ZN384_RAT
ID ZN384_RAT Reviewed; 579 AA.
AC Q9EQJ4; Q9EQJ2; Q9EQJ3; Q9JMJ5;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Zinc finger protein 384;
DE AltName: Full=Cas-associated zinc finger protein;
DE AltName: Full=Nuclear matrix transcription factor 4;
DE Short=Nuclear matrix protein 4;
GN Name=Znf384; Synonyms=Ciz, Nmp4, Zfp384;
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 1), SUBCELLULAR LOCATION, DNA-BINDING,
RP AND INTERACTION WITH BCAR1.
RX PubMed=10669742; DOI=10.1128/mcb.20.5.1649-1658.2000;
RA Nakamoto T., Yamagata T., Sakai R., Ogawa S., Honda H., Ueno H., Hirano N.,
RA Yazaki Y., Hirai H.;
RT "CIZ, a zinc finger protein that interacts with p130cas and activates the
RT expression of matrix metalloproteinases.";
RL Mol. Cell. Biol. 20:1649-1658(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=Sprague-Dawley;
RX PubMed=11149472; DOI=10.1359/jbmr.2001.16.1.10;
RA Thunyakitpisal P., Alvarez M., Tokunaga K., Onyia J.E., Hock J., Ohashi N.,
RA Feister H., Rhodes S.J., Bidwell J.P.;
RT "Cloning and functional analysis of a family of nuclear matrix
RT transcription factors (NP/NMP4) that regulate type I collagen expression in
RT osteoblasts.";
RL J. Bone Miner. Res. 16:10-23(2001).
CC -!- FUNCTION: Transcription factor that binds the consensus DNA sequence
CC [GC]AAAAA. Seems to bind and regulate the promoters of MMP1, MMP3, MMP7
CC and COL1A1.
CC -!- SUBUNIT: Interacts with BCAR1. {ECO:0000269|PubMed:10669742}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10669742}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9EQJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQJ4-2; Sequence=VSP_006921;
CC Name=3;
CC IsoId=Q9EQJ4-3; Sequence=VSP_006922;
CC -!- TISSUE SPECIFICITY: Expressed in osteocytes, osteoblasts, and
CC chondrocytes in bone.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB019281; BAA89664.1; -; mRNA.
DR EMBL; AF216804; AAG40582.1; -; mRNA.
DR EMBL; AF216805; AAG40583.1; -; mRNA.
DR EMBL; AF216806; AAG40584.1; -; mRNA.
DR RefSeq; NP_001030002.1; NM_001034830.1.
DR RefSeq; NP_001030003.1; NM_001034831.1.
DR RefSeq; NP_596920.2; NM_133429.2.
DR AlphaFoldDB; Q9EQJ4; -.
DR SMR; Q9EQJ4; -.
DR STRING; 10116.ENSRNOP00000052839; -.
DR PaxDb; Q9EQJ4; -.
DR GeneID; 171018; -.
DR KEGG; rno:171018; -.
DR UCSC; RGD:708346; rat. [Q9EQJ4-1]
DR CTD; 269800; -.
DR RGD; 708346; Zfp384.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9EQJ4; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9EQJ4; -.
DR PRO; PR:Q9EQJ4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IMP:RGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IMP:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..579
FT /note="Zinc finger protein 384"
FT /id="PRO_0000047553"
FT ZN_FING 229..251
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 257..279
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 318..340
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 346..368
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..398
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..456
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 171..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 103..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11149472"
FT /id="VSP_006921"
FT VAR_SEQ 301..361
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11149472"
FT /id="VSP_006922"
FT CONFLICT 178..179
FT /note="GG -> RS (in Ref. 1; BAA89664)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..577
FT /note="LA -> WP (in Ref. 1; BAA89664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 63139 MW; FBC242E0D1050C45 CRC64;
MEESHFNSNP YFWPSIPTVS GQIENTMFIN KMKDQLLPEK GCGLAPPHYP TLLTVPASVS
LSSGISMDTE SKSEQLTPHS QASVTQNITV VPVPSTGLMT AGVSCSQRWR REGSQSRGPG
LVITSPSGSL VTTASSAQTF PISTPMIVSA LPPGSQALQV VPDLSKKVAS TLTEEGGGGG
GGGGTVAPPK PPRGRKKKRM LESGLPEMND PYVLAPGDDD DHQKDGKTYR CRMCSLTFYS
KSEMQIHSKS HTETKPHKCP HCSKTFANSS YLAQHIRIHS GAKPYSCNFC EKSFRQLSHL
QQHTRIHSKM HTETIKPHKC PHCSKTFANT SYLAQHLRIH SGAKPYNCSY CQKAFRQLSH
LQQHTRIHTG DRPYKCAHPG CEKAFTQLSN LQSHRRQHNK DKPFKCHNCH RAYTDAASLE
AHLSTHTVKH AKVYTCTICS RAYTSETYLM KHMRKHNPPD LQQQVQAAAA AAAVAQAQAQ
AQAQAQAQAQ AQAQAQAQAQ AQASQASQQQ QQQQPPPPQP PHFQSPGAAP QGGGGGDSNQ
NPPPQCSFDL TPYKPAEHHK DICLTVTTST IQVEHLASS
