ANM8B_DANRE
ID ANM8B_DANRE Reviewed; 419 AA.
AC Q5RGQ2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein arginine N-methyltransferase 8-B {ECO:0000305};
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q9NR22};
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4;
DE AltName: Full=zfL3;
GN Name=prmt8b; Synonyms=prmt8; ORFNames=si:dkey-21h14.6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 74-419.
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION.
RX PubMed=15475159; DOI=10.1016/j.gene.2004.07.039;
RA Hung C.M., Li C.;
RT "Identification and phylogenetic analyses of the protein arginine
RT methyltransferase gene family in fish and ascidians.";
RL Gene 340:179-187(2004).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent and membrane-associated
CC arginine methyltransferase that can both catalyze the formation of
CC omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine
CC (aDMA). {ECO:0000250|UniProtKB:Q9NR22}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q9NR22};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC Evidence={ECO:0000250|UniProtKB:Q9NR22};
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:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000250|UniProtKB:Q9NR22};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC Evidence={ECO:0000250|UniProtKB:Q9NR22};
CC -!- SUBUNIT: Homodimer. Tetramer; individual homodimers associates to form
CC a homotetramer. Homooctamer; individual homodimers associates to form a
CC homooctamer and homooligomerization is required for proper localization
CC to the cell membrane. {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NR22};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q9NR22}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- DOMAIN: The N-terminal region (1-60) inhibits the arginine N-
CC methyltransferase activity. {ECO:0000250|UniProtKB:Q9NR22}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT8
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI62920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI62940.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI20944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX784029; CAI20944.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC162920; AAI62920.1; ALT_INIT; mRNA.
DR EMBL; BC162940; AAI62940.1; ALT_INIT; mRNA.
DR RefSeq; NP_001038507.1; NM_001045042.1.
DR RefSeq; XP_005164712.1; XM_005164655.3.
DR AlphaFoldDB; Q5RGQ2; -.
DR SMR; Q5RGQ2; -.
DR STRING; 7955.ENSDARP00000059488; -.
DR PaxDb; Q5RGQ2; -.
DR PRIDE; Q5RGQ2; -.
DR Ensembl; ENSDART00000059489; ENSDARP00000059488; ENSDARG00000045760.
DR GeneID; 564110; -.
DR KEGG; dre:564110; -.
DR CTD; 564110; -.
DR ZFIN; ZDB-GENE-030131-7791; prmt8b.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000155867; -.
DR HOGENOM; CLU_017375_1_1_1; -.
DR InParanoid; Q5RGQ2; -.
DR OMA; CHNSIAS; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q5RGQ2; -.
DR TreeFam; TF300608; -.
DR PRO; PR:Q5RGQ2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000045760; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; Q5RGQ2; baseline.
DR GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016273; F:arginine N-methyltransferase activity; IDA:ZFIN.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:ZFIN.
DR GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:ZFIN.
DR GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR GO; GO:0030917; P:midbrain-hindbrain boundary development; IMP:ZFIN.
DR GO; GO:0048666; P:neuron development; IMP:ZFIN.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Methyltransferase;
KW Myristate; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT CHAIN 2..419
FT /note="Protein arginine N-methyltransferase 8-B"
FT /id="PRO_0000378153"
FT DOMAIN 98..402
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT ACT_SITE 219
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 144..147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT MOD_RES 83
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT MOD_RES 98
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR22"
SQ SEQUENCE 419 AA; 48222 MW; 63111344E2BC7D17 CRC64;
MGLRHSSRCL LLRRKMAEAE STEQQQQKHK QPQHQQQQSI SSIPSSQSLQ PSPLPKPVTS
VHHVPPHPPH TPHVSALSAC PGRGKMAKLL NPEEMTSRDY YFDSYAHFGI HEEMLKDEVR
TLTYRNSMYH NKHIFKDKIV LDVGSGTGIL SMFAAKAGAK HVYGIECSSI SEYSEKIIKS
NHLDSVITIL KGKVEETELP VDQVDIIISE WMGYCLFYES MLNTVIYARD KWLKPGGFMF
PDRATLYVVA IEDRQYKDFK IHWWENVYGF DMTCIRNVAM MEPLVDIVDP KQVVTNSCLV
KEVDIYTVKT EDLSFTSAFC LQIQRNDYVH ALVTYFNIEF TKCHKKTGFS TAPDAPSTHW
KQTVFYLEDY LTVRRGEEIL GSITVRPNEN NERDLDFTFE LDFKGQLCDA AISHDYKMR
