DGCR8_HUMAN
ID DGCR8_HUMAN Reviewed; 773 AA.
AC Q8WYQ5; B2R8G1; Q6DCB2; Q6MZE9; Q6Y2L0; Q96G39; Q96GP8; Q9H6L8; Q9H6T7;
AC Q9NRW2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Microprocessor complex subunit DGCR8;
DE AltName: Full=DiGeorge syndrome critical region 8;
GN Name=DGCR8; Synonyms=C22orf12, DGCRK6; ORFNames=LP4941;
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 [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12705904; DOI=10.1016/s0006-291x(03)00554-0;
RA Shiohama A., Sasaki T., Noda S., Minoshima S., Shimizu N.;
RT "Molecular cloning and expression analysis of a novel gene DGCR8 located in
RT the DiGeorge syndrome chromosomal region.";
RL Biochem. Biophys. Res. Commun. 304:184-190(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 204-773 (ISOFORM 1).
RC TISSUE=Hepatoma, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Muscle, and Testis;
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 [MRNA] OF 1-247.
RC TISSUE=Heart;
RA Gong L., Millas S., Jen J., Yeh E.T.H.;
RT "Isolation and characterization of a novel human gene deleted in DiGeorge
RT syndrome.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-773.
RC TISSUE=Salivary gland;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-773.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH DROSHA.
RX PubMed=15589161; DOI=10.1016/j.cub.2004.11.001;
RA Landthaler M., Yalcin A., Tuschl T.;
RT "The human DiGeorge syndrome critical region gene 8 and its D. melanogaster
RT homolog are required for miRNA biogenesis.";
RL Curr. Biol. 14:2162-2167(2004).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
RX PubMed=15574589; DOI=10.1101/gad.1262504;
RA Han J., Lee Y., Yeom K.-H., Kim Y.-K., Jin H., Kim V.N.;
RT "The Drosha-DGCR8 complex in primary microRNA processing.";
RL Genes Dev. 18:3016-3027(2004).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
RX PubMed=15531877; DOI=10.1038/nature03120;
RA Gregory R.I., Yan K.-P., Amuthan G., Chendrimada T., Doratotaj B.,
RA Cooch N., Shiekhattar R.;
RT "The microprocessor complex mediates the genesis of microRNAs.";
RL Nature 432:235-240(2004).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX, AND RNA-BINDING.
RX PubMed=16751099; DOI=10.1016/j.cell.2006.03.043;
RA Han J., Lee Y., Yeom K.-H., Nam J.-W., Heo I., Rhee J.-K., Sohn S.Y.,
RA Cho Y., Zhang B.-T., Kim V.N.;
RT "Molecular basis for the recognition of primary microRNAs by the Drosha-
RT DGCR8 complex.";
RL Cell 125:887-901(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16906129; DOI=10.1038/sj.embor.7400783;
RA Pauley K.M., Eystathioy T., Jakymiw A., Hamel J.C., Fritzler M.J.,
RA Chan E.K.L.;
RT "Formation of GW bodies is a consequence of microRNA genesis.";
RL EMBO Rep. 7:904-910(2006).
RN [15]
RP FUNCTION, INTERACTION WITH DROSHA, RNA-BINDING, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 568-ALA-ALA-569 AND 676-ALA-SER-677.
RX PubMed=16963499; DOI=10.1093/nar/gkl458;
RA Yeom K.-H., Lee Y., Han J., Suh M.R., Kim V.N.;
RT "Characterization of DGCR8/Pasha, the essential cofactor for Drosha in
RT primary miRNA processing.";
RL Nucleic Acids Res. 34:4622-4629(2006).
RN [16]
RP INTERACTION WITH ILF3; NCL AND DROSHA, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17765891; DOI=10.1016/j.yexcr.2007.07.020;
RA Shiohama A., Sasaki T., Noda S., Minoshima S., Shimizu N.;
RT "Nucleolar localization of DGCR8 and identification of eleven DGCR8-
RT associated proteins.";
RL Exp. Cell Res. 313:4196-4207(2007).
