND
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP ASN-256.
RX PubMed=31388018; DOI=10.1038/s41467-019-11554-6;
RA Dai S., Horton J.R., Woodcock C.B., Wilkinson A.W., Zhang X., Gozani O.,
RA Cheng X.;
RT "Structural basis for the target specificity of actin histidine
RT methyltransferase SETD3.";
RL Nat. Commun. 10:3541-3541(2019).
RN [16] {ECO:0007744|PDB:6JAT}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 1-498 IN COMPLEX WITH ACTIN AND
RP S-ADENOSYL-L-METHIONINE ANALOG, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31993215; DOI=10.1038/s41421-019-0135-5;
RA Zheng Y., Zhang X., Li H.;
RT "Molecular basis for histidine N3-specific methylation of actin H73 by
RT SETD3.";
RL Cell Discov. 6:3-3(2020).
RN [17] {ECO:0007744|PDB:6V62, ECO:0007744|PDB:6V63}
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) IN COMPLEX WITH ACTIN MUTANT AND
RP S-ADENOSYL-L-METHIONINE, AND MUTAGENESIS OF ASN-256 AND TRP-274.
RX PubMed=31911441; DOI=10.1074/jbc.ra119.012319;
RA Dai S., Horton J.R., Wilkinson A.W., Gozani O., Zhang X., Cheng X.;
RT "An engineered variant of SETD3 methyltransferase alters target specificity
RT from histidine to lysine methylation.";
RL J. Biol. Chem. 295:2582-2589(2020).
RN [18] {ECO:0007744|PDB:6WK1, ECO:0007744|PDB:6WK2}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH ACTIN MUTANT AND
RP S-ADENOSYL-L-METHIONINE, AND MUTAGENESIS OF ASN-256.
RX PubMed=32503840; DOI=10.1074/jbc.ra120.014072;
RA Dai S., Holt M.V., Horton J.R., Woodcock C.B., Patel A., Zhang X.,
RA Young N.L., Wilkinson A.W., Cheng X.;
RT "Characterization of SETD3 methyltransferase-mediated protein methionine
RT methylation.";
RL J. Biol. Chem. 295:10901-10910(2020).
CC -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC mediates 3-methylhistidine (tele-methylhistidine) methylation of actin
CC at 'His-73' (PubMed:30526847, PubMed:30626964, PubMed:30785395,
CC PubMed:31388018, PubMed:31993215). Histidine methylation of actin is
CC required for smooth muscle contraction of the laboring uterus during
CC delivery (PubMed:30626964). Does not have protein-lysine N-
CC methyltransferase activity and probably only catalyzes histidine
CC methylation of actin (PubMed:30626964, PubMed:30785395,
CC PubMed:31388018). {ECO:0000269|PubMed:30526847,
CC ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395,
CC ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:31993215}.
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:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964,
CC ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018,
CC ECO:0000269|PubMed:31993215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370;
CC Evidence={ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964,
CC ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018,
CC ECO:0000269|PubMed:31993215};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.752 uM for beta-actin {ECO:0000269|PubMed:30526847};
CC KM=0.502 uM for beta-actin {ECO:0000269|PubMed:30785395};
CC KM=0.116 uM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:30526847};
CC KM=0.111 uM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:30785395};
CC Vmax=9.091 nmol/min/mg enzyme with beta-actin as substrate
CC {ECO:0000269|PubMed:30526847};
CC Vmax=13.550 nmol/min/mg enzyme with beta-actin as substrate
CC {ECO:0000269|PubMed:30785395};
CC Vmax=8.649 nmol/min/mg enzyme with S-adenosyl-L-methionine as
CC substrate {ECO:0000269|PubMed:30526847};
CC Vmax=11.260 nmol/min/mg enzyme with S-adenosyl-L-methionine as
CC substrate {ECO:0000269|PubMed:30785395};
CC Note=kcat is 0.65 min(-1) with beta-actin as substrate
CC (PubMed:30526847). kcat is 0.809 min(-1) with beta-actin as substrate
CC (PubMed:30785395). kcat is 0.61 min(-1) with S-adenosyl-L-methionine
CC as substrate (PubMed:30526847). kcat is 0.673 min(-1) with S-
CC adenosyl-L-methionine as substrate (PubMed:30785395).
