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Protein arginine N-methyltransferase 5 (EC 2.1.1.320) (72 kDa ICln-binding protein) (Histone-arginine N-methyltransferase PRMT5) (Jak-binding protein 1) (Shk1 kinase-binding protein 1 homolog) (SKB1 homolog) (SKB1Hs) [Cleaved into: Protein arginine N-methyltransferase 5, N-terminally processed]

 ANM5_HUMAN              Reviewed;         637 AA.
O14744; A8MTP3; A8MZ91; B4DX49; B4DY30; B5BU10; D3DS33; E2QRE7;
Q6IBR1; Q9UKH1;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 166.
RecName: Full=Protein arginine N-methyltransferase 5;
EC=2.1.1.320 {ECO:0000269|PubMed:23071334};
AltName: Full=72 kDa ICln-binding protein;
AltName: Full=Histone-arginine N-methyltransferase PRMT5;
AltName: Full=Jak-binding protein 1;
AltName: Full=Shk1 kinase-binding protein 1 homolog;
Short=SKB1 homolog;
Short=SKB1Hs;
Contains:
RecName: Full=Protein arginine N-methyltransferase 5, N-terminally processed;
Name=PRMT5; Synonyms=HRMT1L5, IBP72, JBP1, SKB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INTERACTION WITH CLNS1A.
PubMed=9556550; DOI=10.1074/jbc.273.18.10811;
Krapivinsky G., Pu W., Wickman K., Krapivinsky L., Clapham D.E.;
"pICln binds to a mammalian homolog of a yeast protein involved in
regulation of cell morphology.";
J. Biol. Chem. 273:10811-10814(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9843966; DOI=10.1073/pnas.95.25.14781;
Gilbreth M., Yang P., Bartholomeusz G., Pimental R.A., Kansra S.,
Gadiraju R., Marcus S.;
"Negative regulation of mitosis in fission yeast by the shk1
interacting protein skb1 and its human homolog, Skb1Hs.";
Proc. Natl. Acad. Sci. U.S.A. 95:14781-14786(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
JAK2.
PubMed=10531356; DOI=10.1074/jbc.274.44.31531;
Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L.,
Pestka S.;
"The human homologue of the yeast proteins Skb1 and Hsl7p interacts
with Jak kinases and contains protein methyltransferase activity.";
J. Biol. Chem. 274:31531-31542(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
TISSUE=Testis, and Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 1-13 AND 594-601, FUNCTION IN THE REGULATION OF
MAPK1/MAPK3 SIGNALING PATHWAY, INTERACTION WITH BRAF AND RAF1, ENZYME
REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 365-GLY--GLY-369.
PubMed=21917714; DOI=10.1126/scisignal.2001936;
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C.,
Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R.,
Canals F., Merlino G., Avila M.A., Recio J.A.;
"Protein arginine methyltransferase 5 regulates ERK1/2 signal
transduction amplitude and cell fate through CRAF.";
Sci. Signal. 4:RA58-RA58(2011).
[11]
PROTEIN SEQUENCE OF 2-13.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[12]
FUNCTION, AND SUBUNIT.
PubMed=12411503; DOI=10.1093/emboj/cdf585;
Meister G., Fischer U.;
"Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the
formation of spliceosomal UsnRNPs.";
EMBO J. 21:5853-5863(2002).
[13]
FUNCTION, AND INTERACTION WITH EPB41L3.
PubMed=15737618; DOI=10.1016/j.bbrc.2005.01.153;
Jiang W., Roemer M.E., Newsham I.F.;
"The tumor suppressor DAL-1/4.1B modulates protein arginine N-
methyltransferase 5 activity in a substrate-specific manner.";
Biochem. Biophys. Res. Commun. 329:522-530(2005).
[14]
INTERACTION WITH LSM11.
PubMed=16087681; DOI=10.1074/jbc.M505077200;
Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
Fischer U., Schuemperli D.;
"Toward an assembly line for U7 snRNPs: interactions of U7-specific
Lsm proteins with PRMT5 and SMN complexes.";
J. Biol. Chem. 280:34435-34440(2005).
[15]
PROTEIN SEQUENCE OF 2-13; 19-49; 52-60; 69-95; 155-193; 201-248;
334-343; 349-377; 386-393; 422-428; 459-485 AND 489-526, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hepatoma, and Mammary carcinoma;
Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.,
Boldt K., von Kriegsheim A.F.;
Submitted (FEB-2008) to UniProtKB.
