ANM7_MOUSE
ID ANM7_MOUSE Reviewed; 692 AA.
AC Q922X9; Q3TRZ6; Q69Z62; Q6B955; Q6PG80;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein arginine N-methyltransferase 7;
DE EC=2.1.1.321 {ECO:0000250|UniProtKB:Q9NVM4};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT7;
DE AltName: Full=[Myelin basic protein]-arginine N-methyltransferase PRMT7;
GN Name=Prmt7; Synonyms=Kiaa1933;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=16690984; DOI=10.1165/rcmb.2006-0097oc;
RA Yildirim A.O., Bulau P., Zakrzewicz D., Kitowska K.E., Weissmann N.,
RA Grimminger F., Morty R.E., Eickelberg O.;
RT "Increased protein arginine methylation in chronic hypoxia: role of protein
RT arginine methyltransferases.";
RL Am. J. Respir. Cell Mol. Biol. 35:436-443(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Epididymis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 DEVELOPMENTAL STAGE.
RX PubMed=15699352; DOI=10.1073/pnas.0409786102;
RA Zheng Z., Schmidt-Ott K.M., Chua S., Foster K.A., Frankel R.Z.,
RA Pavlidis P., Barasch J., D'Agati V.D., Gharavi A.G.;
RT "A Mendelian locus on chromosome 16 determines susceptibility to
RT doxorubicin nephropathy in the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2502-2507(2005).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INTERACTION WITH CTCFL.
RX PubMed=17048991; DOI=10.1371/journal.pbio.0040355;
RA Jelinic P., Stehle J.-C., Shaw P.;
RT "The testis-specific factor CTCFL cooperates with the protein
RT methyltransferase PRMT7 in H19 imprinting control region methylation.";
RL PLoS Biol. 4:E355-E355(2006).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=18449859; DOI=10.1002/elps.200700738;
RA Buhr N., Carapito C., Schaeffer C., Kieffer E., Van Dorsselaer A.,
RA Viville S.;
RT "Nuclear proteome analysis of undifferentiated mouse embryonic stem and
RT germ cells.";
RL Electrophoresis 29:2381-2390(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-32, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=26437029; DOI=10.1038/ng.3410;
RG DDD study;
RA Akawi N., McRae J., Ansari M., Balasubramanian M., Blyth M., Brady A.F.,
RA Clayton S., Cole T., Deshpande C., Fitzgerald T.W., Foulds N., Francis R.,
RA Gabriel G., Gerety S.S., Goodship J., Hobson E., Jones W.D., Joss S.,
RA King D., Klena N., Kumar A., Lees M., Lelliott C., Lord J., McMullan D.,
RA O'Regan M., Osio D., Piombo V., Prigmore E., Rajan D., Rosser E.,
RA Sifrim A., Smith A., Swaminathan G.J., Turnpenny P., Whitworth J.,
RA Wright C.F., Firth H.V., Barrett J.C., Lo C.W., FitzPatrick D.R.,
RA Hurles M.E.;
RT "Discovery of four recessive developmental disorders using probabilistic
RT genotype and phenotype matching among 4,125 families.";
RL Nat. Genet. 47:1363-1369(2015).
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA), with a preference for the formation of MMA.
CC Specifically mediates the symmetrical dimethylation of arginine
CC residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm
CC D3 (SNRPD3); such methylation being required for the assembly and
CC biogenesis of snRNP core particles. Specifically mediates the symmetric
CC dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in
CC gene imprinting by being recruited by CTCFL at the H19 imprinted
CC control region (ICR) and methylating histone H4 to form H4R3me2s,
CC possibly leading to recruit DNA methyltransferases at these sites. May
CC also play a role in embryonic stem cell (ESC) pluripotency. Also able
CC to mediate the arginine methylation of histone H2A and myelin basic
CC protein (MBP) in vitro; the relevance of such results is however
CC unclear in vivo (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:17048991}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65280; EC=2.1.1.321;
CC Evidence={ECO:0000250|UniProtKB:Q9NVM4};
CC -!- SUBUNIT: Homodimer and heterodimer. Interacts with PRMT5 and SNRPD3 (By
CC similarity). Interacts with CTCFL. {ECO:0000250,
CC ECO:0000269|PubMed:17048991}.
CC -!- INTERACTION:
CC Q922X9; A2APF3: Ctcfl; NbExp=3; IntAct=EBI-15606508, EBI-11566304;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Present in undifferentiated embryonic stem and
CC germ cells; expression is lost when cells differentiate. In the
CC developing testis, it is expressed at all stages. Present in all cells
CC within the developing tubule, including gonocytes and spermatogonia (at
CC protein level). It the developing kidney, it is confined to the
CC nephrogenic zone in the cortical region, where the tips of the ureteric
CC bud induce de novo formation of epithelia in the metanephric mesenchyme
CC and early glomeruli. Expression is around 8-fold lower in adult
CC kidneys. {ECO:0000269|PubMed:15699352, ECO:0000269|PubMed:17048991,
CC ECO:0000269|PubMed:18449859}.
CC -!- DISRUPTION PHENOTYPE: Mutants, shortly after birth, display significant
CC reduced body size, reduced weight and shortened fifth metatarsals. They
CC are subviable with about 45% of the expected number of mutant pups at
CC P14. Surviving adult mice exhibit increased fat mass, reduced length
CC and limb abnormalities. They also have reduced bone mineral content and
CC density. Knockout mice show sexually dimorphic phenotypes, including
CC changes in bone mineral content, bone mineral density and fifth
CC metacarpal length that are only significant in females.
