ANM7_CHICK
ID ANM7_CHICK Reviewed; 689 AA.
AC Q5ZIB9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=RCJMB04_28e13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ720865; CAG32524.1; -; mRNA.
DR RefSeq; NP_001005831.1; NM_001005831.1.
DR AlphaFoldDB; Q5ZIB9; -.
DR SMR; Q5ZIB9; -.
DR STRING; 9031.ENSGALP00000001157; -.
DR PaxDb; Q5ZIB9; -.
DR PRIDE; Q5ZIB9; -.
DR GeneID; 415620; -.
DR KEGG; gga:415620; -.
DR CTD; 54496; -.
DR VEuPathDB; HostDB:geneid_415620; -.
DR eggNOG; KOG1501; Eukaryota.
DR InParanoid; Q5ZIB9; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; Q5ZIB9; -.
DR PRO; PR:Q5ZIB9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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); ISS: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; ISS:HGNC-UCL.
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; ISS:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; ISS: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; 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..689
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373903"
FT DOMAIN 14..344
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 359..685
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"
SQ SEQUENCE 689 AA; 78071 MW; E924B30B918F4109 CRC64;
MKTFCGRANP TTGSLEWVEE DEDYDYHQEI ARSRYADMLH DKDRNMKYYQ GIRAAVSRVK
GRGEKAIVLD IGTGTGLLSM MAASAGADFC YAVEVFKPMA NAAVKIVEKN GFGDKIKVIN
KHSTEVTVGP DGDMQCRANI LVTELFDTEL IGEGALPTYE HAHKYLVQEG CEAVPHRATV
YVQLVESKRM WSWNKLFPVH VEAEDGEKII VSPSEMENCP GVPSVCDIQL NQMPSSDFTI
LSDVVTMFSV DFSKPVRSAS TCYRAQLDPV KSGKAQIVLS WWDIDMDPSG TINCTMAPYW
VKPMSAFQWR DHWMQCVYFL PKEEQVLQGE KVHLTACRDE YSVWYTLQKA REEDESKADA
RVESPVCRCQ AHLLWNRPRF GELNDQNRTR QYIKSLMSVL RTDSVCLCIS DGSLLPVLAH
YLGAEQVFTL ENSAVSCSVM KKFFKANHLE DKIKIVEARP ELLTSSHLEE KKISVLVGEP
FFTTSLLPWH NLYFWYARTA VTEHLASDVT VLPQSAALHM MIVEFQDLWR IRSPCGTCEG
FDVQTMDDMI KNSLNFRESK EAEPHPLWEY PCKSLSNPQE VLLFDFRKTV PQHCLSTEGS
VNLLRKGKSH GAVLWMEYHL TADISVSTGL MQISNEKGNC EWNPHCKQAV YFFSSVIESE
TLADVPTAVT YAIKFDTKTG EIAMDFKLL