[16]
INTERACTION WITH SSTR1.
PubMed=10734105; DOI=10.1074/jbc.275.13.9557;
Schwaerzler A., Kreienkamp H.-J., Richter D.;
"Interaction of the somatostatin receptor subtype 1 with the human
homolog of the Shk1 kinase-binding protein from yeast.";
J. Biol. Chem. 275:9557-9562(2000).
[17]
FUNCTION, AND SUBUNIT.
PubMed=11152681; DOI=10.1074/jbc.M008660200;
Rho J., Choi S., Seong Y.R., Cho W.-K., Kim S.H., Im D.-S.;
"Prmt5, which forms distinct homo-oligomers, is a member of the
protein-arginine methyltransferase family.";
J. Biol. Chem. 276:11393-11401(2001).
[18]
FUNCTION IN THE METHYLATION AT SNRPD1 AND SNRPD3.
PubMed=11747828; DOI=10.1016/S0960-9822(01)00592-9;
Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.;
"Methylation of Sm proteins by a complex containing PRMT5 and the
putative U snRNP assembly factor pICln.";
Curr. Biol. 11:1990-1994(2001).
[19]
COMPONENT OF THE CERC COMPLEX.
PubMed=12101096; DOI=10.1093/embo-reports/kvf136;
Fabbrizio E., El Messaoudi S., Polanowska J., Paul C., Cook J.R.,
Lee J.-H., Negre V., Rousset M., Pestka S., Le Cam A., Sardet C.;
"Negative regulation of transcription by the type II arginine
methyltransferase PRMT5.";
EMBO Rep. 3:641-645(2002).
[20]
FUNCTION, AND INTERACTION WITH SUPT5H.
PubMed=12718890; DOI=10.1016/S1097-2765(03)00101-1;
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B.,
Gehrig P., Gaynor R.B.;
"Methylation of SPT5 regulates its interaction with RNA polymerase II
and transcriptional elongation properties.";
Mol. Cell 11:1055-1066(2003).
[21]
INTERACTION WITH THE SWI/SNF COMPLEX, MUTAGENESIS OF 367-GLY-ARG-368,
AND METHYLATION OF HISTONE H3.
PubMed=15485929; DOI=10.1128/MCB.24.21.9630-9645.2004;
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and
negatively regulates expression of ST7 and NM23 tumor suppressor
genes.";
Mol. Cell. Biol. 24:9630-9645(2004).
[22]
INTERACTION WITH IWS1.
PubMed=17184735; DOI=10.1016/j.bbrc.2006.11.133;
Liu Z., Zhou Z., Chen G., Bao S.;
"A putative transcriptional elongation factor hIws1 is essential for
mammalian cell proliferation.";
Biochem. Biophys. Res. Commun. 353:47-53(2007).
[23]
FUNCTION, AND INTERACTION WITH PRMT7 AND SNRPD3.
PubMed=17709427; DOI=10.1083/jcb.200702147;
Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I.,
Matera A.G.;
"Two distinct arginine methyltransferases are required for biogenesis
of Sm-class ribonucleoproteins.";
J. Cell Biol. 178:733-740(2007).
[24]
IDENTIFICATION IN THE METHYLOSOME COMPLEX.
PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
Englbrecht C., Sickmann A., Stark H., Fischer U.;
"An assembly chaperone collaborates with the SMN complex to generate
spliceosomal SnRNPs.";
Cell 135:497-509(2008).
[25]
INTERACTION WITH COPRS, AND SUBCELLULAR LOCATION.
PubMed=18404153; DOI=10.1038/embor.2008.45;
Lacroix M., Messaoudi S.E., Rodier G., Le Cam A., Sardet C.,
Fabbrizio E.;
"The histone-binding protein COPR5 is required for nuclear functions
of the protein arginine methyltransferase PRMT5.";
EMBO Rep. 9:452-458(2008).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20421892; DOI=10.1038/cr.2010.56;
Zhou Z., Sun X., Zou Z., Sun L., Zhang T., Guo S., Wen Y., Liu L.,
Wang Y., Qin J., Li L., Gong W., Bao S.;
"PRMT5 regulates Golgi apparatus structure through methylation of the
golgin GM130.";
Cell Res. 20:1023-1033(2010).