RN [17]
RP FUNCTION, SUBUNIT, COFACTOR, AND MUTAGENESIS OF CYS-352 AND CYS-430.
RX PubMed=17159994; DOI=10.1038/nsmb1182;
RA Faller M., Matsunaga M., Yin S., Loo J.A., Guo F.;
RT "Heme is involved in microRNA processing.";
RL Nat. Struct. Mol. Biol. 14:23-29(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; SER-275 AND SER-377, AND
RP IDENTIFICATION BY 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 [20]
RP INTERACTION WITH DROSHA.
RX PubMed=19135890; DOI=10.1016/j.cell.2008.10.053;
RA Han J., Pedersen J.S., Kwon S.C., Belair C.D., Kim Y.-K., Yeom K.-H.,
RA Yang W.-Y., Haussler D., Blelloch R., Kim V.N.;
RT "Posttranscriptional crossregulation between Drosha and DGCR8.";
RL Cell 136:75-84(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-275, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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 [24]
RP SUBCELLULAR LOCATION.
RX PubMed=22118463; DOI=10.1016/j.cell.2011.10.039;
RA Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J.,
RA Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.;
RT "Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct
RT mechanisms.";
RL Cell 147:1066-1079(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; THR-371 AND SER-377, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-275; SER-373 AND
RP SER-377, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-707, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [29]
RP FUNCTION, INTERACTION WITH DROSHA, AND SUBUNIT.
RX PubMed=26027739; DOI=10.1016/j.cell.2015.05.010;
RA Nguyen T.A., Jo M.H., Choi Y.G., Park J., Kwon S.C., Hohng S., Kim V.N.,
RA Woo J.S.;
RT "Functional anatomy of the human microprocessor.";
RL Cell 161:1374-1387(2015).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-500 AND LYS-707, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [31]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=25799998; DOI=10.1038/nature14281;
RA Alarcon C.R., Lee H., Goodarzi H., Halberg N., Tavazoie S.F.;
RT "N6-methyladenosine marks primary microRNAs for processing.";
RL Nature 519:482-485(2015).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-424 AND LYS-500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [33]
RP INTERACTION WITH PUS10.
RX PubMed=31819270; DOI=10.1038/s41589-019-0420-5;
RA Song J., Zhuang Y., Zhu C., Meng H., Lu B., Xie B., Peng J., Li M., Yi C.;
RT "Differential roles of human PUS10 in miRNA processing and tRNA
RT pseudouridylation.";
RL Nat. Chem. Biol. 16:160-169(2020).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 493-720, RNA-BINDING, AND
RP MUTAGENESIS OF 561-LYS--LYS-565 AND 669-LYS--LYS-673.
RX PubMed=17704815; DOI=10.1038/nsmb1294;
RA Sohn S.Y., Bae W.J., Kim J.J., Yeom K.-H., Kim V.N., Cho Y.;
RT "Crystal structure of human DGCR8 core.";
RL Nat. Struct. Mol. Biol. 14:847-853(2007).
RN [35]
RP STRUCTURE BY NMR OF 502-586.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of DSRM domain in DGCR8 protein.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [36]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 728-750 IN COMPLEX WITH DROSHA,
RP FUNCTION, INTERACTION WITH DROSHA, AND SUBUNIT.
RX PubMed=26748718; DOI=10.1016/j.cell.2015.12.019;
RA Kwon S.C., Nguyen T.A., Choi Y.G., Jo M.H., Hohng S., Kim V.N., Woo J.S.;
RT "Structure of human DROSHA.";
RL Cell 164:81-90(2016).
