Z354C_RAT
ID Z354C_RAT Reviewed; 560 AA.
AC Q9EPU7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Zinc finger protein 354C;
DE AltName: Full=Protein AJ18;
GN Name=Znf354c; Synonyms=Zfp354c;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH RUNX2.
RC STRAIN=Wistar;
RX PubMed=11278774; DOI=10.1074/jbc.m010885200;
RA Jheon A.H., Ganss B., Cheifetz S., Sodek J.;
RT "Characterization of a novel KRAB/C2H2 zinc finger transcription factor
RT involved in bone development.";
RL J. Biol. Chem. 276:18282-18289(2001).
CC -!- FUNCTION: May function as a transcription repressor. Binds to 5'-CCACA-
CC 3' core sequence. Suppresses osteogenic effects of RUNX2. May be
CC involved in osteoblastic differentiation. Plays a role in postnatal
CC myogenesis, may be involved in the regulation of satellite cells self-
CC renewal (By similarity). {ECO:0000250|UniProtKB:Q571J5,
CC ECO:0000269|PubMed:11278774}.
CC -!- SUBUNIT: Interacts with RUNX2. Binds consensus element OSE2.
CC {ECO:0000269|PubMed:11278774}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11278774}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Very low expression in adult
CC bone tissues. Overexpression suppresses alkaline phosphatase induction
CC by BMP7. {ECO:0000269|PubMed:11278774}.
CC -!- DEVELOPMENTAL STAGE: Expressed during osteoblast differentiation and
CC bone development. Detected in embryonic bone formation in calvariae and
CC tibiae. Very low expression in neonate bone tissues. Expressed in
CC kidney and brain. {ECO:0000269|PubMed:11278774}.
CC -!- DOMAIN: KRAB domain is not required for nuclear targeting or for DNA
CC binding. {ECO:0000269|PubMed:11278774}.
CC -!- DOMAIN: Zinc finger region is involved in nuclear targeting and DNA-
CC binding. {ECO:0000269|PubMed:11278774}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF321874; AAG41994.1; -; mRNA.
DR RefSeq; NP_076478.1; NM_023988.1.
DR AlphaFoldDB; Q9EPU7; -.
DR SMR; Q9EPU7; -.
DR STRING; 10116.ENSRNOP00000000248; -.
DR PaxDb; Q9EPU7; -.
DR GeneID; 78972; -.
DR KEGG; rno:78972; -.
DR UCSC; RGD:69405; rat.
DR CTD; 30944; -.
DR RGD; 69405; Zfp354c.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9EPU7; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9EPU7; -.
DR Reactome; R-RNO-212436; Generic Transcription Pathway.
DR PRO; PR:Q9EPU7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; 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; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR DisProt; DP01555; -.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..560
FT /note="Zinc finger protein 354C"
FT /id="PRO_0000280410"
FT DOMAIN 14..84
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 218..240
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..268
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..296
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..324
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 330..352
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..380
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..464
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 470..492
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..520
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 139..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86Y25"
FT CROSSLNK 169
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86Y25"
SQ SEQUENCE 560 AA; 64193 MW; 09249239626F22F5 CRC64;
MAVDLLAARG TEPVTFRDVA VSFSQDEWLH LDPAQRTLYR EVMLENYSNL ASLGFQASIP
PVIGKLQKGQ DPCMEREAPE DTCLDFQIQS EIEASSPEQD VFIEGPSRGL LKNRSTKCAY
WKISFGELVK YERLETAQEQ EKKAHEPGAA SPKEVTSEDG IPTDPELEKP LFMNKALVSQ
ETDPIERVPG MYHTSEKDLP QDFDLMRNFQ IYPGQKPYVC SECGKGFSQS LHLLEHKRIH
TGEKPYKCSE CGKSFSHRSS LLAHQRTHTG EKPYKCSECE KAFGSSSTLI KHLRVHTGEK
PYRCRECGKA FSQCSTLTVH QRIHTGEKLY KCAECDKAFN CRAKLHRHQR IHTGEKPYKC
AECGKGYSQF PSLAEHQRLH TGGQLCQCLQ CGRTFTRVST LIEHQRIHTG QKPYQCNECG
KTFNQYSSFN EHRKIHTGEK LYTCEECGKA FGCKSNLYRH QRIHTGEKPY QCNQCGKAFS
QYSFLTEHER IHTGEKLYKC MECGKAYSYR SNLCRHKKVH LKERLYKWKE YGTPFMYGSS
LAPHQRCLKG EKPEDLNSSL
