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 05-FEB-2025, entry version 167. 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 = N(tele)- CC methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine + H(+); 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7LMS; EM; 3.50 A; A=2-594. DR PDB; 7W28; X-ray; 1.79 A; A=1-498. DR PDB; 7W29; X-ray; 2.90 A; A=1-498. DR PDB; 8X77; X-ray; 3.52 A; A/B/D/G=1-594. DR PDB; 8X8Q; EM; 3.14 A; B=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 PDBsum; 7LMS; -. DR PDBsum; 7W28; -. DR PDBsum; 7W29; -. DR PDBsum; 8X77; -. DR PDBsum; 8X8Q; -. DR AlphaFoldDB; Q86TU7; -. DR EMDB; EMD-23441; -. DR EMDB; EMD-38156; -. DR SMR; Q86TU7; -. DR BioGRID; 123940; 38. DR IntAct; Q86TU7; 9. 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 jPOST; Q86TU7; -. DR MassIVE; Q86TU7; -. DR PaxDb; 9606-ENSP00000327436; -. DR PeptideAtlas; Q86TU7; -. DR ProteomicsDB; 69732; -. [Q86TU7-1] DR ProteomicsDB; 69733; -. [Q86TU7-2] DR ProteomicsDB; 69734; -. [Q86TU7-3] DR Pumba; Q86TU7; -. DR ABCD; Q86TU7; 1 sequenced antibody. DR Antibodypedia; 147; 211 antibodies from 25 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 AGR; HGNC:20493; -. 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; QHIDGIF; -. DR OrthoDB; 441812at2759; -. 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; 13 hits in 1158 CRISPR screens. DR ChiTaRS; SETD3; human. DR EvolutionaryTrace; Q86TU7; -. 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 219 other cell types or tissues. DR ExpressionAtlas; Q86TU7; baseline and differential. 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 H3K36 methyltransferase activity; ISS:UniProtKB. DR GO; GO:0042800; F:histone H3K4 methyltransferase activity; 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:0018021; P:peptidyl-histidine methylation; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; 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:0070472; P:regulation of uterine smooth muscle contraction; ISS:UniProtKB. DR CDD; cd19176; SET_SETD3; 1. DR FunFam; 3.90.1410.10:FF:000001; histone-lysine N-methyltransferase setd3 isoform X1; 1. DR FunFam; 3.90.1420.10:FF:000001; histone-lysine N-methyltransferase setd3 isoform X1; 1. DR Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1. DR Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 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 InterPro; IPR050600; SETD3_SETD6_MTase. DR PANTHER; PTHR13271:SF47; ACTIN-HISTIDINE N-METHYLTRANSFERASE; 1. DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1. DR Pfam; PF09273; Rubis-subs-bind; 1. DR Pfam; PF00856; SET; 1. DR SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1. DR SUPFAM; SSF82199; SET domain; 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; Proteomics identification; KW Reference proteome; 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 10..20 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 555..572 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 573..582 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 583..594 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 //