ANM7_DANRE
ID ANM7_DANRE Reviewed; 683 AA.
AC A2AV36; Q803G6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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; ORFNames=ch211-51l3.2;
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 1-682.
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q9NVM4}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}.
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=AAH44492.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AL929309; CAM14259.1; -; Genomic_DNA.
DR EMBL; BC044492; AAH44492.1; ALT_SEQ; mRNA.
DR RefSeq; NP_956797.2; NM_200503.2.
DR AlphaFoldDB; A2AV36; -.
DR SMR; A2AV36; -.
DR STRING; 7955.ENSDARP00000068099; -.
DR PaxDb; A2AV36; -.
DR PeptideAtlas; A2AV36; -.
DR Ensembl; ENSDART00000073609; ENSDARP00000068099; ENSDARG00000051902.
DR Ensembl; ENSDART00000183690; ENSDARP00000151596; ENSDARG00000116251.
DR GeneID; 393475; -.
DR KEGG; dre:393475; -.
DR CTD; 54496; -.
DR ZFIN; ZDB-GENE-040426-1560; prmt7.
DR eggNOG; KOG1501; Eukaryota.
DR GeneTree; ENSGT00940000156879; -.
DR HOGENOM; CLU_015180_0_0_1; -.
DR InParanoid; A2AV36; -.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; A2AV36; -.
DR TreeFam; TF315221; -.
DR BRENDA; 2.1.1.320; 928.
DR Reactome; R-DRE-3214858; RMTs methylate histone arginines.
DR PRO; PR:A2AV36; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000051902; Expressed in tail and 21 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS: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; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:ZFIN.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:ZFIN.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IMP:ZFIN.
DR GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; ISS: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 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Differentiation; Methyltransferase;
KW Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..683
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373904"
FT DOMAIN 14..341
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 353..677
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 CONFLICT 59
FT /note="V -> I (in Ref. 2; AAH44492)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="E -> K (in Ref. 2; AAH44492)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="I -> M (in Ref. 2; AAH44492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 76547 MW; 33AB7ED83B972589 CRC64;
MKTFCGRANP TTGALDWVEE SEEYDYHQEI ARSCYADMLH DKDRNEKYYE GIRAAVRRVK
ARGERPVVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA QAASCIVERN GFSDKIKIIN
KHSTEVTVGP DGDMQERANI LVTELFDTEL IGEGALPSYE HAHMHLVQTG CEAVPHRATI
YAQLVESDML WKWAQMRPID VDGHRLMPPG AVQECAGAPS VCDIQLSQVP TDAFTAISPV
CTMFSVDFSK PVSSAAQSYT VRFKSQTGGR AQVVLSWWDI DMDPEGNIVC TMAPSWSYAD
PHAYPWRDHW MQSVYFLPAE ENVSEGEELM LMVSHDDYSL WYSLTHSEQN DVRVAPFRPC
CTCQAHLVWT RPRFGELNDE QRTESYVSAL RSILKPDSVC LSVSDGSLLP VFAHLLGSKK
VFSLESSGMA KQVIEQVLHT NSLKDGVQLL GIRAEQLSLA DLDGNQISVL MGEPYFSTSL
LPWHSLFFWY CRTAVAQLLQ PDATILPRAA TLYAVAVEFQ DLWRIRFPCG TCEGFDVSPM
DEMIQRSLDF RESWEAEPHP LWEYPCRALT KPCPVMTFDF TQCVPEQPIS SDGAVPFTGR
GRCHGVALWM EYQLTDDISV SMGLTKAVSQ EGACEWNPHR KQGVFFFRSA KETSGDGRED
LSYSLTFEPH SGDIKMDFSI TES
