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   27-MAR-2024, entry version 169.
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 7.5 and 8.0. {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; 33.
DR   IntAct; Q6P2P2; 13.
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; 9606-ENSP00000314396; -.
DR   PeptideAtlas; Q6P2P2; -.
DR   ProteomicsDB; 3704; -.
DR   ProteomicsDB; 66914; -. [Q6P2P2-1]
DR   ProteomicsDB; 66915; -. [Q6P2P2-2]
DR   Pumba; Q6P2P2; -.
DR   Antibodypedia; 49190; 146 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   AGR; HGNC:25099; -.
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; NILEPFY; -.
DR   OrthoDB; 2879920at2759; -.
DR   PhylomeDB; Q6P2P2; -.
DR   TreeFam; TF315221; -.
DR   BioCyc; MetaCyc:ENSG00000164169-MONOMER; -.
DR   BRENDA; 2.1.1.320; 2681.
DR   PathwayCommons; Q6P2P2; -.
DR   SignaLink; Q6P2P2; -.
DR   BioGRID-ORCS; 90826; 26 hits in 1165 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 168 other cell types or tissues.
DR   ExpressionAtlas; Q6P2P2; baseline and differential.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11006:SF4; PROTEIN ARGININE N-METHYLTRANSFERASE 7; 1.
DR   Pfam; PF06325; PrmA; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 2.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   Genevisible; Q6P2P2; HS.
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
//