CC -!- FUNCTION: Component of the microprocessor complex that acts as a
CC RNA- and heme-binding protein that is involved in the initial step of
CC microRNA (miRNA) biogenesis. Component of the microprocessor complex
CC that is required to process primary miRNA transcripts (pri-miRNAs) to
CC release precursor miRNA (pre-miRNA) in the nucleus. Within the
CC microprocessor complex, DGCR8 function as a molecular anchor necessary
CC for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs
CC DROSHA to cleave 11 bp away form the junction to release hairpin-shaped
CC pre-miRNAs that are subsequently cut by the cytoplasmic DICER to
CC generate mature miRNAs (PubMed:26027739, PubMed:26748718). The heme-
CC bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers)
CC and is active in triggering pri-miRNA cleavage, whereas the heme-free
CC DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both
CC double-stranded and single-stranded regions of a pri-miRNA are required
CC for its binding (PubMed:15531877, PubMed:15574589, PubMed:15589161,
CC PubMed:16751099, PubMed:16906129, PubMed:16963499, PubMed:17159994).
CC Specifically recognizes and binds N6-methyladenosine (m6A)-containing
CC pri-miRNAs, a modification required for pri-miRNAs processing
CC (PubMed:25799998). Involved in the silencing of embryonic stem cell
CC self-renewal (By similarity). {ECO:0000250|UniProtKB:Q9EQM6,
CC ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15574589,
CC ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099,
CC ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:16963499,
CC ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:25799998,
CC ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:17159994};
CC Note=Binds 1 heme group per homodimer. {ECO:0000269|PubMed:17159994};
CC -!- SUBUNIT: Monomer; in absence of heme. Homodimer; the association with
CC heme promotes its dimerization (PubMed:17159994). Component of the
CC microprocessor complex, or pri-miRNA processing protein complex, which
CC is composed of DROSHA and DGCR8 (PubMed:15589161, PubMed:15574589,
CC PubMed:15531877, PubMed:16751099, PubMed:19135890, PubMed:26027739,
CC PubMed:26748718). The microprocessor complex is a heterotrimer; each of
CC the two DROSHA RNase III domains binds one DGCR8 (via C-terminal
CC region) (PubMed:26027739, PubMed:26748718). Interacts with ILF3, NCL
CC and DROSHA (PubMed:17765891). Interacts with CPSF3 and ISY1; this
CC interaction is in an RNA dependent manner (By similarity). Interacts
CC with PUS10; interaction promotes pri-miRNAs processing
CC (PubMed:31819270). {ECO:0000250|UniProtKB:Q9EQM6,
CC ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15574589,
CC ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099,
CC ECO:0000269|PubMed:16963499, ECO:0000269|PubMed:17159994,
CC ECO:0000269|PubMed:17765891, ECO:0000269|PubMed:19135890,
CC ECO:0000269|PubMed:26748718, ECO:0000269|PubMed:31819270}.
CC -!- INTERACTION:
CC Q8WYQ5; Q8WYQ5: DGCR8; NbExp=2; IntAct=EBI-528411, EBI-528411;
CC Q8WYQ5; Q9NRR4: DROSHA; NbExp=13; IntAct=EBI-528411, EBI-528367;
CC Q8WYQ5; P50222: MEOX2; NbExp=3; IntAct=EBI-528411, EBI-748397;
CC Q8WYQ5; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-528411, EBI-539478;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16906129,
CC ECO:0000269|PubMed:16963499, ECO:0000269|PubMed:17159994,
CC ECO:0000269|PubMed:22118463}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:17159994}. Note=Colocalizes with nucleolin and
CC DROSHA in the nucleolus. Mostly detected in the nucleolus as electron-
CC dense granular patches around the fibrillar center (FC) and granular
CC component (GC). Also detected in the nucleoplasm as small foci adjacent
CC to splicing speckles near the chromatin structure. Localized with
CC DROSHA in GW bodies (GWBs), also known as P-bodies (PubMed:17159994).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WYQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WYQ5-2; Sequence=VSP_003847, VSP_003848;
CC Name=3;
CC IsoId=Q8WYQ5-3; Sequence=VSP_012707;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12705904}.
CC -!- DOMAIN: Both DRBM domains are required for efficient binding to pri-
CC miRNA. The region between residues 276 and 498 has an autoinhibitory
CC function on pri-miRNA processing activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO86726.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15165.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15238.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB050770; BAB83032.1; -; Genomic_DNA.
