ST18_RAT
ID ST18_RAT Reviewed; 1032 AA.
AC Q9QX27; P70588;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Suppression of tumorigenicity 18 protein;
DE AltName: Full=C2-HC type zinc finger protein r-MyT3;
DE AltName: Full=Neural zinc finger factor 3;
DE Short=NZF-3;
GN Name=St18; Synonyms=Nzf3;
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] (ISOFORM 2).
RC TISSUE=Brain cortex;
RX PubMed=8980226; DOI=10.1016/s0092-8674(00)81815-2;
RA Bellefroid E.J., Bourguignon C., Hollemann T., Ma Q., Anderson D.J.,
RA Kintner C., Pieler T.;
RT "X-MyT1, a Xenopus C2HC-type zinc finger protein with a regulatory function
RT in neuronal differentiation.";
RL Cell 87:1191-1202(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9478997; DOI=10.1074/jbc.273.9.5366;
RA Yee K.S.Y., Yu V.C.;
RT "Isolation and characterization of a novel member of the neural zinc finger
RT factor/myelin transcription factor family with transcriptional repression
RT activity.";
RL J. Biol. Chem. 273:5366-5374(1998).
CC -!- FUNCTION: Repressor that binds to DNA sequences containing a bipartite
CC element consisting of a direct repeat of the sequence 5'-AAAGTTT-3'
CC separated by 2-9 nucleotides. Represses basal transcription activity
CC from target promoters. {ECO:0000269|PubMed:9478997}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9478997}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QX27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QX27-2; Sequence=VSP_018195;
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:9478997}.
CC -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
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DR EMBL; U67080; AAB40717.1; -; mRNA.
DR EMBL; AF031942; AAC40048.1; -; mRNA.
DR PIR; T14124; T14124.
DR PIR; T31669; T31669.
DR RefSeq; NP_695222.2; NM_153310.2.
DR AlphaFoldDB; Q9QX27; -.
DR SMR; Q9QX27; -.
DR STRING; 10116.ENSRNOP00000056380; -.
DR PaxDb; Q9QX27; -.
DR GeneID; 266680; -.
DR KEGG; rno:266680; -.
DR UCSC; RGD:708566; rat. [Q9QX27-1]
DR CTD; 9705; -.
DR RGD; 708566; St18.
DR eggNOG; KOG3803; Eukaryota.
DR InParanoid; Q9QX27; -.
DR PhylomeDB; Q9QX27; -.
DR PRO; PR:Q9QX27; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:RGD.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR InterPro; IPR013681; Myelin_TF.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF08474; MYT1; 1.
DR Pfam; PF01530; zf-C2HC; 6.
DR SUPFAM; SSF103637; SSF103637; 6.
DR PROSITE; PS51802; ZF_CCHHC; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1032
FT /note="Suppression of tumorigenicity 18 protein"
FT /id="PRO_0000234032"
FT ZN_FING 344..387
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 388..431
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 700..743
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 744..787
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 792..835
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 845..888
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 29..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 905..974
FT /evidence="ECO:0000255"
FT COMPBIAS 48..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 758
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 771
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 777
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 806
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 854
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 859
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 872
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT VAR_SEQ 1..17
FT /note="MQRLKIKRCILSQKEPK -> MDSLIPELR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8980226"
FT /id="VSP_018195"
FT CONFLICT 70
FT /note="G -> N (in Ref. 1; AAC40048)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="N -> P (in Ref. 1; AAC40048)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="V -> E (in Ref. 2; AAB40717)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="A -> S (in Ref. 2; AAB40717)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="N -> H (in Ref. 1; AAC40048)"
FT /evidence="ECO:0000305"
FT CONFLICT 614..615
FT /note="PP -> GG (in Ref. 2; AAB40717)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="L -> V (in Ref. 2; AAB40717)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="Missing (in Ref. 2; AAB40717)"
FT /evidence="ECO:0000305"
FT CONFLICT 1027
FT /note="V -> A (in Ref. 1; AAC40048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1032 AA; 113434 MW; 4BD50C73A4201C56 CRC64;
MQRLKIKRCI LSQKEPKVAY DCSMAKKRRA EEQALGVPVN KRKSLLMKPR HYSPDMDCKE
NPDNRNEDDG LETNDHSTAD EIVVKPMDKT LHLPAQESSL PKEDQYACYP ELMVKSLMHL
GKFEESESVQ TVGENLNGNG IQSLKAECDE ANECFMVHSD DGRDKVHHSQ PPFCSSGDSE
SDSDNTENGW GSGSNSSEDT DTHKGPKRKL TYNRKDLLEV PEIKAEDDKF IPCENRCDSD
TSGRDPQNSH MEPLAVKVQP SFPEVEESES LATVIAESAE VEKAKGSLSL LEQAIALQAE
RGSVFHHTYK ELDRFLLDHL ARQRRQPKVT DASGRQIFNN KHSPRPERRE AKCPIPGCDG
TGHVTGLYPH HRSLSGCPHK VRVPLEILAM HENVLKCPTP GCTGRGHVNS NRNTHRSLSG
CPIAAAEKLA MTQDKSQLDS SQTGQGPEQA HRVNLVKQIE FNFRSQAITS PRASASKEQE
KFGKVPFDYA SFDAQVFGKR PLLQTGQGQK APPFPESKHF SNPVKFSNGL PSAGAHTQST
VRASSYGHGQ YSEDTHIAAA AAILNLSTRC REATDILSNK PQSLRAKGAE IEVDENGTLD
LSMKKNRILD KSIPPTSSHT TIATPSSSPF KASSLLVNAA FYQALCDQEG WNVPINYSKS
HGKTEEEKEK DPVNSLENLE EKKFAGEASI PSPKPKLHTR DLKKELITCP TPGCDGSGHV
TGNYASHRSV SGCPLADKTL KSLMAANSQE LKCPTPGCDG SGHVTGNYAS HRSLSGCPRA
RKGGIKMTPT KEEKEDSELR CPVIGCDGQG HISGKYTSHR TASGCPLAAK RQKENPLNGT
PLSWKLNKQE LPHCPLPGCN GLGHVNNVFV THRSLSGCPL NAQAIKKVKV SEELMTIKLK
ATGGIEGDEE IRHLDEEIKE LNESNLKIEA DMMKLQTQIT SMESNLKTIE EENKLIEQSN
ESLLKELAGL SQALISSLAD IQLPQMGPIN EQNFEAYVNT LTDMYSNLER DYSPECKALL
ESIKQAVKGI HV
