ZKSC3_MOUSE
ID ZKSC3_MOUSE Reviewed; 553 AA.
AC Q91VW9; Q3V3Z2; Q8CD81; Q9ESY5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 3;
DE AltName: Full=SCAN-KRAB-zinc finger protein;
DE AltName: Full=Zinc finger protein 306;
DE AltName: Full=Zinc finger protein 307;
DE AltName: Full=Zinc finger protein 47 homolog;
DE Short=Zf47;
DE Short=Zfp-47;
GN Name=Zkscan3; Synonyms=Skz1, Zfp306, Zfp307, Zfp47;
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], AND TISSUE SPECIFICITY.
RC STRAIN=CD-1;
RX PubMed=11342224; DOI=10.1016/s0167-4781(00)00274-8;
RA Honer C., Chen P., Toth M.J., Schumacher C.;
RT "Identification of SCAN dimerization domains in four gene families.";
RL Biochim. Biophys. Acta 1517:441-448(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-44; THR-136 AND
RP SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcriptional factor that binds to the consensus sequence
CC 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of autophagy.
CC Specifically represses expression of genes involved in autophagy and
CC lysosome biogenesis/function such as MAP1LC3B, ULK1 or WIPI2.
CC Associates with chromatin at the ITGB4 and VEGF promoters (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC Cytoplasm {ECO:0000250}. Note=Mainly localizes in the nucleus. Under
CC starvation conditions translocates to the cytoplasm, allowing
CC expression of target genes involved in autophagy and lysosome
CC biogenesis/function (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:11342224}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00602.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF291722; AAG00602.1; ALT_FRAME; mRNA.
DR EMBL; AK028902; BAE20446.1; -; mRNA.
DR EMBL; AK031286; BAC27333.1; -; mRNA.
DR EMBL; CH466561; EDL32657.1; -; Genomic_DNA.
DR EMBL; CH466561; EDL32658.1; -; Genomic_DNA.
DR EMBL; CH466561; EDL32661.1; -; Genomic_DNA.
DR EMBL; BC007473; AAH07473.1; -; mRNA.
DR CCDS; CCDS26274.1; -.
DR RefSeq; NP_001139250.1; NM_001145778.1.
DR RefSeq; NP_076174.3; NM_023685.4.
DR RefSeq; XP_006516852.1; XM_006516789.3.
DR RefSeq; XP_006516853.1; XM_006516790.3.
DR AlphaFoldDB; Q91VW9; -.
DR SMR; Q91VW9; -.
DR STRING; 10090.ENSMUSP00000068424; -.
DR iPTMnet; Q91VW9; -.
DR PhosphoSitePlus; Q91VW9; -.
DR jPOST; Q91VW9; -.
DR MaxQB; Q91VW9; -.
DR PaxDb; Q91VW9; -.
DR PRIDE; Q91VW9; -.
DR ProteomicsDB; 274993; -.
DR DNASU; 72739; -.
DR GeneID; 72739; -.
DR KEGG; mmu:72739; -.
DR UCSC; uc007pqg.2; mouse.
DR CTD; 80317; -.
DR MGI; MGI:1919989; Zkscan3.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q91VW9; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q91VW9; -.
DR TreeFam; TF350830; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 72739; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Zkscan3; mouse.
DR PRO; PR:Q91VW9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91VW9; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Activator; Autophagy; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..553
FT /note="Zinc finger protein with KRAB and SCAN domains 3"
FT /id="PRO_0000394861"
FT DOMAIN 51..133
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 213..273
FT /note="KRAB"
FT ZN_FING 313..335
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..363
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..419
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 425..447
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 479..501
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 507..529
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRR0"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRR0"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BRR0"
FT CONFLICT 32
FT /note="S -> A (in Ref. 2; BAC27333/BAE20446)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="A -> T (in Ref. 1; AAG00602)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Q -> R (in Ref. 2; BAE20446)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="V -> M (in Ref. 1; AAG00602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 62642 MW; 53B41483D21AC3C8 CRC64;
MARESRESTT LDSHSAEDQM ELLVIKVEQE ESSPLAEETS WLGSPGPDRS RQRFRAFRYP
EAAGPRQALS RLRELCRQWL RPDMHSKEQI LELLVLEQFL TILPGELQAW VREQHPDSGE
EVVALLEYLD RQLDDTPPQV PDDDDGQELL CSKAVLLTSA QGSESSQMEP VEPLLKQESL
GSLPSEVRVT HVGHCGEDGV TATRLTSELQ GLLKMEDVAP VLSPRWTEQD SSQMNLYKDG
MQEHSGSLVS LDQDMQTKVR DLPRAEEYRD QKPEQTVCFL GEDTVPIPTG AEASEQEGKL
QAAQKSATGT RRFYCRECGK SFAQSSGLSK HKRIHTGLKP YECEECGKAF IGSSALIIHQ
RVHTGEKPYE CEECGKAFSH SSDLIKHQRT HTGEKPYECD DCGKTFTQSC SLLEHHRIHT
GEKPYQCNMC PKAFRRSSHL LRHQRTHTGD KDFFVPEPYW ESQSRVESHW ENIETPVSYQ
CNDCERSFSR ITSLIEHQKV HTGEKPFECQ TCGKGFTRPS YLIQHQRRHT GKKTSVTVTP
AVHSEVGVQL SLN