[28]
FUNCTION, AND INTERACTION WITH RPS10.
PubMed=20159986; DOI=10.1074/jbc.M110.103911;
Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.;
"Methylation of ribosomal protein S10 by protein-arginine
methyltransferase 5 regulates ribosome biogenesis.";
J. Biol. Chem. 285:12695-12705(2010).
[29]
FUNCTION IN CELL MIGRATION, AND INTERACTION WITH SRGAP2.
PubMed=20810653; DOI=10.1074/jbc.M110.153429;
Guo S., Bao S.;
"srGAP2 arginine methylation regulates cell migration and cell
spreading through promoting dimerization.";
J. Biol. Chem. 285:35133-35141(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
FUNCTION IN EGFR SIGNALING, FUNCTION IN EGFR METHYLATION, AND
INTERACTION WITH EGFR.
PubMed=21258366; DOI=10.1038/ncb2158;
Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J.,
Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T.,
Tsai C.H., Hung M.C.;
"Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation
negatively modulates EGFR-mediated ERK activation.";
Nat. Cell Biol. 13:174-181(2011).
[32]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOXA9.
PubMed=22269951; DOI=10.1128/MCB.05977-11;
Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A.,
Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.;
"HOXA9 methylation by PRMT5 is essential for endothelial cell
expression of leukocyte adhesion molecules.";
Mol. Cell. Biol. 32:1202-1213(2012).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[35]
FUNCTION, INTERACTION WITH CHTOP, AND IDENTIFICATION IN THE
METHYLOSOME COMPLEX WITH PRMT1; WDR77 AND ERH.
PubMed=25284789; DOI=10.1016/j.celrep.2014.08.071;
Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T.,
Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y.,
Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N.,
Toyoshima C., Shirahige K., Akiyama T.;
"5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis
by recruiting the CHTOP-methylosome complex.";
Cell Rep. 9:48-60(2014).
[36]
FUNCTION, AND INTERACTION WITH POLR2A AND SMN1.
PubMed=26700805; DOI=10.1038/nature16469;
Yanling Zhao D., Gish G., Braunschweig U., Li Y., Ni Z.,
Schmitges F.W., Zhong G., Liu K., Li W., Moffat J., Vedadi M., Min J.,
Pawson T.J., Blencowe B.J., Greenblatt J.F.;
"SMN and symmetric arginine dimethylation of RNA polymerase II C-
terminal domain control termination.";
Nature 529:48-53(2016).
[37]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH WDR77;
S-ADENOSYLMETHIONINE ANALOG AND HISTONE H4 PEPTIDE, CATALYTIC
ACTIVITY, ACTIVE SITE, SUBSTRATE-BINDING SITES, AND SUBUNIT.
PubMed=23071334; DOI=10.1073/pnas.1209814109;
Antonysamy S., Bonday Z., Campbell R.M., Doyle B., Druzina Z.,
Gheyi T., Han B., Jungheim L.N., Qian Y., Rauch C., Russell M.,
Sauder J.M., Wasserman S.R., Weichert K., Willard F.S., Zhang A.,
Emtage S.;
"Crystal structure of the human PRMT5:MEP50 complex.";
Proc. Natl. Acad. Sci. U.S.A. 109:17960-17965(2012).
-!- FUNCTION: Arginine methyltransferase that can both catalyze the
formation of omega-N monomethylarginine (MMA) and symmetrical
dimethylarginine (sDMA), with a preference for the formation of
MMA (PubMed:10531356, PubMed:11152681, PubMed:11747828,
PubMed:12411503, PubMed:15737618, PubMed:17709427,
PubMed:20159986, PubMed:20810653, PubMed:21258366,
PubMed:21917714, PubMed:22269951). Specifically mediates the
symmetrical dimethylation of arginine residues in the small
nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such
methylation being required for the assembly and biogenesis of
snRNP core particles (PubMed:12411503, PubMed:11747828,
PubMed:17709427). Methylates SUPT5H and may regulate its
transcriptional elongation properties (PubMed:12718890). Mono- and
dimethylates arginine residues of myelin basic protein (MBP) in
vitro. May play a role in cytokine-activated transduction
pathways. Negatively regulates cyclin E1 promoter activity and
cellular proliferation. Methylates histone H2A and H4 'Arg-3'
during germ cell development. Methylates histone H3 'Arg-8', which
may repress transcription. Methylates the Piwi proteins (PIWIL1,
PIWIL2 and PIWIL4), methylation of Piwi proteins being required
for the interaction with Tudor domain-containing proteins and
subsequent localization to the meiotic nuage (By similarity).
Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3
pathway acting at 2 levels. First, monomethylates EGFR; this
enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment,
eventually leading to reduced SOS1 phosphorylation
(PubMed:21917714, PubMed:21258366). Second, methylates RAF1 and
probably BRAF, hence destabilizing these 2 signaling proteins and
reducing their catalytic activity (PubMed:21917714). Required for
induction of E-selectin and VCAM-1, on the endothelial cells
surface at sites of inflammation. Methylates HOXA9
(PubMed:22269951). Methylates and regulates SRGAP2 which is
involved in cell migration and differentiation (PubMed:20810653).
Acts as a transcriptional corepressor in CRY1-mediated repression
of the core circadian component PER1 by regulating the H4R3
dimethylation at the PER1 promoter (By similarity). Methylates
GM130/GOLGA2, regulating Golgi ribbon formation (PubMed:20421892).
Methylates H4R3 in genes involved in glioblastomagenesis in a
CHTOP- and/or TET1-dependent manner (PubMed:25284789).
Symmetrically methylates POLR2A, a modification that allows the
recruitment to POLR2A of proteins including SMN1/SMN2 and SETX.
This is required for resolving RNA-DNA hybrids created by RNA
polymerase II, that form R-loop in transcription terminal regions,
an important step in proper transcription termination
(PubMed:26700805). {ECO:0000250|UniProtKB:Q8CIG8,
ECO:0000269|PubMed:10531356, ECO:0000269|PubMed:11152681,
ECO:0000269|PubMed:11747828, ECO:0000269|PubMed:12411503,
ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15737618,
ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:20159986,
ECO:0000269|PubMed:20421892, ECO:0000269|PubMed:20810653,
ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21917714,
ECO:0000269|PubMed:22269951, ECO:0000269|PubMed:25284789,
ECO:0000269|PubMed:26700805}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + [protein]-L-
arginine = 2 S-adenosyl-L-homocysteine + [protein]-
N(omega),N(omega')-dimethyl-L-arginine.
{ECO:0000269|PubMed:23071334}.
-!- ENZYME REGULATION: Activity is increased by EGF, HGF, FGF1 or FGF2
treatments, and slightly decreased by NGF treatment.
{ECO:0000269|PubMed:21917714}.
-!- SUBUNIT: Forms, at least, homodimers and homotetramers. Interacts
with PRDM1 (By similarity). Component of the methylosome, a 20S
complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50,
PRMT1 and ERH. Interacts with EGFR; methylates EGFR and stimulates
EGFR-mediated ERK activation. Interacts with HOXA9. Interacts with
SRGAP2. Found in a complex with COPRS, RUNX1 AND CBFB. Interacts
with CHTOP; the interaction symmetrically methylates CHTOP, but
seems to require the presence of PRMT1 (PubMed:25284789).
Interacts with EPB41L3; this modulates methylation of target
proteins. Component of a high molecular weight E2F-pocket protein
complex, CERC (cyclin E1 repressor complex). Associates with
SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4.
Interacts with JAK2, SSTR1, SUPT5H, BRAF and with active RAF1.
Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS;
promoting its recruitment on histone H4. Interacts with
CLNS1A/pICln. Identified in a complex with CLNS1A/pICln and Sm
proteins. Interacts with RPS10. Interacts with WDR77. Interacts
with IWS1. Interacts with CRY1. Interacts with POLR2A. Interacts
with SMN1/SMN2. {ECO:0000250|UniProtKB:Q8CIG8,
ECO:0000269|PubMed:10531356, ECO:0000269|PubMed:10734105,
ECO:0000269|PubMed:11152681, ECO:0000269|PubMed:12411503,
ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15485929,
ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:16087681,
ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17709427,
ECO:0000269|PubMed:18404153, ECO:0000269|PubMed:18984161,
ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:20810653,
ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21917714,
ECO:0000269|PubMed:22269951, ECO:0000269|PubMed:23071334,
ECO:0000269|PubMed:25284789, ECO:0000269|PubMed:26700805,
ECO:0000269|PubMed:9556550}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-351098, EBI-351098;
Q91XC0:Ajuba (xeno); NbExp=4; IntAct=EBI-351098, EBI-1565930;
Q8N8U2:CDYL2; NbExp=2; IntAct=EBI-351098, EBI-8467076;
P54105:CLNS1A; NbExp=8; IntAct=EBI-351098, EBI-724693;
Q9NQ92:COPRS; NbExp=6; IntAct=EBI-351098, EBI-1642558;
Q9Y6K1:DNMT3A; NbExp=4; IntAct=EBI-351098, EBI-923653;
Q01094:E2F1; NbExp=8; IntAct=EBI-351098, EBI-448924;
Q8TE85:GRHL3; NbExp=2; IntAct=EBI-351098, EBI-8469396;
Q9BX10:GTPBP2; NbExp=2; IntAct=EBI-351098, EBI-6115579;
P62805:HIST2H4B; NbExp=6; IntAct=EBI-351098, EBI-302023;
P31269:HOXA9; NbExp=4; IntAct=EBI-351098, EBI-742314;
P03418:N (xeno); NbExp=2; IntAct=EBI-351098, EBI-6930799;
Q86UQ8-1:NFE4; NbExp=2; IntAct=EBI-351098, EBI-15759783;
Q8WVJ2:NUDCD2; NbExp=2; IntAct=EBI-351098, EBI-1052153;
P24928:POLR2A; NbExp=6; IntAct=EBI-351098, EBI-295301;
Q86U06:RBM23; NbExp=3; IntAct=EBI-351098, EBI-780319;
Q9BRS2:RIOK1; NbExp=4; IntAct=EBI-351098, EBI-7307838;
O75044:SRGAP2; NbExp=4; IntAct=EBI-351098, EBI-1051034;
Q96RU7:TRIB3; NbExp=2; IntAct=EBI-351098, EBI-492476;
Q9BQA1:WDR77; NbExp=16; IntAct=EBI-351098, EBI-1237307;
P63104:YWHAZ; NbExp=2; IntAct=EBI-351098, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21917714,
ECO:0000269|PubMed:22269951}. Nucleus
{ECO:0000269|PubMed:18404153, ECO:0000269|PubMed:21917714,
ECO:0000269|PubMed:22269951}. Golgi apparatus
{ECO:0000269|PubMed:20421892}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seems to exist. According to EST
sequences.;
Name=1;
IsoId=O14744-1; Sequence=Displayed;
Name=2;
IsoId=O14744-2; Sequence=VSP_043382;
Note=No experimental confirmation available.;
Name=4;
IsoId=O14744-4; Sequence=VSP_043382, VSP_054768;
Note=No experimental confirmation available.;
Name=5;
IsoId=O14744-5; Sequence=VSP_054685;
Note=No experimental confirmation available.;
Name=3;
IsoId=O14744-3; Sequence=VSP_043382, VSP_054685;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9556550}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
-!- SEQUENCE CAUTION:
Sequence=BC005820; Type=Frameshift; Positions=370; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF015913; AAB66581.1; -; mRNA.
EMBL; AF167572; AAF04502.1; -; mRNA.
EMBL; AK075251; BAG52095.1; -; mRNA.
EMBL; AK301812; BAG63261.1; -; mRNA.
EMBL; AK302240; BAG63592.1; -; mRNA.
EMBL; CR456741; CAG33022.1; -; mRNA.
EMBL; AB451246; BAG70060.1; -; mRNA.
EMBL; AB451370; BAG70184.1; -; mRNA.
EMBL; AL132780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW66218.1; -; Genomic_DNA.
EMBL; CH471078; EAW66219.1; -; Genomic_DNA.
EMBL; CH471078; EAW66220.1; -; Genomic_DNA.
EMBL; CH471078; EAW66221.1; -; Genomic_DNA.
EMBL; BC005820; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC025979; AAH25979.1; -; mRNA.
CCDS; CCDS41922.1; -. [O14744-2]
CCDS; CCDS61394.1; -. [O14744-3]
CCDS; CCDS61395.1; -. [O14744-4]
CCDS; CCDS61396.1; -. [O14744-5]
CCDS; CCDS9579.1; -. [O14744-1]
PIR; T03842; T03842.
