ANM9_MOUSE
ID ANM9_MOUSE Reviewed; 846 AA.
AC Q3U3W5; D3YU52; Q8BLF8; Q8BLG1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein arginine N-methyltransferase 9;
DE AltName: Full=Protein arginine N-methyltransferase 10;
DE EC=2.1.1.320 {ECO:0000250|UniProtKB:Q6P2P2};
GN Name=Prmt9; Synonyms=Prmt10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA). Specifically mediates the symmetrical
CC dimethylation of SF3B2. Involved in the regulation of alternative
CC splicing of pre-mRNA. {ECO:0000250|UniProtKB:Q6P2P2}.
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:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000250|UniProtKB:Q6P2P2};
CC -!- SUBUNIT: Found in a complex with PRMT9, SF3B2 and SF3B4. Interacts with
CC SF3B2. {ECO:0000250|UniProtKB:Q6P2P2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6P2P2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U3W5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U3W5-2; Sequence=VSP_032488, VSP_032489;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- CAUTION: This protein should not be confused with Fbxo11 (AC Q7TPD1)
CC that was initially erroneously named Prmt9. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32307.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK045296; BAC32300.1; -; mRNA.
DR EMBL; AK045315; BAC32307.1; ALT_FRAME; mRNA.
DR EMBL; AK154546; BAE32670.1; -; mRNA.
DR EMBL; AC109139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40394.1; -. [Q3U3W5-1]
DR RefSeq; NP_001074709.1; NM_001081240.3.
DR AlphaFoldDB; Q3U3W5; -.
DR SMR; Q3U3W5; -.
DR IntAct; Q3U3W5; 1.
DR MINT; Q3U3W5; -.
DR STRING; 10090.ENSMUSP00000050181; -.
DR iPTMnet; Q3U3W5; -.
DR PhosphoSitePlus; Q3U3W5; -.
DR EPD; Q3U3W5; -.
DR MaxQB; Q3U3W5; -.
DR PaxDb; Q3U3W5; -.
DR PeptideAtlas; Q3U3W5; -.
DR PRIDE; Q3U3W5; -.
DR ProteomicsDB; 281991; -. [Q3U3W5-1]
DR ProteomicsDB; 281992; -. [Q3U3W5-2]
DR Antibodypedia; 49190; 136 antibodies from 19 providers.
DR DNASU; 102182; -.
DR Ensembl; ENSMUST00000118622; ENSMUSP00000112692; ENSMUSG00000037134. [Q3U3W5-1]
DR GeneID; 102182; -.
DR KEGG; mmu:102182; -.
DR UCSC; uc009mhp.1; mouse. [Q3U3W5-2]
DR UCSC; uc012ggg.1; mouse. [Q3U3W5-1]
DR CTD; 90826; -.
DR MGI; MGI:2142651; Prmt9.
DR VEuPathDB; HostDB:ENSMUSG00000037134; -.
DR eggNOG; KOG1501; Eukaryota.
DR GeneTree; ENSGT00940000158472; -.
DR InParanoid; Q3U3W5; -.
DR OrthoDB; 519653at2759; -.
DR PhylomeDB; Q3U3W5; -.
DR BioGRID-ORCS; 102182; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Prmt9; mouse.
DR PRO; PR:Q3U3W5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3U3W5; protein.
DR Bgee; ENSMUSG00000037134; Expressed in superior cervical ganglion and 222 other tissues.
DR ExpressionAtlas; Q3U3W5; baseline and differential.
DR Genevisible; Q3U3W5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; 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:0006397; P:mRNA processing; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11006; PTHR11006; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51678; SAM_MT_PRMT; 2.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Methyltransferase; Reference proteome;
KW Repeat; S-adenosyl-L-methionine; TPR repeat; Transferase.
FT CHAIN 1..846
FT /note="Protein arginine N-methyltransferase 9"
FT /id="PRO_0000325930"
FT REPEAT 25..58
FT /note="TPR 1"
FT REPEAT 67..100
FT /note="TPR 2"
FT REPEAT 101..134
FT /note="TPR 3"
FT DOMAIN 137..466
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 530..846
FT /note="SAM-dependent MTase PRMT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT VAR_SEQ 249..257
FT /note="LSLVVTETV -> CVYKSLKTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032488"
FT VAR_SEQ 258..846
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032489"
FT CONFLICT 249
FT /note="L -> V (in Ref. 1; BAC32300/BAE32670)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="E -> G (in Ref. 1; BAC32307)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="Q -> H (in Ref. 1; BAE32670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 94220 MW; DFFAE1B0D3116049 CRC64;
MPNSRPRPRR GAGGGAGAAG RDRLVARSLQ SAEHCLGDQD FGTAYAHYLL VLSLAPELKD
DVKETFQYTL FKWAEELHAL SRIQDLLGCY EQALELFPDD EVICNSMGEH LFRMGFRDEA
AGYFHKAVKL NPDFNDAKEN FYRVANWLVE RWHFIMLNDT RRNMVYNAAI QKAVCLGSRT
VLDIGTGTGI LSMFAKKAGA QSVYACELSK TMYELACDVV AANKMENGIK LLHMKSLDIE
IPKHIPERLS LVVTETVDAG VFGEGIVESL IHAWEHLLLQ PKTKEENGNC GKYGKVIPAG
AVIFGMAVEC AEIRRHHRVG AKDIAGIHLP TNVKFQSPAY TSVDTEETVE PYTTEKMSGI
PGGYLPLTEC FQIMKVDFNN LQELKSLATK KPHSLNVPAI KEGVLDAIMV WFVLQLDDEY
SLSTSPSEET CWEQAVYPVQ ALEDYCIQPG DRVTMEASCH DCYLRIQGIS ILHLEHEMEV
MKGFTKSKDL LSLGNEAELC SALANLQTSR PEALEQTCML EPTEIALLNN IPYHEGFKTA
MRKVLSSLAP ELLWQPMDTH CQYMEMNSGS GQSDAAPSTA DPFYVLDVSE GFSLLPILAG
TLGHVKPYSS VEKDQHCIAL DLIAEANHFP KETLEFWLRH IEDEAAVLQR PKSDKLWSII
ILDVIEPSGL IQQELMEKAA ISRCLLQSGG KIFPQYVLMF GMLVESQTLV EESAVQGTEH
TLGLNIAPFI NQFQVPIRVC LDLSSLPCVP LSQPVELLRL DLMTPYLNTS NKEVKVRVCR
SGRVTAVPFW FHLCLDDEVR LDTSGEASHW KQAAVVLDNP IQVQAGEELV LSVEHHKSNV
SIAVKP
