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Protein

Protein arginine N-methyltransferase 7

Gene

Prmt7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo (By similarity).By similarity1 Publication

Catalytic activityi

S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-arginine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei144By similarity1
Active sitei153By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.125. 3474.
ReactomeiR-MMU-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 7 (EC:2.1.1.321By similarity)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT7
[Myelin basic protein]-arginine N-methyltransferase PRMT7
Gene namesi
Name:Prmt7
Synonyms:Kiaa1933
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2384879. Prmt7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutants, shortly after birth, display significant reduced body size, reduced weight and shortened fifth metatarsals. They are subviable with about 45% of the expected number of expected mutant pups ar P14. Surviving adult mice exhibit increased fat mass, reduced length and limb anormalities. They also have reduced bone mineral content and density. Knockout mice show sexually dimorphic phenotypes, including changes in bone mineral content, bone mineral density and fifth metacarpal length that are only significant in females.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123361 – 692Protein arginine N-methyltransferase 7Add BLAST692

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Omega-N-methylarginineCombined sources1

Keywords - PTMi

Methylation

Proteomic databases

EPDiQ922X9.
MaxQBiQ922X9.
PaxDbiQ922X9.
PeptideAtlasiQ922X9.
PRIDEiQ922X9.

PTM databases

iPTMnetiQ922X9.
PhosphoSitePlusiQ922X9.

Expressioni

Developmental stagei

Present in undifferentiated embryonic stem and germ cells; expression is lost when cells differentiate. In the developing testis, it is expressed at all stages. Present in all cells within the developing tubule, including gonocytes and spermatogonia (at protein level). It the developing kidney, it is confined to the nephrogenic zone in the cortical region, where the tips of the ureteric bud induce de novo formation of epithelia in the metanephric mesenchyme and early glomeruli. Expression is around 8-fold lower in adult kidneys.3 Publications

Gene expression databases

BgeeiENSMUSG00000060098.
CleanExiMM_PRMT7.
ExpressionAtlasiQ922X9. baseline and differential.
GenevisibleiQ922X9. MM.

Interactioni

Subunit structurei

Homodimer and heterodimer. Interacts with PRMT5 and SNRPD3 (By similarity). Interacts with CTCFL.By similarity1 Publication

Protein-protein interaction databases

BioGridi229540. 1 interactor.
DIPiDIP-29210N.
STRINGi10090.ENSMUSP00000071521.