RefSeq; NP_001034708.1; NM_001039619.2. [O14744-2]
RefSeq; NP_001269882.1; NM_001282953.1. [O14744-3]
RefSeq; NP_001269884.1; NM_001282955.1. [O14744-5]
RefSeq; NP_001269885.1; NM_001282956.1. [O14744-4]
RefSeq; NP_006100.2; NM_006109.4. [O14744-1]
UniGene; Hs.367854; -.
PDB; 4GQB; X-ray; 2.06 A; A=1-637.
PDB; 4X60; X-ray; 2.35 A; A=2-637.
PDB; 4X61; X-ray; 2.85 A; A=2-637.
PDB; 4X63; X-ray; 3.05 A; A=2-637.
PDB; 5C9Z; X-ray; 2.36 A; A=2-637.
PDB; 5EMJ; X-ray; 2.27 A; A=2-637.
PDB; 5EMK; X-ray; 2.52 A; A=2-637.
PDB; 5EML; X-ray; 2.39 A; A=2-637.
PDB; 5EMM; X-ray; 2.37 A; A=2-637.
PDB; 5FA5; X-ray; 2.34 A; A=1-637.
PDBsum; 4GQB; -.
PDBsum; 4X60; -.
PDBsum; 4X61; -.
PDBsum; 4X63; -.
PDBsum; 5C9Z; -.
PDBsum; 5EMJ; -.
PDBsum; 5EMK; -.
PDBsum; 5EML; -.
PDBsum; 5EMM; -.
PDBsum; 5FA5; -.
ProteinModelPortal; O14744; -.
SMR; O14744; -.
BioGrid; 115688; 185.
CORUM; O14744; -.
DIP; DIP-33172N; -.
IntAct; O14744; 102.
MINT; MINT-1216859; -.
STRING; 9606.ENSP00000319169; -.
BindingDB; O14744; -.
ChEMBL; CHEMBL1795116; -.
GuidetoPHARMACOLOGY; 1256; -.
iPTMnet; O14744; -.
PhosphoSitePlus; O14744; -.
SwissPalm; O14744; -.
EPD; O14744; -.
MaxQB; O14744; -.
PaxDb; O14744; -.
PeptideAtlas; O14744; -.
PRIDE; O14744; -.
DNASU; 10419; -.
Ensembl; ENST00000216350; ENSP00000216350; ENSG00000100462. [O14744-3]
Ensembl; ENST00000324366; ENSP00000319169; ENSG00000100462. [O14744-1]
Ensembl; ENST00000397440; ENSP00000380582; ENSG00000100462. [O14744-4]
Ensembl; ENST00000397441; ENSP00000380583; ENSG00000100462. [O14744-2]
Ensembl; ENST00000553897; ENSP00000452555; ENSG00000100462. [O14744-5]
GeneID; 10419; -.
KEGG; hsa:10419; -.
UCSC; uc001whl.3; human. [O14744-1]
CTD; 10419; -.
DisGeNET; 10419; -.
EuPathDB; HostDB:ENSG00000100462.15; -.
GeneCards; PRMT5; -.
H-InvDB; HIX0011525; -.
HGNC; HGNC:10894; PRMT5.
HPA; CAB012459; -.
HPA; HPA005525; -.
HPA; HPA064708; -.
MIM; 604045; gene.
neXtProt; NX_O14744; -.
OpenTargets; ENSG00000100462; -.
PharmGKB; PA35794; -.
eggNOG; KOG0822; Eukaryota.
eggNOG; ENOG410XNZM; LUCA.
GeneTree; ENSGT00390000001141; -.
HOGENOM; HOG000175933; -.
HOVERGEN; HBG057083; -.
InParanoid; O14744; -.
KO; K02516; -.
OMA; INPLTHT; -.
OrthoDB; EOG091G03PD; -.
PhylomeDB; O14744; -.
TreeFam; TF300626; -.
BioCyc; MetaCyc:HS02092-MONOMER; -.
BRENDA; 2.1.1.125; 2681.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
SIGNOR; O14744; -.
ChiTaRS; PRMT5; human.
GeneWiki; Protein_arginine_methyltransferase_5; -.
GenomeRNAi; 10419; -.
PRO; PR:O14744; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100462; -.
CleanEx; HS_PRMT5; -.
ExpressionAtlas; O14744; baseline and differential.
Genevisible; O14744; HS.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0035097; C:histone methyltransferase complex; IDA:ParkinsonsUK-UCL.
