PLAG1_RAT
ID PLAG1_RAT Reviewed; 499 AA.
AC Q5U2T6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zinc finger protein PLAG1;
DE AltName: Full=Pleiomorphic adenoma gene 1 protein;
GN Name=Plag1;
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 [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Transcription factor whose activation results in up-
CC regulation of target genes, such as IGFII, leading to uncontrolled cell
CC proliferation: when overexpressed in cultured cells, higher
CC proliferation rate and transformation are observed. Other target genes
CC such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with
CC PLAG1 induction. Proto-oncogene whose ectopic expression can trigger
CC the development of pleomorphic adenomas of the salivary gland and
CC lipoblastomas. Cooperates with CBFB-MYH11 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KPNA2, which escorts protein to the nucleus via
CC interaction with nuclear localization signal. Interacts with E3 SUMO-
CC protein ligase PIAS1, PIAS2 and PIAS4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Strong nucleolar localization when
CC sumoylation is inhibited. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, spleen, lung, kidney, brain,
CC testis and epididymis but not in salivary glands.
CC -!- DOMAIN: C2H2-type zinc fingers 3 interacts with DNA-binding site G-
CC clusterinc fingers. C2H2-type zinc fingers 6 and 7 interact with DNA-
CC binding site core sequence (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO1; which inhibits transcriptional activity,
CC but does not affect nuclear localization. Blockers of sumoylation
CC pathway such as SENP3 and inactive UBE2I increases transcriptional
CC capacity. Sumoylation is increased in the presence of PIAS1 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylated by lysine acetyltransferase EP300; which activates
CC transcriptional capacity. Lysine residues that are sumoylated also seem
CC to be target for acetylation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC085871; AAH85871.1; -; mRNA.
DR RefSeq; NP_001008317.1; NM_001008316.1.
DR RefSeq; XP_008761747.1; XM_008763525.2.
DR RefSeq; XP_008761748.1; XM_008763526.2.
DR RefSeq; XP_017448710.1; XM_017593221.1.
DR RefSeq; XP_017448711.1; XM_017593222.1.
DR RefSeq; XP_017448712.1; XM_017593223.1.
DR AlphaFoldDB; Q5U2T6; -.
DR SMR; Q5U2T6; -.
DR STRING; 10116.ENSRNOP00000011721; -.
DR PaxDb; Q5U2T6; -.
DR Ensembl; ENSRNOT00000011721; ENSRNOP00000011721; ENSRNOG00000008846.
DR GeneID; 297804; -.
DR KEGG; rno:297804; -.
DR UCSC; RGD:1305286; rat.
DR CTD; 5324; -.
DR RGD; 1305286; Plag1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159246; -.
DR HOGENOM; CLU_002678_66_1_1; -.
DR InParanoid; Q5U2T6; -.
DR OMA; GTENRHD; -.
DR OrthoDB; 615178at2759; -.
DR PhylomeDB; Q5U2T6; -.
DR TreeFam; TF332024; -.
DR PRO; PR:Q5U2T6; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008846; Expressed in cerebellum and 15 other tissues.
DR Genevisible; Q5U2T6; RN.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0022612; P:gland morphogenesis; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0035265; P:organ growth; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0060736; P:prostate gland growth; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR027765; PLAG1/PLAGL2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24390:SF64; PTHR24390:SF64; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..499
FT /note="Zinc finger protein PLAG1"
FT /id="PRO_0000295109"
FT ZN_FING 34..56
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 62..86
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 92..114
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 121..143
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 150..172
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 185..207
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 213..236
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..84
FT /note="Interaction with KPNA2"
FT /evidence="ECO:0000250"
FT REGION 41..242
FT /note="Decreased nuclear import with localization in the
FT nucleus but also in the cytoplasm"
FT /evidence="ECO:0000250"
FT REGION 243..499
FT /note="Activates transcription; Inhibition of nuclear
FT import due to lack of NLS and KPNA2 interaction"
FT /evidence="ECO:0000250"
FT REGION 243..383
FT /note="Repression domain; contains 3 sumoylation motifs and
FT massively decrease transcription activity"
FT /evidence="ECO:0000250"
FT REGION 364..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..499
FT /note="Massively activates transcription"
FT /evidence="ECO:0000250"
FT MOTIF 22..25
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 364..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 499 AA; 55640 MW; 8EC2FA9F25A1CC8B CRC64;
MATVIPGDLS EVRDTQKAPS GKRKRGESKP RKNFPCQLCD KAFNSVEKLK VHSFSHTGER
PYKCTHQDCT KAFVSKYKLQ RHMATHSPEK THKCNYCEKM FHRKDHLKNH LHTHDPNKET
FKCEECGKSY NTKLGFKRHL ALHAATSGDL TCKVCLQTFE STGVLLEHLK SHAGKSSGGV
KEKKHQCEHC ERRFYTRKDV RRHMVVHTGR KDFLCQYCAQ RFGRKDHLTR HMKKSHNQEL
LKVKTEPVDF LDPFTCNMSV PIKDELLPVM SLPSSELLSK PFTNTLQLNL YNTPFQSMQS
SGSTHQMITT LPLGMTCPID MDTVHPSHHL AFKCPFSSTS YAISIPEKEQ PLKGEIESYL
MELQGGAPSS SQDSQASSSK LGLEPQSGSP DDGAGDLSLS KSSISISDPL NTPALDFSQL
FNFIPLNGPP YNPLSVGSLG MSYSQDEAHS SVSQLPTQTQ DLQDPANTVG LGSLHSLSAA
FTSSLSSSTT LPRFHQAFQ