DR EMBL; CR456356; CAG30242.1; -; mRNA.
DR EMBL; AK025539; BAB15165.1; ALT_INIT; mRNA.
DR EMBL; AK025780; BAB15238.1; ALT_INIT; mRNA.
DR EMBL; AK313357; BAG36158.1; -; mRNA.
DR EMBL; AC006547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009323; AAH09323.2; -; mRNA.
DR EMBL; BC009984; AAH09984.1; -; mRNA.
DR EMBL; BC078147; AAH78147.1; -; mRNA.
DR EMBL; AF165527; AAF82263.1; -; mRNA.
DR EMBL; BX649187; CAE46205.2; -; mRNA.
DR EMBL; AY189282; AAO86726.1; ALT_INIT; mRNA.
DR CCDS; CCDS13773.1; -. [Q8WYQ5-1]
DR CCDS; CCDS54501.1; -. [Q8WYQ5-3]
DR RefSeq; NP_001177255.1; NM_001190326.1. [Q8WYQ5-3]
DR RefSeq; NP_073557.3; NM_022720.6. [Q8WYQ5-1]
DR PDB; 1X47; NMR; -; A=502-586.
DR PDB; 2YT4; X-ray; 2.60 A; A=493-720.
DR PDB; 3LE4; X-ray; 1.70 A; A=275-353.
DR PDB; 5B16; X-ray; 3.20 A; B/C=728-750.
DR PDB; 6LXD; EM; 3.90 A; B/C=1-773.
DR PDB; 6LXE; EM; 4.20 A; B/C=1-773.
DR PDB; 6V5B; EM; 3.70 A; B/C=223-751.
DR PDB; 6V5C; EM; 4.40 A; B/C=223-751.
DR PDB; 7CNC; X-ray; 1.60 A; B=96-126.
DR PDBsum; 1X47; -.
DR PDBsum; 2YT4; -.
DR PDBsum; 3LE4; -.
DR PDBsum; 5B16; -.
DR PDBsum; 6LXD; -.
DR PDBsum; 6LXE; -.
DR PDBsum; 6V5B; -.
DR PDBsum; 6V5C; -.
DR PDBsum; 7CNC; -.
DR AlphaFoldDB; Q8WYQ5; -.
DR BMRB; Q8WYQ5; -.
DR SASBDB; Q8WYQ5; -.
DR SMR; Q8WYQ5; -.
DR BioGRID; 119986; 248.
DR ComplexPortal; CPX-3080; Microprocessor complex.
DR CORUM; Q8WYQ5; -.
DR DIP; DIP-29261N; -.
DR IntAct; Q8WYQ5; 118.
DR MINT; Q8WYQ5; -.
DR STRING; 9606.ENSP00000263209; -.
DR GlyGen; Q8WYQ5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WYQ5; -.
DR PhosphoSitePlus; Q8WYQ5; -.
DR BioMuta; DGCR8; -.
DR DMDM; 23813990; -.
DR EPD; Q8WYQ5; -.
DR jPOST; Q8WYQ5; -.
DR MassIVE; Q8WYQ5; -.
DR MaxQB; Q8WYQ5; -.
DR PaxDb; Q8WYQ5; -.
DR PeptideAtlas; Q8WYQ5; -.
DR PRIDE; Q8WYQ5; -.
DR ProteomicsDB; 75188; -. [Q8WYQ5-1]
DR ProteomicsDB; 75189; -. [Q8WYQ5-2]
DR ProteomicsDB; 75190; -. [Q8WYQ5-3]
DR Antibodypedia; 7887; 327 antibodies from 35 providers.
DR DNASU; 54487; -.
DR Ensembl; ENST00000351989.8; ENSP00000263209.3; ENSG00000128191.16. [Q8WYQ5-1]
DR Ensembl; ENST00000383024.6; ENSP00000372488.2; ENSG00000128191.16. [Q8WYQ5-3]
DR Ensembl; ENST00000407755.1; ENSP00000384726.1; ENSG00000128191.16. [Q8WYQ5-3]
DR GeneID; 54487; -.