CC {ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30785395};
CC -!- SUBUNIT: Interacts with MYOD1. {ECO:0000250|UniProtKB:Q91WC0}.
CC -!- INTERACTION:
CC Q86TU7; P12004: PCNA; NbExp=3; IntAct=EBI-2908049, EBI-358311;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28442573,
CC ECO:0000269|PubMed:30626964}. Nucleus {ECO:0000269|PubMed:28442573}.
CC Note=Localizes mainly in the cytoplasm. {ECO:0000269|PubMed:28442573}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86TU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TU7-2; Sequence=VSP_021190, VSP_021193;
CC Name=3;
CC IsoId=Q86TU7-3; Sequence=VSP_021191, VSP_021192;
CC -!- DEVELOPMENTAL STAGE: Protein levels peak in S phase and are lowest
CC during M phase (at protein level). {ECO:0000269|PubMed:28442573}.
CC -!- DOMAIN: The SET domain specifically recognizes and binds actin,
CC suggesting that it does not accommodate substrates diverging from
CC actin. {ECO:0000269|PubMed:30626964}.
CC -!- PTM: Phosphorylated by GSK3B, which is required for recognition by the
CC SCF(FBXW7) complex and subsequent degradation.
CC {ECO:0000269|PubMed:28442573}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex following phosphorylation
CC by GSK3B, leading to its degradation by the proteasome.
CC {ECO:0000269|PubMed:28442573}.
CC -!- MISCELLANEOUS: Shows protein-methionine methyltransferase activity in
CC vitro on an actin mutant with a Met instead of a His residue at
CC position 73. {ECO:0000269|PubMed:32503840}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. SETD3 actin-histidine methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00898}.
CC -!- CAUTION: Was initially reported to have histone methyltransferase
CC activity and methylate 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and
CC H3K36me) (By similarity). However, this conclusion was based on mass
CC spectrometry data wherin mass shifts were inconsistent with a bona fide
CC methylation event (PubMed:30626964). In vitro, the protein-lysine
CC methyltransferase activity is weak compared to the protein-histidine
CC methyltransferase activity (PubMed:30526847).
CC {ECO:0000250|UniProtKB:Q91WC0, ECO:0000269|PubMed:30526847,
CC ECO:0000269|PubMed:30626964}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15525.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On versatility - Issue 215
CC of June 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/215/";
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DR EMBL; BX161441; CAD61911.1; -; mRNA.
DR EMBL; BX161471; CAD61927.1; -; mRNA.
DR EMBL; AK026680; BAB15525.1; ALT_FRAME; mRNA.
DR EMBL; AK302882; BAG64060.1; -; mRNA.
DR EMBL; AL110504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81664.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81665.1; -; Genomic_DNA.
DR EMBL; BC009054; AAH09054.2; -; mRNA.
DR EMBL; BC120967; AAI20968.1; -; mRNA.
DR EMBL; BC120968; AAI20969.1; -; mRNA.
DR EMBL; BC127624; AAI27625.1; -; mRNA.
DR EMBL; BC127625; AAI27626.1; -; mRNA.
DR EMBL; BC142995; AAI42996.1; -; mRNA.
DR EMBL; BC148251; AAI48252.1; -; mRNA.
DR EMBL; AL359581; CAH56365.1; -; mRNA.
DR CCDS; CCDS9951.1; -. [Q86TU7-1]
DR CCDS; CCDS9952.1; -. [Q86TU7-2]
DR PIR; T50614; T50614.
DR RefSeq; NP_115609.2; NM_032233.2. [Q86TU7-1]
DR RefSeq; NP_954574.1; NM_199123.1. [Q86TU7-2]
DR RefSeq; XP_011535533.2; XM_011537231.2. [Q86TU7-1]
DR RefSeq; XP_011535534.1; XM_011537232.2. [Q86TU7-1]
DR RefSeq; XP_011535537.1; XM_011537235.1. [Q86TU7-2]
DR RefSeq; XP_016877188.1; XM_017021699.1. [Q86TU7-1]
DR RefSeq; XP_016877189.1; XM_017021700.1. [Q86TU7-1]
DR PDB; 3SMT; X-ray; 2.04 A; A=2-498.