Structurei

Secondary structure

1692
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 31Combined sources4
Helixi35 – 39Combined sources5
Helixi42 – 61Combined sources20
Beta strandi67 – 72Combined sources6
Helixi77 – 85Combined sources9
Beta strandi88 – 93Combined sources6
Helixi97 – 109Combined sources13
Turni113 – 115Combined sources3
Beta strandi116 – 119Combined sources4
Helixi123 – 125Combined sources3
Beta strandi132 – 136Combined sources5
Beta strandi138 – 143Combined sources6
Helixi155 – 165Combined sources11
Beta strandi167 – 175Combined sources9
Beta strandi177 – 186Combined sources10
Helixi188 – 191Combined sources4
Turni192 – 194Combined sources3
Beta strandi199 – 203Combined sources5
Beta strandi206 – 210Combined sources5
Helixi214 – 218Combined sources5
Beta strandi226 – 228Combined sources3
Helixi230 – 232Combined sources3
Helixi235 – 237Combined sources3
Beta strandi245 – 251Combined sources7
Beta strandi261 – 267Combined sources7
Beta strandi273 – 287Combined sources15
Beta strandi292 – 295Combined sources4
Helixi299 – 301Combined sources3
Helixi305 – 307Combined sources3
Beta strandi312 – 314Combined sources3
Beta strandi316 – 327Combined sources12
Beta strandi333 – 339Combined sources7
Beta strandi344 – 348Combined sources5
Helixi370 – 373Combined sources4
Helixi376 – 382Combined sources7
Helixi385 – 398Combined sources14
Beta strandi404 – 409Combined sources6
Helixi414 – 420Combined sources7
Beta strandi424 – 429Combined sources6
Helixi433 – 445Combined sources13
Turni449 – 451Combined sources3
Beta strandi452 – 455Combined sources4
Helixi459 – 461Combined sources3
Helixi465 – 467Combined sources3
Beta strandi472 – 476Combined sources5
Helixi487 – 491Combined sources5
Helixi492 – 499Combined sources8
Helixi501 – 503Combined sources3
Beta strandi504 – 512Combined sources9
Beta strandi514 – 526Combined sources13
Helixi527 – 531Combined sources5
Beta strandi535 – 537Combined sources3
Helixi543 – 553Combined sources11
Beta strandi555 – 558Combined sources4
Beta strandi562 – 564Combined sources3
Helixi566 – 568Combined sources3
Beta strandi571 – 575Combined sources5
Beta strandi578 – 584Combined sources7
Beta strandi594 – 602Combined sources9
Beta strandi610 – 620Combined sources11
Beta strandi623 – 630Combined sources8
Beta strandi647 – 651Combined sources5
Beta strandi667 – 674Combined sources8
Turni676 – 678Combined sources3
Beta strandi681 – 688Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C4AX-ray1.70A1-692[»]
ProteinModelPortaliQ922X9.
SMRiQ922X9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 345SAM-dependent MTase PRMT-type 1PROSITE-ProRule annotationAdd BLAST332
Domaini358 – 684SAM-dependent MTase PRMT-type 2PROSITE-ProRule annotationAdd BLAST327

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.PROSITE-ProRule annotation
Contains 2 SAM-dependent MTase PRMT-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410INRX. Eukaryota.
COG0500. LUCA.
GeneTreeiENSGT00860000133873.
HOGENOMiHOG000033951.
HOVERGENiHBG018729.
InParanoidiQ922X9.
KOiK11438.
OMAiGENSWQE.
OrthoDBiEOG091G07KL.
PhylomeDBiQ922X9.
TreeFamiTF315221.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR025799. Arg_MeTrfase.
IPR014644. MeTrfase_PRMT7.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PIRSFiPIRSF036946. Arg_N-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51678. SAM_MT_PRMT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q922X9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVFCGRANP TTGSLEWLEE DEHYDYHQEI ARSSYADMLH DKDRNIKYYQ
60 70 80 90 100
GIRAAVSRVK DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA
110 120 130 140 150
EAAVKIVERN GFSDKIKVIN KHSTEVTVGP DGDLPCRANI LITELFDTEL
160 170 180 190 200
IGEGALPSYE HAHKHLVQED CEAVPHRATV YAQLVESRRM WSWNKLFPVR
210 220 230 240 250
VRTSLGEQVI VPPSELERCP GAPSVCDIQL NQVSPADFTV LSDVLPMFSV
260 270 280 290 300
DFSKQVSSSA ACHSRQFVPL ASGQAQVVLS WWDIEMDPEG KIKCTMAPFW
310 320 330 340 350
AQTDPQELQW RDHWMQCVYF LPQEEPVVQG SPRCLVAHHD DYCVWYSLQR
360 370 380 390 400
TSPDENDSAY QVRPVCDCQA HLLWNRPRFG EINDQDRTDH YAQALRTVLL
410 420 430 440 450
PGSVCLCVSD GSLLSMLAHH LGAEQVFTVE SSVASYRLMK RIFKVNHLED
460 470 480 490 500
KISVINKRPE LLTAADLEGK KVSLLLGEPF FTTSLLPWHN LYFWYVRTSV
510 520 530 540 550
DQHLAPGAVV MPQAASLHAV IVEFRDLWRI RSPCGDCEGF DVHIMDDMIK
560 570 580 590 600
HSLDFRESRE AEPHPLWEYP CRSLSKPQEI LTFDFQQPIP QQPMQSKGTM
610 620 630 640 650
ELTRPGKSHG AVLWMEYQLT PDSTISTGLI NPAEDKGDCC WNPHCKQAVY
660 670 680 690
FLSTTLDLRV PLNGPRSVSY VVEFHPLTGD ITMEFRLADT LS
Length:692
Mass (Da):78,301
Last modified:December 1, 2001 - v1
Checksum:iD61A9500956BF02D
GO