DR KEGG; hsa:54487; -.
DR MANE-Select; ENST00000351989.8; ENSP00000263209.3; NM_022720.7; NP_073557.3.
DR UCSC; uc002zri.4; human. [Q8WYQ5-1]
DR CTD; 54487; -.
DR DisGeNET; 54487; -.
DR GeneCards; DGCR8; -.
DR GeneReviews; DGCR8; -.
DR HGNC; HGNC:2847; DGCR8.
DR HPA; ENSG00000128191; Low tissue specificity.
DR MalaCards; DGCR8; -.
DR MIM; 609030; gene.
DR neXtProt; NX_Q8WYQ5; -.
DR OpenTargets; ENSG00000128191; -.
DR PharmGKB; PA27309; -.
DR VEuPathDB; HostDB:ENSG00000128191; -.
DR eggNOG; KOG4334; Eukaryota.
DR GeneTree; ENSGT00390000015977; -.
DR HOGENOM; CLU_017211_3_0_1; -.
DR InParanoid; Q8WYQ5; -.
DR OMA; QDYKADT; -.
DR OrthoDB; 855874at2759; -.
DR PhylomeDB; Q8WYQ5; -.
DR TreeFam; TF324256; -.
DR PathwayCommons; Q8WYQ5; -.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-HSA-8986944; Transcriptional Regulation by MECP2.
DR SignaLink; Q8WYQ5; -.
DR SIGNOR; Q8WYQ5; -.
DR BioGRID-ORCS; 54487; 362 hits in 1093 CRISPR screens.
DR ChiTaRS; DGCR8; human.
DR EvolutionaryTrace; Q8WYQ5; -.
DR GeneWiki; DGCR8_(gene); -.
DR GenomeRNAi; 54487; -.
DR Pharos; Q8WYQ5; Tbio.
DR PRO; PR:Q8WYQ5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8WYQ5; protein.
DR Bgee; ENSG00000128191; Expressed in right hemisphere of cerebellum and 188 other tissues.
DR ExpressionAtlas; Q8WYQ5; baseline and differential.
DR Genevisible; Q8WYQ5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070877; C:microprocessor complex; IDA:BHF-UCL.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0140517; F:protein-RNA adaptor activity; IDA:BHF-UCL.
DR GO; GO:0031053; P:primary miRNA processing; IDA:BHF-UCL.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IEA:Ensembl.
DR CDD; cd00201; WW; 1.
DR InterPro; IPR040375; DGCR8.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR13482; PTHR13482; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Heme; Iron; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..773
FT /note="Microprocessor complex subunit DGCR8"
FT /id="PRO_0000079878"
FT DOMAIN 301..334
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 511..578
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 620..685
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 1..342
FT /note="Necessary for interaction with NCL"
FT /evidence="ECO:0000269|PubMed:17765891"
FT REGION 1..275
FT /note="Necessary for nuclear localization and retention"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..751
FT /note="Necessary for heme-binding and pri-miRNA processing"
FT REGION 360..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..773
FT /note="Interaction with DROSHA"
FT /evidence="ECO:0000269|PubMed:26748718"
FT REGION 742..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:17159994"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQM6"
FT MOD_RES 371
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 707
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297"
FT VAR_SEQ 303..304
FT /note="LP -> VL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_003847"
FT VAR_SEQ 305..773
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_003848"
FT VAR_SEQ 536..568
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012707"
FT VARIANT 174
FT /note="I -> V (in dbSNP:rs35987994)"
FT /id="VAR_050952"
FT VARIANT 725
FT /note="N -> D (in dbSNP:rs11546015)"
FT /id="VAR_050953"
FT MUTAGEN 352
FT /note="C->A,H: Inhibits heme-binding and dimerization."
FT /evidence="ECO:0000269|PubMed:17159994"
FT MUTAGEN 430
FT /note="C->A: Does not inhibit heme-binding and
FT dimerization."
