Z354C_MOUSE
ID Z354C_MOUSE Reviewed; 560 AA.
AC Q571J5; Q3UKS9; Q8C365; Q9JLD3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zinc finger protein 354C;
DE AltName: Full=Kidney, ischemia, and developmentally-regulated protein 3;
GN Name=Znf354c; Synonyms=Kiaa4218, Kid3, Zfp354c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10786630; DOI=10.1016/s0167-4781(99)00239-0;
RA Watson R.P., Tekki-Kessaris N., Boulter C.A.;
RT "Characterisation, chromosomal localisation and expression of the mouse
RT Kid3 gene.";
RL Biochim. Biophys. Acta 1490:153-158(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
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 (By similarity). Plays a role
CC in postnatal myogenesis, may be involved in the regulation of satellite
CC cells self-renewal (PubMed:27446912). {ECO:0000250|UniProtKB:Q86Y25,
CC ECO:0000250|UniProtKB:Q9EPU7, ECO:0000269|PubMed:27446912}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9EPU7}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Lower levels in kidney, heart,
CC lung, spleen and eye. Down-regulated during kidney maturation.
CC Expressed in embryonic myogenic progenitor cells, not expressed in
CC adult and aged satellite cells (PubMed:27446912).
CC {ECO:0000269|PubMed:10786630, ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: In myogenic progenitor cells, expressed during
CC early myogenic development (11.5 dpc) to be gradually down-regulated
CC during the fetal stages (from 14.5 dpc to adulthood).
CC {ECO:0000269|PubMed:27446912}.
CC -!- DOMAIN: KRAB domain is not required for nuclear targeting or for DNA
CC binding. {ECO:0000250|UniProtKB:Q9EPU7}.
CC -!- DOMAIN: Zinc finger region is involved in nuclear targeting and DNA-
CC binding. {ECO:0000250|UniProtKB:Q9EPU7}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90379.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF192804; AAF35173.1; -; mRNA.
DR EMBL; AK086760; BAC39738.1; -; mRNA.
DR EMBL; AK145882; BAE26722.1; -; mRNA.
DR EMBL; AK220194; BAD90379.1; ALT_INIT; mRNA.
DR EMBL; AL627215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079908; AAH79908.1; -; mRNA.
DR CCDS; CCDS24637.1; -.
DR RefSeq; NP_038950.3; NM_013922.4.
DR AlphaFoldDB; Q571J5; -.
DR SMR; Q571J5; -.
DR STRING; 10090.ENSMUSP00000104763; -.
DR iPTMnet; Q571J5; -.
DR PhosphoSitePlus; Q571J5; -.
DR SwissPalm; Q571J5; -.
DR MaxQB; Q571J5; -.
DR PaxDb; Q571J5; -.
DR PeptideAtlas; Q571J5; -.
DR PRIDE; Q571J5; -.
DR ProteomicsDB; 275259; -.
DR Antibodypedia; 29471; 47 antibodies from 13 providers.
DR DNASU; 30944; -.
DR Ensembl; ENSMUST00000000632; ENSMUSP00000000632; ENSMUSG00000044807.
DR Ensembl; ENSMUST00000109135; ENSMUSP00000104763; ENSMUSG00000044807.
DR GeneID; 30944; -.
DR KEGG; mmu:30944; -.
DR UCSC; uc007isq.1; mouse.
DR CTD; 30944; -.
DR MGI; MGI:1353621; Zfp354c.
DR VEuPathDB; HostDB:ENSMUSG00000044807; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162715; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q571J5; -.
DR OMA; STFIEHQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q571J5; -.
DR TreeFam; TF350822; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 30944; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q571J5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q571J5; protein.
DR Bgee; ENSMUSG00000044807; Expressed in embryonic brain and 211 other tissues.
DR Genevisible; Q571J5; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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 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 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..560
FT /note="Zinc finger protein 354C"
FT /id="PRO_0000280409"
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..168
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"
FT CONFLICT 77
FT /note="E -> K (in Ref. 2; BAC39738)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="E -> K (in Ref. 2; BAE26722)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="G -> D (in Ref. 2; BAE26722)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> P (in Ref. 2; BAE26722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 64065 MW; A348B1C5C9392A22 CRC64;
MAVDLLAARG TEPVTFRDVA VSFSQDEWLH LDPAQRSLYR EVMLENYSNL ASLGFQASIP
PVIGKLQKGQ DPCMEREAPE DTCLDFEIWP EIEALPPKQD VLTKETSHGL IKNGSTKCVY
WKISFGELVK TECRDIAQEQ EKKVHGPGAE SPKETTSEDG TPTGFEPEKP LFISKALVSQ
EGDPTESVPA TYHTSEKDLP QDFDLMRSFQ MYPGQKPHVC SECGKGFTQS LHLLEHKRLH
TGEKPYKCSE CGKSFSHRSS LLAHQRTHTG EKPYKCSECE KAFGSSSTLI KHLRVHTGEK
PYRCRQCGKA FSQCSTLTVH QRIHTGEKLY KCAECDKAFN CRAKLHRHQR IHTGEKPYKC
AECGKGYSQF PSLAEHQRLH TGEQLCQCLQ CGRTFTRVST LIEHQRIHTG QKPYQCNECG
KTFNQYSSFN EHRKIHTGEK LYTCEECGKA FGCKSNLYRH QRIHTGEKPY QCNQCGKAFS
QYSFLTEHER IHTGEKLYKC MECGKAYSYR SNLCRHKKVH LKERLYKWKE YGTPFIYGSS
LTPYQKFLKG DKPENFNSSL
