ANM9_HUMAN
ID ANM9_HUMAN Reviewed; 845 AA.
AC Q6P2P2; A8KA39; B3KU92; Q6ZR58; Q8N383; Q9BT55; Q9NT98;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein arginine N-methyltransferase 9;
DE AltName: Full=Protein arginine N-methyltransferase 10;
DE EC=2.1.1.320 {ECO:0000269|PubMed:25737013, ECO:0000269|PubMed:25979344, ECO:0000269|PubMed:27387499};
GN Name=PRMT9 {ECO:0000312|HGNC:HGNC:25099}; Synonyms=PRMT10;
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=Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, Skin, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 678-845 (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 [6]
RP IDENTIFICATION.
RX PubMed=17005254; DOI=10.1016/j.pharmthera.2006.06.007;
RA Krause C.D., Yang Z.-H., Kim Y.-S., Lee J.-H., Cook J.R., Pestka S.;
RT "Protein arginine methyltransferases: evolution and assessment of their
RT pharmacological and therapeutic potential.";
RL Pharmacol. Ther. 113:50-87(2007).
RN [7]
RP IDENTIFICATION.
RX PubMed=19300908; DOI=10.1007/s00018-009-0010-x;
RA Wolf S.S.;
RT "The protein arginine methyltransferase family: an update about function,
RT new perspectives and the physiological role in humans.";
RL Cell. Mol. Life Sci. 66:2109-2121(2009).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH SF3B2, CATALYTIC ACTIVITY,
RP AND MUTAGENESIS OF 182-LEU--GLY-185.
RX PubMed=25737013; DOI=10.1038/ncomms7428;
RA Yang Y., Hadjikyriacou A., Xia Z., Gayatri S., Kim D., Zurita-Lopez C.,
RA Kelly R., Guo A., Li W., Clarke S.G., Bedford M.T.;
RT "PRMT9 is a type II methyltransferase that methylates the splicing factor
RT SAP145.";
RL Nat. Commun. 6:6428-6428(2015).
RN [9]
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF ASP-258 AND GLY-260, AND IDENTIFICATION IN A
RP COMPLEX WITH PRMT9; SF3B2 AND SF3B4.
RX PubMed=25979344; DOI=10.1074/jbc.m115.659433;
RA Hadjikyriacou A., Yang Y., Espejo A., Bedford M.T., Clarke S.G.;
RT "Unique features of human protein arginine methyltransferase 9 (PRMT9) and
RT its substrate RNA splicing factor SF3B2.";
RL J. Biol. Chem. 290:16723-16743(2015).
RN [10]
RP MUTAGENESIS OF CYS-431, AND CATALYTIC ACTIVITY.
RX PubMed=27387499; DOI=10.1074/jbc.m116.740399;
RA Jain K., Warmack R.A., Debler E.W., Hadjikyriacou A., Stavropoulos P.,
RA Clarke S.G.;
RT "Protein arginine methyltransferase product specificity is mediated by
RT distinct active-site architectures.";
RL J. Biol. Chem. 291:18299-18308(2016).
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA). Specifically mediates the symmetrical
CC dimethylation of SF3B2. Involved in the regulation of alternative
CC splicing of pre-mRNA (PubMed:25737013, PubMed:25979344).
CC {ECO:0000269|PubMed:25737013, ECO:0000269|PubMed:25979344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000269|PubMed:25737013, ECO:0000269|PubMed:25979344,
CC ECO:0000269|PubMed:27387499};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between is between 7.5 and 8.0.
CC {ECO:0000269|PubMed:25979344};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:25979344};
CC -!- SUBUNIT: Found in a complex with PRMT9, SF3B2 and SF3B4
CC (PubMed:25737013). Interacts with SF3B2 (PubMed:25737013).
CC {ECO:0000269|PubMed:25737013}.
CC -!- INTERACTION:
CC Q6P2P2; Q13435: SF3B2; NbExp=9; IntAct=EBI-10962083, EBI-749111;
CC Q6P2P2; Q15427: SF3B4; NbExp=3; IntAct=EBI-10962083, EBI-348469;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25737013,
CC ECO:0000269|PubMed:25979344}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P2P2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2P2-2; Sequence=VSP_053972;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- CAUTION: This protein should not be confused with FBXO11 (AC Q86XK2)
CC that was initially erroneously named PRMT9. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87459.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK128483; BAC87459.1; ALT_SEQ; mRNA.
