ID   ANM5_BOVIN              Reviewed;         637 AA.
AC   A7YW45;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Protein arginine N-methyltransferase 5;
DE            EC=2.1.1.-;
DE   AltName: Full=Histone-arginine N-methyltransferase PRMT5;
DE            EC=2.1.1.125;
DE   AltName: Full=Shk1 kinase-binding protein 1 homolog;
DE            Short=SKB1 homolog;
GN   Name=PRMT5; Synonyms=SKB1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) 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
CC       MMA. Specifically mediates the symmetrical dimethylation of
CC       arginine residues in the small nuclear ribonucleoproteins Sm D1
CC       (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for
CC       the assembly and biogenesis of snRNP core particles. Methylates
CC       SUPT5H. Mono- and dimethylates arginine residues of myelin basic
CC       protein (MBP) in vitro. Plays a role in the assembly of snRNP core
CC       particles. May play a role in cytokine-activated transduction
CC       pathways. Negatively regulates cyclin E1 promoter activity and
CC       cellular proliferation. May regulate the SUPT5H transcriptional
CC       elongation properties. May be part of a pathway that is connected
CC       to a chloride current, possibly through cytoskeletal
CC       rearrangement. Methylates histone H2A and H4 'Arg-3' during germ
CC       cell development. Methylates histone H3 'Arg-8', which may repress
CC       transcription (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone-arginine =
CC       S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine.
CC   -!- SUBUNIT: Forms, at least, homodimers and homotetramers. Interacts
CC       with PRDM1 (By similarity). Component of the methylosome, a 20S
CC       complex containing at least pICLn, PRMT1/SKB1 and MEP50. Component
CC       of a high molecular weight E2F-pocket protein complex, CERC
CC       (cyclin E1 repressor complex). Also interacts with Sm proteins,
CC       JAK2, SSTR1 and SUPT5H. Associates with SWI/SNF remodeling
CC       complexes containing SMARCA2 and SMARCA4. Interacts with PRMT7 and
CC       SNRPD3. Interacts with COPR5; promoting its recruitment on histone
CC       H4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- PTM: Disulfide bonds and non-covalent association mediate
CC       homooligomer formation (By similarity).
CC   -!- SIMILARITY: Belongs to the protein arginine N-methyltransferase
CC       family.
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DR   EMBL; BC134449; AAI34450.1; -; mRNA.
DR   IPI; IPI00868673; -.
DR   RefSeq; NP_001098844.1; -.
DR   UniGene; Bt.16112; -.
DR   Ensembl; ENSBTAG00000010890; Bos taurus.
DR   GeneID; 515594; -.
DR   KEGG; bta:515594; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IEA:EC.
DR   GO; GO:0035243; F:protein-arginine omega-N symmetric methyltr...; ISS:UniProtKB.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0000387; P:spliceosomal snRNP biogenesis; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007857; Skb1_MeTrfase.
DR   PANTHER; PTHR10738; Skb1_mtfrase; 1.
DR   Pfam; PF05185; PRMT5; 1.
DR   PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chromatin regulator; Cytoplasm; Disulfide bond;
KW   Methyltransferase; Nucleus; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    637       Protein arginine N-methyltransferase 5.
FT                                /FTId=PRO_0000330891.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   637 AA;  72629 MW;  08E7EBA71410809C CRC64;
     MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFTQEPAK
     SRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR RNSEAAMLQE LNFGAYLGLP
     AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDIIEN APTSHTEEYS
     GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK
     KGFPVLSKMH QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
     AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKDTNIQV
     LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM
     REWVAPEKAD IIVSELLGSF ADNELSPESL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL
     YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF
     PVEVNTVLHG FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV
     RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL
//