Sequence cautioni

The sequence BAD32582 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37D → E in AAH57177 (PubMed:15489334).Curated1
Sequence conflicti612V → G in BAE36880 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY673972 mRNA. Translation: AAT76979.1.
AK173304 mRNA. Translation: BAD32582.1. Different initiation.
AK154255 mRNA. Translation: BAE32467.1.
AK162376 mRNA. Translation: BAE36880.1.
CH466525 Genomic DNA. Translation: EDL11358.1.
BC006705 mRNA. Translation: AAH06705.1.
BC057177 mRNA. Translation: AAH57177.1.
CCDSiCCDS22633.1.
RefSeqiNP_663379.1. NM_145404.1.
UniGeneiMm.251804.
Mm.446217.

Genome annotation databases

EnsembliENSMUST00000071592; ENSMUSP00000071521; ENSMUSG00000060098.
GeneIDi214572.
KEGGimmu:214572.
UCSCiuc009nfu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY673972 mRNA. Translation: AAT76979.1.
AK173304 mRNA. Translation: BAD32582.1. Different initiation.
AK154255 mRNA. Translation: BAE32467.1.
AK162376 mRNA. Translation: BAE36880.1.
CH466525 Genomic DNA. Translation: EDL11358.1.
BC006705 mRNA. Translation: AAH06705.1.
BC057177 mRNA. Translation: AAH57177.1.
CCDSiCCDS22633.1.
RefSeqiNP_663379.1. NM_145404.1.
UniGeneiMm.251804.
Mm.446217.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C4AX-ray1.70A1-692[»]
ProteinModelPortaliQ922X9.
SMRiQ922X9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229540. 1 interactor.
DIPiDIP-29210N.
STRINGi10090.ENSMUSP00000071521.

PTM databases

iPTMnetiQ922X9.
PhosphoSitePlusiQ922X9.

Proteomic databases

EPDiQ922X9.
MaxQBiQ922X9.
PaxDbiQ922X9.
PeptideAtlasiQ922X9.
PRIDEiQ922X9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071592; ENSMUSP00000071521; ENSMUSG00000060098.
GeneIDi214572.
KEGGimmu:214572.
UCSCiuc009nfu.1. mouse.

Organism-specific databases

CTDi54496.
MGIiMGI:2384879. Prmt7.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410INRX. Eukaryota.
COG0500. LUCA.
GeneTreeiENSGT00860000133873.
HOGENOMiHOG000033951.
HOVERGENiHBG018729.
InParanoidiQ922X9.
KOiK11438.
OMAiGENSWQE.
OrthoDBiEOG091G07KL.
PhylomeDBiQ922X9.
TreeFamiTF315221.

Enzyme and pathway databases

BRENDAi2.1.1.125. 3474.
ReactomeiR-MMU-3214858. RMTs methylate histone arginines.

Miscellaneous databases

ChiTaRSiPrmt7. mouse.
PROiQ922X9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000060098.
CleanExiMM_PRMT7.
ExpressionAtlasiQ922X9. baseline and differential.
GenevisibleiQ922X9. MM.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR025799. Arg_MeTrfase.
IPR014644. MeTrfase_PRMT7.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PIRSFiPIRSF036946. Arg_N-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51678. SAM_MT_PRMT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANM7_MOUSE
AccessioniPrimary (citable) accession number: Q922X9
Secondary accession number(s): Q3TRZ6
, Q69Z62, Q6B955, Q6PG80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.