DR EMBL; AK096703; BAG53354.1; -; mRNA.
DR EMBL; AK292904; BAF85593.1; -; mRNA.
DR EMBL; AC093835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX05013.1; -; Genomic_DNA.
DR EMBL; BC004337; AAH04337.1; -; mRNA.
DR EMBL; BC021250; AAH21250.2; -; mRNA.
DR EMBL; BC064403; AAH64403.1; -; mRNA.
DR EMBL; AL137452; CAB70744.1; -; mRNA.
DR EMBL; CH471056; EAX05011.1; -; Genomic_DNA.
DR CCDS; CCDS3771.1; -. [Q6P2P2-1]
DR PIR; T46267; T46267.
DR RefSeq; NP_001291387.1; NM_001304458.1. [Q6P2P2-2]
DR RefSeq; NP_612373.2; NM_138364.3. [Q6P2P2-1]
DR PDB; 6PDM; X-ray; 2.45 A; A=127-845.
DR PDB; 7RBQ; X-ray; 2.20 A; A=127-845.
DR PDB; 7T39; X-ray; 2.81 A; A=127-845.
DR PDBsum; 6PDM; -.
DR PDBsum; 7RBQ; -.
DR PDBsum; 7T39; -.
DR AlphaFoldDB; Q6P2P2; -.
DR SMR; Q6P2P2; -.
DR BioGRID; 124766; 27.
DR IntAct; Q6P2P2; 12.
DR STRING; 9606.ENSP00000314396; -.
DR ChEMBL; CHEMBL4105724; -.
DR iPTMnet; Q6P2P2; -.
DR PhosphoSitePlus; Q6P2P2; -.
DR BioMuta; PRMT9; -.
DR DMDM; 74758248; -.
DR EPD; Q6P2P2; -.
DR jPOST; Q6P2P2; -.
DR MassIVE; Q6P2P2; -.
DR MaxQB; Q6P2P2; -.
DR PaxDb; Q6P2P2; -.
DR PeptideAtlas; Q6P2P2; -.
DR PRIDE; Q6P2P2; -.
DR ProteomicsDB; 3704; -.
DR ProteomicsDB; 66914; -. [Q6P2P2-1]
DR ProteomicsDB; 66915; -. [Q6P2P2-2]
DR Antibodypedia; 49190; 136 antibodies from 19 providers.
DR DNASU; 90826; -.
DR Ensembl; ENST00000322396.7; ENSP00000314396.6; ENSG00000164169.13. [Q6P2P2-1]
DR GeneID; 90826; -.
DR KEGG; hsa:90826; -.
DR MANE-Select; ENST00000322396.7; ENSP00000314396.6; NM_138364.4; NP_612373.2.
DR UCSC; uc003ilc.4; human. [Q6P2P2-1]
DR CTD; 90826; -.
DR DisGeNET; 90826; -.
DR GeneCards; PRMT9; -.
DR HGNC; HGNC:25099; PRMT9.
DR HPA; ENSG00000164169; Low tissue specificity.
DR MIM; 616125; gene.
DR neXtProt; NX_Q6P2P2; -.
DR OpenTargets; ENSG00000164169; -.
DR PharmGKB; PA165664476; -.
DR VEuPathDB; HostDB:ENSG00000164169; -.
DR eggNOG; KOG1501; Eukaryota.
DR GeneTree; ENSGT00940000158472; -.
DR HOGENOM; CLU_017482_1_0_1; -.
DR InParanoid; Q6P2P2; -.
DR OMA; QTCILES; -.
DR OrthoDB; 519653at2759; -.
DR PhylomeDB; Q6P2P2; -.
DR TreeFam; TF315221; -.
DR BioCyc; MetaCyc:ENSG00000164169-MON; -.
DR BRENDA; 2.1.1.320; 2681.
DR PathwayCommons; Q6P2P2; -.
DR SignaLink; Q6P2P2; -.
DR BioGRID-ORCS; 90826; 22 hits in 1086 CRISPR screens.
DR ChiTaRS; PRMT9; human.
DR GenomeRNAi; 90826; -.
DR Pharos; Q6P2P2; Tbio.
DR PRO; PR:Q6P2P2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6P2P2; protein.
DR Bgee; ENSG00000164169; Expressed in secondary oocyte and 166 other tissues.
DR ExpressionAtlas; Q6P2P2; baseline and differential.