DR PDB; 6ICT; X-ray; 1.95 A; A/B/C/D=1-503.
DR PDB; 6ICV; X-ray; 2.15 A; A/B=1-503.
DR PDB; 6JAT; X-ray; 2.71 A; A/C=1-498.
DR PDB; 6MBJ; X-ray; 1.78 A; A/B=21-500, A/B=1-594.
DR PDB; 6MBK; X-ray; 1.69 A; A/B=21-503, A/B=1-594.
DR PDB; 6MBL; X-ray; 2.20 A; A=21-500, A=1-594.
DR PDB; 6OX0; X-ray; 1.75 A; A/B=1-594.
DR PDB; 6OX1; X-ray; 1.95 A; A/B=1-594.
DR PDB; 6OX2; X-ray; 2.09 A; A/B=1-594.
DR PDB; 6OX3; X-ray; 1.78 A; A/B=1-594.
DR PDB; 6OX4; X-ray; 2.29 A; A/B=1-594.
DR PDB; 6OX5; X-ray; 2.10 A; A=1-594.
DR PDB; 6V62; X-ray; 2.36 A; A=1-594.
DR PDB; 6V63; X-ray; 2.02 A; A/B=1-594.
DR PDB; 6WK1; X-ray; 1.89 A; A/B=1-594.
DR PDB; 6WK2; X-ray; 1.76 A; A/D=1-594.
DR PDBsum; 3SMT; -.
DR PDBsum; 6ICT; -.
DR PDBsum; 6ICV; -.
DR PDBsum; 6JAT; -.
DR PDBsum; 6MBJ; -.
DR PDBsum; 6MBK; -.
DR PDBsum; 6MBL; -.
DR PDBsum; 6OX0; -.
DR PDBsum; 6OX1; -.
DR PDBsum; 6OX2; -.
DR PDBsum; 6OX3; -.
DR PDBsum; 6OX4; -.
DR PDBsum; 6OX5; -.
DR PDBsum; 6V62; -.
DR PDBsum; 6V63; -.
DR PDBsum; 6WK1; -.
DR PDBsum; 6WK2; -.
DR AlphaFoldDB; Q86TU7; -.
DR SMR; Q86TU7; -.
DR BioGRID; 123940; 25.
DR IntAct; Q86TU7; 8.
DR MINT; Q86TU7; -.
DR STRING; 9606.ENSP00000327436; -.
DR GlyGen; Q86TU7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86TU7; -.
DR PhosphoSitePlus; Q86TU7; -.
DR BioMuta; SETD3; -.
DR DMDM; 74750394; -.
DR EPD; Q86TU7; -.
DR jPOST; Q86TU7; -.
DR MassIVE; Q86TU7; -.
DR MaxQB; Q86TU7; -.
DR PaxDb; Q86TU7; -.
DR PeptideAtlas; Q86TU7; -.
DR PRIDE; Q86TU7; -.
DR ProteomicsDB; 69732; -. [Q86TU7-1]
DR ProteomicsDB; 69733; -. [Q86TU7-2]
DR ProteomicsDB; 69734; -. [Q86TU7-3]
DR ABCD; Q86TU7; 1 sequenced antibody.
DR Antibodypedia; 147; 173 antibodies from 24 providers.
DR DNASU; 84193; -.
DR Ensembl; ENST00000329331.7; ENSP00000327910.3; ENSG00000183576.13. [Q86TU7-2]
DR Ensembl; ENST00000331768.10; ENSP00000327436.5; ENSG00000183576.13. [Q86TU7-1]
DR GeneID; 84193; -.
DR KEGG; hsa:84193; -.
DR MANE-Select; ENST00000331768.10; ENSP00000327436.5; NM_032233.3; NP_115609.2.
DR UCSC; uc001ygc.4; human. [Q86TU7-1]
DR CTD; 84193; -.
DR DisGeNET; 84193; -.
DR GeneCards; SETD3; -.
DR HGNC; HGNC:20493; SETD3.
DR HPA; ENSG00000183576; Low tissue specificity.
