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P43244 (MATR3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrin-3
Alternative name(s):
Nuclear scaffold protein p130/MAT3
Gene names
Name:Matr3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs By similarity.

Subunit structure

Part of complex consisting of SFPQ, NONO and MATR3. Interacts with EIF2C1 and EIF2C2 By similarity.

Subcellular location

Nucleus matrix.

Sequence similarities

Contains 1 matrin-type zinc finger.

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 845844Matrin-3
PRO_0000081624

Regions

Domain398 – 47376RRM 1
Domain496 – 57176RRM 2
Zinc finger799 – 83032Matrin-type
Motif708 – 7169Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue31N6-acetyllysine By similarity
Modified residue41Phosphoserine By similarity
Modified residue91Phosphoserine By similarity
Modified residue141Phosphoserine By similarity
Modified residue221Phosphoserine By similarity
Modified residue411Phosphoserine By similarity
Modified residue1181Phosphoserine By similarity
Modified residue1881Phosphoserine Ref.5
Modified residue1951Phosphoserine By similarity
Modified residue2061Phosphoserine By similarity
Modified residue2081Phosphoserine By similarity
Modified residue2191Phosphotyrosine By similarity
Modified residue5221N6-acetyllysine By similarity
Modified residue5331Phosphoserine By similarity
Modified residue5711N6-acetyllysine By similarity
Modified residue5961Phosphoserine By similarity
Modified residue5981Phosphoserine Ref.4
Modified residue6041Phosphoserine By similarity
Modified residue6061Phosphoserine By similarity
Modified residue7391Phosphothreonine By similarity
Modified residue7451Phosphoserine By similarity
Modified residue8341N6-acetyllysine By similarity

Experimental info

Sequence conflict4861E → Q in BAD90681. Ref.3
Sequence conflict6691I → L in BAD90681. Ref.3
Sequence conflict7881G → V in BAD90681. Ref.3
Sequence conflict8451S → T in BAD90681. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P43244 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 5EA8D05529171238

FASTA84594,447
        10         20         30         40         50         60 
MSKSFQQSSL GRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM 

        70         80         90        100        110        120 
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDTDQASN ILASFGLSAR 

       130        140        150        160        170        180 
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE 

       190        200        210        220        230        240 
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS 

       250        260        270        280        290        300 
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV 

       310        320        330        340        350        360 
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP 

       370        380        390        400        410        420 
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE 

       430        440        450        460        470        480 
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP 

       490        500        510        520        530        540 
EGKPDEKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME 

       550        560        570        580        590        600 
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD 

       610        620        630        640        650        660 
GKESPSDKKS KTDGAQKTEN PAEGKEQEEK SGEDGEKDTK DDQTEQEPSM LLESEDELLV 

       670        680        690        700        710        720 
DEEEAAALIE SGSSVGDETD LANLGDVSSD GKKEPSDKAV KKDASATSKK KLKKVDKIEE 

       730        740        750        760        770        780 
LDQENEAALE NGIKNEENTE PGAESAENAD DPNKDASDNS DGQNDENKED YTIPDEYRIG 

       790        800        810        820        830        840 
PYQPNVPGGI DYVIPKTGFY CKLCSLFYTN EEVAKNTHCS SLPHYQKLKK FLNKLAEERR 


QKKES

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of matrin 3. A 125-kilodalton protein of the nuclear matrix contains an extensive acidic domain."
Belgrader P., Dey R., Berezney R.
J. Biol. Chem. 266:9893-9899(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]Berezney R.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Hibino Y.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
Moser K., White F.M.
J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, MASS SPECTROMETRY.
Strain: Fischer.
Tissue: Liver.
[5]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, MASS SPECTROMETRY.
Tissue: Renal collecting duct.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M63485 mRNA. Translation: AAB63955.1.
AB205483 mRNA. Translation: BAD90681.1.
IPIIPI00555259.
RefSeqNP_062022.2. NM_019149.3.
UniGeneRn.29774.

3D structure databases

ProteinModelPortalP43244.
SMRP43244. Positions 390-576.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000026949.

PTM databases

PhosphoSiteP43244.

Proteomic databases

PaxDbP43244.
PRIDEP43244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026949; ENSRNOP00000026949; ENSRNOG00000019875.
GeneID29150.
KEGGrno:29150.
UCSCRGD:3052. rat.

Organism-specific databases

CTD9782.
RGD3052. Matr3.

Phylogenomic databases

eggNOGNOG80010.
GeneTreeENSGT00650000093206.
HOGENOMHOG000015369.
HOVERGENHBG057347.
InParanoidP43244.
KOK13213.
OrthoDBEOG4KSPJ4.

Gene expression databases

GenevestigatorP43244.
GermOnlineENSRNOG00000019875. Rattus norvegicus.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
SM00355. ZnF_C2H2. 1 hit.
SM00451. ZnF_U1. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608155.

Entry information

Entry nameMATR3_RAT
AccessionPrimary (citable) accession number: P43244
Secondary accession number(s): O35833, Q5DVW1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 24, 2001
Last modified: April 3, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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