GO; GO:0034709; C:methylosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); IMP:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
GO; GO:0008168; F:methyltransferase activity; IDA:MGI.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IMP:UniProtKB.
GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0006353; P:DNA-templated transcription, termination; IMP:UniProtKB.
GO; GO:0042118; P:endothelial cell activation; IMP:UniProtKB.
GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0018216; P:peptidyl-arginine methylation; IMP:UniProtKB.
GO; GO:0035246; P:peptidyl-arginine N-methylation; IDA:WormBase.
GO; GO:1904992; P:positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway; IGI:WormBase.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:ProtInc.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0000387; P:spliceosomal snRNP assembly; IMP:UniProtKB.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR007857; Arg_MeTrfase_PRMT5.
InterPro; IPR035075; PRMT5.
InterPro; IPR035248; PRMT5_C.
InterPro; IPR035247; PRMT5_TIM.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR10738; PTHR10738; 1.
Pfam; PF05185; PRMT5; 1.
Pfam; PF17286; PRMT5_C; 1.
Pfam; PF17285; PRMT5_TIM; 1.
PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Biological rhythms;
Chromatin regulator; Complete proteome; Cytoplasm;
Direct protein sequencing; Golgi apparatus; Methyltransferase;
Nucleus; Reference proteome; Repressor; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase.
CHAIN 1 637 Protein arginine N-methyltransferase 5.
/FTId=PRO_0000212342.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.15}.
CHAIN 2 637 Protein arginine N-methyltransferase 5,
N-terminally processed.
/FTId=PRO_0000417602.
DOMAIN 308 615 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
REGION 13 292 TIM barrel.
{ECO:0000269|PubMed:23071334}.
REGION 333 334 S-adenosyl-L-methionine binding.
{ECO:0000269|PubMed:23071334}.
REGION 419 420 S-adenosyl-L-methionine binding.
{ECO:0000269|PubMed:23071334}.
REGION 465 637 Beta barrel.
{ECO:0000269|PubMed:23071334}.
REGION 488 494 Dimerization.
{ECO:0000269|PubMed:23071334}.
ACT_SITE 435 435 Proton donor/acceptor.
{ECO:0000305|PubMed:23071334}.
ACT_SITE 444 444 Proton donor/acceptor.
{ECO:0000305|PubMed:23071334}.
BINDING 304 304 Peptide substrate.
{ECO:0000269|PubMed:23071334}.
BINDING 307 307 Peptide substrate.
{ECO:0000269|PubMed:23071334}.
BINDING 324 324 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:23071334}.
BINDING 392 392 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:23071334}.
SITE 327 327 Critical for specifying symmetric
addition of methyl groups.
{ECO:0000250|UniProtKB:P46580}.
MOD_RES 2 2 N-acetylalanine; in Protein arginine N-
methyltransferase 5, N-terminally
processed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.15}.
VAR_SEQ 1 34 MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA -> MRG
PNSGTEKGRLVIPE (in isoform 2, isoform 3
and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.5}.
/FTId=VSP_043382.
VAR_SEQ 77 120 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054685.
VAR_SEQ 106 259 Missing (in isoform 4).
{ECO:0000303|Ref.5}.
/FTId=VSP_054768.
MUTAGEN 365 369 Missing: Increased MAPK1/MAPK3
phosphorylation in response to EGF.
{ECO:0000269|PubMed:21917714}.
MUTAGEN 367 368 GR->AA: Abolishes enzymatic activity.
{ECO:0000269|PubMed:15485929}.
CONFLICT 183 183 E -> K (in Ref. 4; BAG63592).
{ECO:0000305}.
CONFLICT 247 247 S -> F (in Ref. 2; AAB66581).
{ECO:0000305}.
CONFLICT 420 420 M -> T (in Ref. 4; BAG63592).
{ECO:0000305}.
CONFLICT 553 553 G -> V (in Ref. 2; AAB66581).
{ECO:0000305}.
STRAND 16 19 {ECO:0000244|PDB:4GQB}.
HELIX 26 35 {ECO:0000244|PDB:4GQB}.
STRAND 39 46 {ECO:0000244|PDB:4GQB}.
STRAND 54 56 {ECO:0000244|PDB:4GQB}.
HELIX 59 61 {ECO:0000244|PDB:4GQB}.
HELIX 70 72 {ECO:0000244|PDB:4GQB}.
HELIX 75 81 {ECO:0000244|PDB:4GQB}.