CC {ECO:0000269|PubMed:26437029}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT7
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32582.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY673972; AAT76979.1; -; mRNA.
DR EMBL; AK173304; BAD32582.1; ALT_INIT; mRNA.
DR EMBL; AK154255; BAE32467.1; -; mRNA.
DR EMBL; AK162376; BAE36880.1; -; mRNA.
DR EMBL; CH466525; EDL11358.1; -; Genomic_DNA.
DR EMBL; BC006705; AAH06705.1; -; mRNA.
DR EMBL; BC057177; AAH57177.1; -; mRNA.
DR CCDS; CCDS22633.1; -.
DR RefSeq; NP_663379.1; NM_145404.1.
DR PDB; 4C4A; X-ray; 1.70 A; A=1-692.
DR PDB; 6OGN; X-ray; 2.40 A; A=1-692.
DR PDBsum; 4C4A; -.
DR PDBsum; 6OGN; -.
DR AlphaFoldDB; Q922X9; -.
DR SMR; Q922X9; -.
DR BioGRID; 229540; 1.
DR DIP; DIP-29210N; -.
DR IntAct; Q922X9; 1.
DR STRING; 10090.ENSMUSP00000071521; -.
DR iPTMnet; Q922X9; -.
DR PhosphoSitePlus; Q922X9; -.
DR EPD; Q922X9; -.
DR MaxQB; Q922X9; -.
DR PaxDb; Q922X9; -.
DR PeptideAtlas; Q922X9; -.
DR PRIDE; Q922X9; -.
DR ProteomicsDB; 296252; -.
DR Antibodypedia; 29775; 255 antibodies from 33 providers.
DR DNASU; 214572; -.
DR Ensembl; ENSMUST00000071592; ENSMUSP00000071521; ENSMUSG00000060098.
DR GeneID; 214572; -.
DR KEGG; mmu:214572; -.
DR UCSC; uc009nfu.1; mouse.
DR CTD; 54496; -.
DR MGI; MGI:2384879; Prmt7.
DR VEuPathDB; HostDB:ENSMUSG00000060098; -.
DR eggNOG; KOG1501; Eukaryota.
DR GeneTree; ENSGT00940000156879; -.
DR HOGENOM; CLU_015180_0_0_1; -.
DR InParanoid; Q922X9; -.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; Q922X9; -.
DR TreeFam; TF315221; -.
DR BRENDA; 2.1.1.321; 3474.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR BioGRID-ORCS; 214572; 10 hits in 79 CRISPR screens.
DR ChiTaRS; Prmt7; mouse.
DR PRO; PR:Q922X9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q922X9; protein.
DR Bgee; ENSMUSG00000060098; Expressed in spermatid and 247 other tissues.
DR ExpressionAtlas; Q922X9; baseline and differential.
DR Genevisible; Q922X9; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); IDA:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IDA:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; IDA:UniProtKB.
DR GO; GO:0016571; P:histone methylation; ISS:HGNC-UCL.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISS:HGNC-UCL.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IDA:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR014644; MeTrfase_PRMT7.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51678; SAM_MT_PRMT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Cytoplasm; Differentiation; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..692
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000212336"
FT DOMAIN 14..345
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 358..684
FT /note="SAM-dependent MTase PRMT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 37
FT /note="D -> E (in Ref. 5; AAH57177)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="V -> G (in Ref. 3; BAE36880)"
FT /evidence="ECO:0000305"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 42..61
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:4C4A"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4C4A"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 273..287
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 316..327
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:6OGN"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 414..420
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:4C4A"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 487..491
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 492..499
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 504..512
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 514..526
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 527..531
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 543..553
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:4C4A"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 594..602
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 610..620
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 623..630
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 667..674
FT /evidence="ECO:0007829|PDB:4C4A"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:4C4A"
FT STRAND 681..688
FT /evidence="ECO:0007829|PDB:4C4A"
SQ SEQUENCE 692 AA; 78301 MW; D61A9500956BF02D CRC64;
MKVFCGRANP TTGSLEWLEE DEHYDYHQEI ARSSYADMLH DKDRNIKYYQ GIRAAVSRVK
DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA EAAVKIVERN GFSDKIKVIN
KHSTEVTVGP DGDLPCRANI LITELFDTEL IGEGALPSYE HAHKHLVQED CEAVPHRATV
YAQLVESRRM WSWNKLFPVR VRTSLGEQVI VPPSELERCP GAPSVCDIQL NQVSPADFTV
LSDVLPMFSV DFSKQVSSSA ACHSRQFVPL ASGQAQVVLS WWDIEMDPEG KIKCTMAPFW
AQTDPQELQW RDHWMQCVYF LPQEEPVVQG SPRCLVAHHD DYCVWYSLQR TSPDENDSAY
QVRPVCDCQA HLLWNRPRFG EINDQDRTDH YAQALRTVLL PGSVCLCVSD GSLLSMLAHH
LGAEQVFTVE SSVASYRLMK RIFKVNHLED KISVINKRPE LLTAADLEGK KVSLLLGEPF
FTTSLLPWHN LYFWYVRTSV DQHLAPGAVV MPQAASLHAV IVEFRDLWRI RSPCGDCEGF
DVHIMDDMIK HSLDFRESRE AEPHPLWEYP CRSLSKPQEI LTFDFQQPIP QQPMQSKGTM
ELTRPGKSHG AVLWMEYQLT PDSTISTGLI NPAEDKGDCC WNPHCKQAVY FLSTTLDLRV
PLNGPRSVSY VVEFHPLTGD ITMEFRLADT LS
