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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
 
 
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