ID   ANM5_MOUSE              Reviewed;         637 AA.
AC   Q8CIG8; Q3TNN1; Q9QZS9;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 54.
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;
DE   AltName: Full=Jak-binding protein 1;
GN   Name=Prmt5; Synonyms=Jbp1, Skb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-637.
RX   MEDLINE=20002682; PubMed=10531356; DOI=10.1074/jbc.274.44.31531;
RA   Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L.,
RA   Pestka S.;
RT   "The human homologue of the yeast proteins Skb1 and Hsl7p interacts
RT   with Jak kinases and contains protein methyltransferase activity.";
RL   J. Biol. Chem. 274:31531-31542(1999).
RN   [4]
RP   METHYLATION OF HISTONE H3.
RX   PubMed=15485929; DOI=10.1128/MCB.24.21.9630-9645.2004;
RA   Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
RT   "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and
RT   negatively regulates expression of ST7 and NM23 tumor suppressor
RT   genes.";
RL   Mol. Cell. Biol. 24:9630-9645(2004).
RN   [5]
RP   INTERACTION WITH PRDM1.
RX   PubMed=16699504; DOI=10.1038/ncb1413;
RA   Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
RA   Kouzarides T., Surani M.A.;
RT   "Blimp1 associates with Prmt5 and directs histone arginine methylation
RT   in mouse germ cells.";
RL   Nat. Cell Biol. 8:623-630(2006).
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.
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. Component
CC       of the methylosome, a 20S complex containing at least pICLn,
CC       PRMT5/SKB1 and MEP50. Component of a high molecular weight E2F-
CC       pocket protein complex, CERC (cyclin E1 repressor complex). Also
CC       interacts with Sm proteins, JAK2 and SSTR1. Associates with
CC       SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4.
CC       Interacts with PRMT7 and SNRPD3. Interacts with COPR5; promoting
CC       its recruitment on histone H4 (By similarity). Interacts with
CC       PRDM1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- PTM: Disulfide bonds and non-covalent association mediate
CC       homooligomers formation (By similarity).
CC   -!- SIMILARITY: Belongs to the protein arginine N-methyltransferase
CC       family.
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DR   EMBL; AK132414; BAE21155.1; -; mRNA.
DR   EMBL; AK165165; BAE38057.1; -; mRNA.
DR   EMBL; BC023905; AAH23905.1; -; mRNA.
DR   EMBL; AF167573; AAF04503.1; -; mRNA.
DR   IPI; IPI00229845; -.
DR   RefSeq; NP_038796.2; -.
DR   UniGene; Mm.196585; -.
DR   PhosphoSite; Q8CIG8; -.
DR   PRIDE; Q8CIG8; -.
DR   Ensembl; ENSMUSG00000023110; Mus musculus.
DR   GeneID; 27374; -.
DR   KEGG; mmu:27374; -.
DR   MGI; MGI:1351645; Prmt5.
DR   HOVERGEN; Q8CIG8; -.
DR   BRENDA; 2.1.1.125; 244.
DR   ArrayExpress; Q8CIG8; -.
DR   Bgee; Q8CIG8; -.
DR   CleanEx; MM_PRMT5; -.
DR   GermOnline; ENSMUSG00000023110; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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   1: Evidence at protein 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_0000212344.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   CONFLICT    169    169       A -> E (in Ref. 1; BAE21155/BAE38057).
FT   CONFLICT    376    376       L -> F (in Ref. 3; AAF04503).
SQ   SEQUENCE   637 AA;  72680 MW;  E8014CA172B30543 CRC64;
     MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFIQEPAK
     NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR RNSEAAMLQE LNFGAYLGLP
     AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDVIAN APTTHTEEYS
     GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK
     KGFPVLSKVQ QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
     AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKETNVQV
     LMVLGAGRGP LVNASLRAAK QAERRIRLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM
     REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL
     YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPKPCFT FSHPNRDPMI DNNRYCTLEF
     PVEVNTVLHG FAGYFETVLY RDITLSIRPE THSPGMFSWF PIFFPIKQPI TVHEGQNICV
     RFWRCSNSKK VWYEWAVTAP VCSSIHNPTG RSYTIGL
//