DR MIM; 615671; gene.
DR neXtProt; NX_Q86TU7; -.
DR OpenTargets; ENSG00000183576; -.
DR PharmGKB; PA134883013; -.
DR VEuPathDB; HostDB:ENSG00000183576; -.
DR eggNOG; KOG1337; Eukaryota.
DR GeneTree; ENSGT00940000153577; -.
DR HOGENOM; CLU_028272_0_0_1; -.
DR InParanoid; Q86TU7; -.
DR OMA; DFWMKIP; -.
DR PhylomeDB; Q86TU7; -.
DR TreeFam; TF354226; -.
DR BRENDA; 2.1.1.85; 2681.
DR PathwayCommons; Q86TU7; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR SignaLink; Q86TU7; -.
DR BioGRID-ORCS; 84193; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; SETD3; human.
DR GenomeRNAi; 84193; -.
DR Pharos; Q86TU7; Tbio.
DR PRO; PR:Q86TU7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86TU7; protein.
DR Bgee; ENSG00000183576; Expressed in calcaneal tendon and 217 other tissues.
DR ExpressionAtlas; Q86TU7; baseline and differential.
DR Genevisible; Q86TU7; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0030047; P:actin modification; IDA:UniProtKB.
DR GO; GO:0010452; P:histone H3-K36 methylation; ISS:UniProtKB.
DR GO; GO:0018021; P:peptidyl-histidine methylation; IDA:UniProtKB.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0070472; P:regulation of uterine smooth muscle contraction; ISS:UniProtKB.
DR CDD; cd19176; SET_SETD3; 1.
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 InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR025785; SETD3.
DR InterPro; IPR044428; SETD3_SET.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF81822; SSF81822; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51565; SAM_MT85_SETD3; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT CHAIN 1..594
FT /note="Actin-histidine N-methyltransferase"
FT /id="PRO_0000254175"
FT DOMAIN 94..314
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:30626964,
FT ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018,
FT ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215,
FT ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT,
FT ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT,
FT ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK,
FT ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0,
FT ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2,
FT ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4,
FT ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62,
FT ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1,
FT ECO:0007744|PDB:6WK2"
FT BINDING 104..106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:30626964,
FT ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018,
FT ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215,
FT ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT,
FT ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT,
FT ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK,
FT ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0,
FT ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2,
FT ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4,
FT ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62,
FT ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1,
FT ECO:0007744|PDB:6WK2"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:30626964,
FT ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018,
FT ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215,
FT ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT,
FT ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT,
FT ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK,
FT ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0,
FT ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2,
FT ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4,
FT ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62,
FT ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1,
FT ECO:0007744|PDB:6WK2"
FT BINDING 275..279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:30626964,
FT ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018,
FT ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215,
FT ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT,
FT ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT,
FT ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK,
FT ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0,
FT ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2,
FT ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4,
FT ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62,
FT ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1,
FT ECO:0007744|PDB:6WK2"
FT BINDING 325..327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:30626964,
FT ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018,
FT ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215,
FT ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT,
FT ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT,
FT ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK,
FT ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0,
FT ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2,
FT ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4,
FT ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62,
FT ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1,
FT ECO:0007744|PDB:6WK2"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 284..296
FT /note="ITTGYNLEDDRCE -> TPEDSFALAVASA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_021190"
FT VAR_SEQ 284
FT /note="I -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021191"
FT VAR_SEQ 285..594
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021192"
FT VAR_SEQ 297..594
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_021193"
FT VARIANT 278
FT /note="N -> D (in dbSNP:rs1740231)"
FT /id="VAR_028830"
FT MUTAGEN 37..42
FT /note="SSPAPG->ASPAPA: Does not affect ubiquitination and
FT degradation by the SCF(FBXW7) complex."
FT /evidence="ECO:0000269|PubMed:28442573"
FT MUTAGEN 181..185
FT /note="SEYDT->AEYDA: Decreased ubiquitination and
FT degradation by the SCF(FBXW7) complex."