STRAND 82 85 {ECO:0000244|PDB:4GQB}.
HELIX 97 117 {ECO:0000244|PDB:4GQB}.
STRAND 120 125 {ECO:0000244|PDB:4GQB}.
HELIX 132 142 {ECO:0000244|PDB:4GQB}.
STRAND 144 146 {ECO:0000244|PDB:5FA5}.
STRAND 150 158 {ECO:0000244|PDB:4GQB}.
HELIX 160 163 {ECO:0000244|PDB:4GQB}.
HELIX 181 183 {ECO:0000244|PDB:4GQB}.
HELIX 184 195 {ECO:0000244|PDB:4GQB}.
TURN 196 198 {ECO:0000244|PDB:4GQB}.
STRAND 202 207 {ECO:0000244|PDB:4GQB}.
HELIX 215 219 {ECO:0000244|PDB:4GQB}.
TURN 220 223 {ECO:0000244|PDB:4GQB}.
STRAND 226 232 {ECO:0000244|PDB:4GQB}.
HELIX 233 235 {ECO:0000244|PDB:4GQB}.
HELIX 248 259 {ECO:0000244|PDB:4GQB}.
STRAND 263 268 {ECO:0000244|PDB:4GQB}.
HELIX 273 275 {ECO:0000244|PDB:4GQB}.
HELIX 279 289 {ECO:0000244|PDB:4GQB}.
HELIX 296 300 {ECO:0000244|PDB:4GQB}.
HELIX 302 304 {ECO:0000244|PDB:5EMJ}.
STRAND 309 311 {ECO:0000244|PDB:4GQB}.
TURN 314 316 {ECO:0000244|PDB:4GQB}.
HELIX 321 327 {ECO:0000244|PDB:4GQB}.
HELIX 331 348 {ECO:0000244|PDB:4GQB}.
HELIX 351 353 {ECO:0000244|PDB:4GQB}.
TURN 354 356 {ECO:0000244|PDB:4GQB}.
STRAND 358 365 {ECO:0000244|PDB:4GQB}.
TURN 367 369 {ECO:0000244|PDB:5EMK}.
HELIX 370 381 {ECO:0000244|PDB:4GQB}.
STRAND 385 393 {ECO:0000244|PDB:4GQB}.
HELIX 395 407 {ECO:0000244|PDB:4GQB}.
HELIX 410 412 {ECO:0000244|PDB:4GQB}.
STRAND 413 418 {ECO:0000244|PDB:4GQB}.
TURN 420 422 {ECO:0000244|PDB:4GQB}.
STRAND 429 433 {ECO:0000244|PDB:4GQB}.
HELIX 442 444 {ECO:0000244|PDB:4GQB}.
HELIX 446 453 {ECO:0000244|PDB:4GQB}.
HELIX 454 456 {ECO:0000244|PDB:4GQB}.
STRAND 457 465 {ECO:0000244|PDB:4GQB}.
STRAND 467 476 {ECO:0000244|PDB:4GQB}.
HELIX 478 485 {ECO:0000244|PDB:4GQB}.
HELIX 496 499 {ECO:0000244|PDB:4GQB}.
STRAND 502 505 {ECO:0000244|PDB:5EMJ}.
STRAND 516 524 {ECO:0000244|PDB:4GQB}.
STRAND 527 529 {ECO:0000244|PDB:5FA5}.
STRAND 534 541 {ECO:0000244|PDB:4GQB}.
STRAND 546 560 {ECO:0000244|PDB:4GQB}.
STRAND 563 566 {ECO:0000244|PDB:4GQB}.
HELIX 569 571 {ECO:0000244|PDB:4GQB}.
STRAND 582 592 {ECO:0000244|PDB:4GQB}.
STRAND 597 606 {ECO:0000244|PDB:4GQB}.
STRAND 608 621 {ECO:0000244|PDB:4GQB}.
HELIX 628 630 {ECO:0000244|PDB:4GQB}.
SEQUENCE 637 AA; 72684 MW; 522E255B384F25E7 CRC64;
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFIQEPAK
NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR RNSEAAMLQE LNFGAYLGLP
AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDIIEN APTTHTEEYS
GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK
KGFPVLSKMH QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKDTNVQV
LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM
REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL
YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF
PVEVNTVLHG FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV
RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL


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