DR Genevisible; Q6P2P2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IBA:GO_Central.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11006; PTHR11006; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51678; SAM_MT_PRMT; 2.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Methyltransferase;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; TPR repeat;
KW Transferase.
FT CHAIN 1..845
FT /note="Protein arginine N-methyltransferase 9"
FT /id="PRO_0000325929"
FT REPEAT 25..58
FT /note="TPR 1"
FT REPEAT 67..100
FT /note="TPR 2"
FT REPEAT 101..134
FT /note="TPR 3"
FT DOMAIN 137..466
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 530..845
FT /note="SAM-dependent MTase PRMT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053972"
FT VARIANT 483
FT /note="S -> G (in dbSNP:rs17023638)"
FT /id="VAR_039954"
FT VARIANT 747
FT /note="C -> Y (in dbSNP:rs11557361)"
FT /id="VAR_039955"
FT MUTAGEN 182..185
FT /note="LDIG->AAAA: Loss of interaction with SF3B2;
FT Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:25737013"
FT MUTAGEN 258
FT /note="D->G: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:25979344"
FT MUTAGEN 260
FT /note="G->E: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:25979344"
FT MUTAGEN 431
FT /note="C->H: 8-fold increase in MMA production and almost
FT complete elimination of sDMA production."
FT /evidence="ECO:0000269|PubMed:27387499"
FT CONFLICT 504
FT /note="A -> P (in Ref. 4; AAH21250)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="E -> G (in Ref. 1; BAF85593)"
FT /evidence="ECO:0000305"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:7RBQ"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7RBQ"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6PDM"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:7RBQ"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 407..417
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6PDM"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 465..472
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 522..528
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 531..546
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 594..601
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 602..608
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 613..625
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:7T39"
FT STRAND 656..661
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 674..683
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 685..700
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 706..710
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 718..720
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 726..729
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 735..740
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 742..744
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 754..762
FT /evidence="ECO:0007829|PDB:7RBQ"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 770..776
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 781..797
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 811..822
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 827..835
FT /evidence="ECO:0007829|PDB:7RBQ"
FT STRAND 838..843
FT /evidence="ECO:0007829|PDB:7RBQ"
SQ SEQUENCE 845 AA; 94501 MW; 96C509E190D05A53 CRC64;
MSNSRPRSRR DAGGGAGAAG RDELVSRSLQ SAEHCLGVQD FGTAYAHYLL VLSLAPELKH
DVKETFQYTL FRWAEELDAL SRIQDLLGCY EQALELFPDD EVICNSMGEH LFRMGFRDEA
AGYFHKAVKL NPDFSDAKEN FYRVANWLVE RWHFIMLNDT KRNTIYNAAI QKAVCLGSKS
VLDIGAGTGI LSMFAKKAGA HSVYACELSK TMYELACDVV AANKMEAGIK LLHTKSLDIE
IPKHIPERVS LVVTETVDAG LFGEGIVESL IHAWEHLLLQ PKTKGESANC EKYGKVIPAS
AVIFGMAVEC AEIRRHHRVG IKDIAGIHLP TNVKFQSPAY SSVDTEETIE PYTTEKMSRV
PGGYLALTEC FEIMTVDFNN LQELKSLATK KPDKIGIPVI KEGILDAIMV WFVLQLDDEH
SLSTSPSEET CWEQAVYPVQ DLADYWIKPG DHVMMEVSCQ DCYLRIQSIS VLGLECEMDV
AKSFTQNKDL LSLGNEAELC SALANLQTSK PDAVEQTCIL ESTEIALLNN IPYHEGFKMA
MSKVLSSLTP EKLYQTMDTH CQNEMSSGTG QSNTVQNILE PFYVLDVSEG FSVLPVIAGT
LGQVKPYSSV EKDQHRIALD LISEANHFPK ETLEFWLRHV EDESAMLQRP KSDKLWSIII
LDVIEPSGLI QQEIMEKAAI SRCLLQSGGK IFPQYVLMFG LLVESQTLLE ENAVQGTERT
LGLNIAPFIN QFQVPIRVFL DLSSLPCIPL SKPVELLRLD LMTPYLNTSN REVKVYVCKS
GRLTAIPFWY HMYLDEEIRL DTSSEASHWK QAAVVLDNPI QVEMGEELVL SIQHHKSNVS
ITVKQ