FT /evidence="ECO:0000269|PubMed:28442573"
FT MUTAGEN 215
FT /note="R->A: Decreased binding to actin and decreased
FT protein-histidine N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30785395"
FT MUTAGEN 256
FT /note="N->A,V: Decreased binding to actin and decreased
FT protein-histidine N-methyltransferase activity. Increased
FT protein-lysine methyltransferase activity toward an actin
FT mutant with a Lys instead of a His target residue.
FT Increased protein-methionine methyltransferase activity
FT toward an actin mutant with a Met instead of a His target
FT residue."
FT /evidence="ECO:0000269|PubMed:30785395,
FT ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:32503840"
FT MUTAGEN 256
FT /note="N->F: Shows protein-lysine methyltransferase
FT activity toward an actin mutant with a Lys instead of a His
FT target residue; when associated with A-274."
FT /evidence="ECO:0000269|PubMed:31911441"
FT MUTAGEN 260..264
FT /note="TEDGS->AEDGA: Does not affect ubiquitination and
FT degradation by the SCF(FBXW7) complex."
FT /evidence="ECO:0000269|PubMed:28442573"
FT MUTAGEN 274
FT /note="W->A: Shows protein-lysine methyltransferase
FT activity toward an actin mutant with a Lys instead of a His
FT target residue; when associated with F-256."
FT /evidence="ECO:0000269|PubMed:31911441"
FT MUTAGEN 313
FT /note="Y->A: Abolished protein-histidine N-
FT methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30626964"
FT MUTAGEN 313
FT /note="Y->F: Strongly decreased binding to actin and
FT decreased protein-histidine N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30785395"
FT MUTAGEN 316
FT /note="R->A: Decreased binding to actin and decreased
FT protein-histidine N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30785395"
FT MUTAGEN 373..378
FT /note="TEPPIS->AEPPIA: Strongly decreased ubiquitination
FT and degradation by the SCF(FBXW7) complex."
FT /evidence="ECO:0000269|PubMed:28442573"
FT MUTAGEN 512..517
FT /note="SSVGDS->ASVGDA: Does not affect ubiquitination and
FT degradation by the SCF(FBXW7) complex."
FT /evidence="ECO:0000269|PubMed:28442573"
FT MUTAGEN 565..569
FT /note="SENES->AENEA: Does not affect ubiquitination and
FT degradation by the SCF(FBXW7) complex."
FT /evidence="ECO:0000269|PubMed:28442573"
FT CONFLICT 415
FT /note="E -> K (in Ref. 5; AAI42996)"
FT /evidence="ECO:0000305"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6OX1"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:6MBK"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6JAT"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:6MBK"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 203..226
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6OX0"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6V62"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6MBK"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 350..359
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 364..377
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:6JAT"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:6MBK"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 420..438
FT /evidence="ECO:0007829|PDB:6MBK"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 445..454
FT /evidence="ECO:0007829|PDB:6MBK"
FT HELIX 459..495
FT /evidence="ECO:0007829|PDB:6MBK"
SQ SEQUENCE 594 AA; 67257 MW; DF27C8B133A19E16 CRC64;
MGKKSRVKTQ KSGTGATATV SPKEILNLTS ELLQKCSSPA PGPGKEWEEY VQIRTLVEKI
RKKQKGLSVT FDGKREDYFP DLMKWASENG ASVEGFEMVN FKEEGFGLRA TRDIKAEELF
LWVPRKLLMT VESAKNSVLG PLYSQDRILQ AMGNIALAFH LLCERASPNS FWQPYIQTLP
SEYDTPLYFE EDEVRYLQST QAIHDVFSQY KNTARQYAYF YKVIQTHPHA NKLPLKDSFT
YEDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
QDFRAGEQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
GIPTSSVFAL HFTEPPISAQ LLAFLRVFCM TEEELKEHLL GDSAIDRIFT LGNSEFPVSW
DNEVKLWTFL EDRASLLLKT YKTTIEEDKS VLKNHDLSVR AKMAIKLRLG EKEILEKAVK
SAAVNREYYR QQMEEKAPLP KYEESNLGLL ESSVGDSRLP LVLRNLEEEA GVQDALNIRE
AISKAKATEN GLVNGENSIP NGTRSENESL NQESKRAVED AKGSSSDSTA GVKE
