ID   ZMAT3_RAT               Reviewed;         289 AA.
AC   O08781;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Zinc finger matrin-type protein 3;
DE   AltName: Full=Zinc finger protein WIG-1;
DE   AltName: Full=p53-activated gene 608 protein;
GN   Name=Zmat3 {ECO:0000250|UniProtKB:Q9HA38};
GN   Synonyms=Pag608 {ECO:0000312|EMBL:CAA73610.1},
GN   Wig1 {ECO:0000312|RGD:620134};
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] {ECO:0000305, ECO:0000312|EMBL:CAA73610.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=Fischer {ECO:0000312|EMBL:CAA73610.1};
RC   TISSUE=Embryonic fibroblast {ECO:0000312|EMBL:CAA73610.1};
RX   PubMed=9250682; DOI=10.1093/emboj/16.14.4384;
RA   Israeli D., Tessler E., Haupt Y., Elkeles A., Wilder S., Amson R.,
RA   Telerman A., Oren M.;
RT   "A novel p53-inducible gene, PAG608, encodes a nuclear zinc finger protein
RT   whose overexpression promotes apoptosis.";
RL   EMBO J. 16:4384-4392(1997).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=12196512; DOI=10.1074/jbc.m203594200;
RA   Higashi Y., Asanuma M., Miyazaki I., Haque M.E., Fujita N., Tanaka K.,
RA   Ogawa N.;
RT   "The p53-activated gene, PAG608, requires a zinc finger domain for nuclear
RT   localization and oxidative stress-induced apoptosis.";
RL   J. Biol. Chem. 277:42224-42232(2002).
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:12196512, ECO:0000269|PubMed:9250682}.
CC   -!- SUBUNIT: Interacts with dsRNA. {ECO:0000250|UniProtKB:Q9HA38}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12196512,
CC       ECO:0000269|PubMed:9250682}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:12196512, ECO:0000269|PubMed:9250682}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, gut, lung, and testis.
CC       {ECO:0000269|PubMed:9250682}.
CC   -!- INDUCTION: By DNA damage in a p53-dependent manner, and by 6-
CC       hydroxydopamine (6-OHDA) in PC12 cells. {ECO:0000269|PubMed:12196512,
CC       ECO:0000269|PubMed:9250682}.
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DR   EMBL; Y13148; CAA73610.1; -; mRNA.
DR   RefSeq; NP_071993.1; NM_022548.1.
DR   AlphaFoldDB; O08781; -.
DR   SMR; O08781; -.
DR   STRING; 10116.ENSRNOP00000013858; -.
DR   PaxDb; O08781; -.
DR   Ensembl; ENSRNOT00000113458; ENSRNOP00000083964; ENSRNOG00000063864.
DR   GeneID; 64394; -.
DR   KEGG; rno:64394; -.
DR   UCSC; RGD:620134; rat.
DR   CTD; 64393; -.
DR   RGD; 620134; Zmat3.
DR   eggNOG; ENOG502QW4K; Eukaryota.
DR   GeneTree; ENSGT00730000111202; -.
DR   HOGENOM; CLU_051920_1_0_1; -.
DR   InParanoid; O08781; -.
DR   OMA; QAHYRGK; -.
DR   OrthoDB; 1565630at2759; -.
DR   PhylomeDB; O08781; -.
DR   PRO; PR:O08781; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000010119; Expressed in frontal cortex and 18 other tissues.
DR   GO; GO:0005730; C:nucleolus; IDA:RGD.
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:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; 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..289
FT                   /note="Zinc finger matrin-type protein 3"
FT                   /id="PRO_0000310781"
FT   ZN_FING         70..100
FT                   /note="Matrin-type 1"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         147..177
FT                   /note="Matrin-type 2"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         245..275
FT                   /note="Matrin-type 3"
FT                   /evidence="ECO:0000255"
FT   REGION          180..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   289 AA;  31918 MW;  DE2403036A43DBF1 CRC64;
     MILLQQVWLP LPNRPSTSPP MSVAARSTGT LQLPPQKAFG QEASLPLAGE EDLAKRGEPD
     SALEELCKPL FCKLCNVTLN SAQQAQAHYQ GKNHGKKLRN YYAANSCPPP ARMSSVAEPV
     ATPLVPVPPQ VGSCKPGGRV ILATENDYCK LCDASFSSPA VAQAHYQGKN HAKRLRLAEA
     QSHSFSDSAE AGQRRTRKEG SEFKMVTTRR NMYTVQSNSG PYFNARSRQR IPRDLAMCVT
     PSGQFYCSMC NVGAGEEVEF RQHLESKQHK SKVSEQRYRS EMENLGYVQ