FT /evidence="ECO:0000269|PubMed:17159994"
FT MUTAGEN 561..565
FT /note="KKLAK->AALAA: Strongly reduces pri-miRNA binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:17704815"
FT MUTAGEN 568..569
FT /note="AA->KK: Reduces pri-miRNA binding affinity and pri-
FT miRNA processing activity. Does not inhibit interaction
FT with DROSHA. When associated with A-676 and S-677, strongly
FT reduces binding affinity and pri-miRNA processing
FT activity."
FT /evidence="ECO:0000269|PubMed:16963499"
FT MUTAGEN 669..673
FT /note="KRVGK->AAVGA: Strongly reduces pri-miRNA binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:17704815"
FT MUTAGEN 676..677
FT /note="AS->KK: Reduces pri-miRNA binding affinity and pri-
FT miRNA processing activity. Slightly inhibits interaction
FT with DROSHA. When associated with A-568 and A-568, strongly
FT reduces binding affinity and pri-miRNA processing
FT activity."
FT /evidence="ECO:0000269|PubMed:16963499"
FT CONFLICT 241..247
FT /note="DDFDNDV -> VCWQPLL (in Ref. 6; AAF82263)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="P -> L (in Ref. 3; BAB15165)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="H -> Y (in Ref. 3; BAB15165)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="V -> A (in Ref. 3; BAB15165)"
FT /evidence="ECO:0000305"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:7CNC"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:3LE4"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:3LE4"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:3LE4"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:3LE4"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3LE4"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3LE4"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 512..522
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:1X47"
FT STRAND 542..548
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 551..560
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 561..576
FT /evidence="ECO:0007829|PDB:2YT4"
FT TURN 578..582
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 594..600
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 608..615
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 620..629
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 637..640
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 651..657
FT /evidence="ECO:0007829|PDB:2YT4"
FT STRAND 660..668
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 669..684
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 691..698
FT /evidence="ECO:0007829|PDB:2YT4"
FT HELIX 728..749
FT /evidence="ECO:0007829|PDB:5B16"
SQ SEQUENCE 773 AA; 86045 MW; 72D962BBE32890EC CRC64;
METDESPSPL PCGPAGEAVM ESRARPFQAL PREQSPPPPL QTSSGAEVMD VGSGGDGQSE
LPAEDPFNFY GASLLSKGSF SKGRLLIDPN CSGHSPRTAR HAPAVRKFSP DLKLLKDVKI
SVSFTESCRS KDRKVLYTGA ERDVRAECGL LLSPVSGDVH ACPFGGSVGD GVGIGGESAD
KKDEENELDQ EKRVEYAVLD ELEDFTDNLE LDEEGAGGFT AKAIVQRDRV DEEALNFPYE
DDFDNDVDAL LEEGLCAPKK RRTEEKYGGD SDHPSDGETS VQPMMTKIKT VLKSRGRPPT
EPLPDGWIMT FHNSGVPVYL HRESRVVTWS RPYFLGTGSI RKHDPPLSSI PCLHYKKMKD
NEEREQSSDL TPSGDVSPVK PLSRSAELEF PLDEPDSMGA DPGPPDEKDP LGAEAAPGAL
GQVKAKVEVC KDESVDLEEF RSYLEKRFDF EQVTVKKFRT WAERRQFNRE MKRKQAESER
PILPANQKLI TLSVQDAPTK KEFVINPNGK SEVCILHEYM QRVLKVRPVY NFFECENPSE
PFGASVTIDG VTYGSGTASS KKLAKNKAAR ATLEILIPDF VKQTSEEKPK DSEELEYFNH
ISIEDSRVYE LTSKAGLLSP YQILHECLKR NHGMGDTSIK FEVVPGKNQK SEYVMACGKH
TVRGWCKNKR VGKQLASQKI LQLLHPHVKN WGSLLRMYGR ESSKMVKQET SDKSVIELQQ
YAKKNKPNLH ILSKLQEEMK RLAEEREETR KKPKMSIVAS AQPGGEPLCT VDV
