MATR3_RAT
ID MATR3_RAT Reviewed; 845 AA.
AC P43244; O35833; Q5DVW1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Matrin-3;
DE AltName: Full=Nuclear scaffold protein p130/MAT3;
GN Name=Matr3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=2033075; DOI=10.1016/s0021-9258(18)92902-9;
RA Belgrader P., Dey R., Berezney R.;
RT "Molecular cloning of matrin 3. A 125-kilodalton protein of the nuclear
RT matrix contains an extensive acidic domain.";
RL J. Biol. Chem. 266:9893-9899(1991).
RN [2]
RP SEQUENCE REVISION.
RA Berezney R.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hibino Y.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-195; SER-206;
RP SER-208; SER-598; THR-739; SER-745; SER-757 AND SER-760, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role in transcription or may interact with other
CC nuclear matrix proteins to form the internal fibrogranular network. In
CC association with the SFPQ-NONO heteromer may play a role in nuclear
CC retention of defective RNAs. Plays a role in the regulation of DNA
CC virus-mediated innate immune response by assembling into the HDP-RNP
CC complex, a complex that serves as a platform for IRF3 phosphorylation
CC and subsequent innate immune response activation through the cGAS-STING
CC pathway. Binds to N6-methyladenosine (m6A)-containing mRNAs and
CC contributes to MYC stability by binding to m6A-containing MYC mRNAs.
CC May bind to specific miRNA hairpins. {ECO:0000250|UniProtKB:P43243}.
CC -!- SUBUNIT: Part of a complex consisting of SFPQ, NONO and MATR3.
CC Interacts with AGO1 and AGO2 (By similarity). Part of a complex
CC composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67,
CC RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-
CC specific methyltransferase activity. Interacts with TARDBP. Part of the
CC HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6,
CC paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1
CC RNA. Interacts with FUS. Interacts with IGF2BP1. Interacts with IGF2BP2
CC and IGF2BP3. {ECO:0000250|UniProtKB:P43243}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix.
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DR EMBL; M63485; AAB63955.1; -; mRNA.
DR EMBL; AB205483; BAD90681.1; -; mRNA.
DR RefSeq; NP_062022.2; NM_019149.3.
DR RefSeq; XP_006254596.1; XM_006254534.3.
DR RefSeq; XP_017456375.1; XM_017600886.1.
DR RefSeq; XP_017456376.1; XM_017600887.1.
DR AlphaFoldDB; P43244; -.
DR SMR; P43244; -.
DR BioGRID; 247833; 6.
DR IntAct; P43244; 3.
DR MINT; P43244; -.
DR STRING; 10116.ENSRNOP00000026949; -.
DR iPTMnet; P43244; -.
DR PhosphoSitePlus; P43244; -.
DR jPOST; P43244; -.
DR PaxDb; P43244; -.
DR PRIDE; P43244; -.
DR GeneID; 29150; -.
DR KEGG; rno:29150; -.
DR UCSC; RGD:3052; rat.
DR CTD; 9782; -.
DR RGD; 3052; Matr3.
DR eggNOG; ENOG502QRVG; Eukaryota.
DR InParanoid; P43244; -.
DR OrthoDB; 200901at2759; -.
DR PhylomeDB; P43244; -.
DR TreeFam; TF333921; -.
DR PRO; PR:P43244; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; ISO:RGD.
DR GO; GO:0001825; P:blastocyst formation; ISO:RGD.
DR GO; GO:0003170; P:heart valve development; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:RGD.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR CDD; cd12714; RRM1_MATR3; 1.
DR CDD; cd12715; RRM2_MATR3; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034928; MATR3_RRM1.
DR InterPro; IPR034930; MATR3_RRM2.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Immunity; Innate immunity; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CHAIN 2..845
FT /note="Matrin-3"
FT /id="PRO_0000081624"
FT DOMAIN 398..473
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 496..571
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 799..830
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 147..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 708..716
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 588..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 3
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 158
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 571
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 679
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 739
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 834
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 617
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 717
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 768
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 834
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CONFLICT 486
FT /note="E -> Q (in Ref. 3; BAD90681)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="I -> L (in Ref. 3; BAD90681)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="G -> V (in Ref. 3; BAD90681)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="S -> T (in Ref. 3; BAD90681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 845 AA; 94447 MW; 5EA8D05529171238 CRC64;
MSKSFQQSSL GRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDTDQASN ILASFGLSAR
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP
EGKPDEKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD
GKESPSDKKS KTDGAQKTEN PAEGKEQEEK SGEDGEKDTK DDQTEQEPSM LLESEDELLV
DEEEAAALIE SGSSVGDETD LANLGDVSSD GKKEPSDKAV KKDASATSKK KLKKVDKIEE
LDQENEAALE NGIKNEENTE PGAESAENAD DPNKDASDNS DGQNDENKED YTIPDEYRIG
PYQPNVPGGI DYVIPKTGFY CKLCSLFYTN EEVAKNTHCS SLPHYQKLKK FLNKLAEERR
QKKES
