ZMAT3_MOUSE
ID ZMAT3_MOUSE Reviewed; 290 AA.
AC O54836;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Zinc finger matrin-type protein 3;
DE AltName: Full=Wild-type p53-induced gene 1 protein;
DE AltName: Full=Zinc finger protein WIG-1;
DE AltName: Full=p53-activated gene 608 protein;
GN Name=Zmat3 {ECO:0000312|MGI:MGI:1195270};
GN Synonyms=Pag608 {ECO:0000303|PubMed:17234339},
GN Wig1 {ECO:0000312|MGI:MGI:1195270};
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] {ECO:0000305, ECO:0000312|EMBL:AAB97673.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=T-cell lymphoma {ECO:0000312|EMBL:AAB97673.1};
RX PubMed=9400996; DOI=10.1038/sj.onc.1201454;
RA Varmeh-Ziaie S., Okan I., Wang Y., Magnusson K.P., Warthoe P., Strauss M.,
RA Wiman K.G.;
RT "Wig-1, a new p53-induced gene encoding a zinc finger protein.";
RL Oncogene 15:2699-2704(1997).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=12135743; DOI=10.1016/s0014-5793(02)03004-1;
RA Wilhelm M.T., Mendez-Vidal C., Wiman K.G.;
RT "Identification of functional p53-binding motifs in the mouse wig-1
RT promoter.";
RL FEBS Lett. 524:69-72(2002).
RN [3] {ECO:0000305}
RP INDUCTION.
RX PubMed=17234339; DOI=10.1016/j.neulet.2006.12.036;
RA Asanuma M., Miyazaki I., Higashi Y., Diaz-Corrales F.J., Shimizu M.,
RA Miyoshi K., Ogawa N.;
RT "Suppression of p53-activated gene, PAG608, attenuates methamphetamine-
RT induced neurotoxicity.";
RL Neurosci. Lett. 414:263-267(2007).
CC -!- FUNCTION: Acts as a bona fide target gene of p53/TP53. May play a role
CC in the TP53-dependent growth regulatory pathway. May contribute to
CC TP53-mediated apoptosis by regulation of TP53 expression and
CC translocation to the nucleus and nucleolus.
CC {ECO:0000269|PubMed:12135743}.
CC -!- SUBUNIT: Interacts with dsRNA. {ECO:0000250|UniProtKB:Q9HA38}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08781}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:O08781}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in brain and testis. Also
CC expressed in lung, kidney and spleen after whole body gamma
CC irradiation. {ECO:0000269|PubMed:9400996}.
CC -!- INDUCTION: By DNA damage in a p53-dependent manner, and by
CC methamphetamine (METH) in a catecholaminergic cell line.
CC {ECO:0000269|PubMed:17234339, ECO:0000269|PubMed:9400996}.
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DR EMBL; AF012923; AAB97673.1; -; mRNA.
DR CCDS; CCDS17293.1; -.
DR AlphaFoldDB; O54836; -.
DR SMR; O54836; -.
DR IntAct; O54836; 1.
DR STRING; 10090.ENSMUSP00000029199; -.
DR iPTMnet; O54836; -.
DR PhosphoSitePlus; O54836; -.
DR EPD; O54836; -.
DR MaxQB; O54836; -.
DR PaxDb; O54836; -.
DR PRIDE; O54836; -.
DR ProteomicsDB; 299563; -.
DR MGI; MGI:1195270; Zmat3.
DR eggNOG; ENOG502QW4K; Eukaryota.
DR InParanoid; O54836; -.
DR PhylomeDB; O54836; -.
DR ChiTaRS; Zmat3; mouse.
DR PRO; PR:O54836; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O54836; protein.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; TAS:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 3.
PE 2: Evidence at transcript level;
KW Apoptosis; DNA damage; Growth regulation; Metal-binding; Nucleus;
KW Protein transport; Reference proteome; Repeat; RNA-binding; Translocation;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..290
FT /note="Zinc finger matrin-type protein 3"
FT /id="PRO_0000310780"
FT ZN_FING 70..100
FT /note="Matrin-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 148..178
FT /note="Matrin-type 2"
FT /evidence="ECO:0000255"
FT ZN_FING 246..276
FT /note="Matrin-type 3"
FT /evidence="ECO:0000255"
FT REGION 181..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 32001 MW; 32E545A54E04581B CRC64;
MILLQQVWLP LPNRPSTSPP MSVAARSTRT LQLPPQKAFG QEASLPLAGE EDLAKRGEPD
SALEELCKPL FCKLCNVTLN SAQQAQAHYQ GKNHGKKLRN YYAANSCPPP ARVSSVVAEP
VATPLVPVPP QVGSCKPGGR VILATENDYC KLCDASFSSP AVAQAHYQGK NHAKRLRLAE
AQSHSFSDSA EAGQRRTRKE GSEFKMVATR RNMNPVQSNS GPYFNARSRQ RIPRDLAMCV
TPSGQFYCSM CNVGAGEEVE FRQHLESKQH KSKVSEQRYR SEMENLGYVQ