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 01-MAY-2013, entry version 99.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Transcriptional factor that binds to the consensus
CC sequence 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of
CC autophagy. Specifically represses expression of genes involved in
CC autophagy and lysosome biogenesis/function such as MAP1LC3B, ULK1
CC or WIPI2. Associates with chromatin at the ITGB4 and VEGF
CC promoters (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC similarity). 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).
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung,
CC liver, skeletal muscle, kidney and testis.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family.
CC -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC -!- SIMILARITY: Contains 1 KRAB domain.
CC -!- SIMILARITY: Contains 1 SCAN box domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00602.1; Type=Frameshift; Positions=421, 432;
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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 IPI; IPI00228736; -.
DR RefSeq; NP_001139250.1; NM_001145778.1.
DR RefSeq; NP_076174.3; NM_023685.4.
DR UniGene; Mm.296071; -.
DR HSSP; P08047; 1SP2.
DR ProteinModelPortal; Q91VW9; -.
DR SMR; Q91VW9; 43-135, 281-533.
DR STRING; 10090.ENSMUSP00000112135; -.
DR PRIDE; Q91VW9; -.
DR Ensembl; ENSMUST00000070785; ENSMUSP00000068424; ENSMUSG00000021327.
DR Ensembl; ENSMUST00000116434; ENSMUSP00000112135; ENSMUSG00000021327.
DR GeneID; 72739; -.
DR KEGG; mmu:72739; -.
DR UCSC; uc007pqg.2; mouse.
DR CTD; 80317; -.
DR MGI; MGI:1919989; Zkscan3.
DR eggNOG; COG5048; -.
DR GeneTree; ENSGT00700000104203; -.
DR HOGENOM; HOG000234619; -.
DR HOVERGEN; HBG018163; -.
DR InParanoid; Q91VW9; -.
DR KO; K09229; -.
DR OrthoDB; EOG4H19VD; -.
DR NextBio; 336842; -.
DR ArrayExpress; Q91VW9; -.
DR Bgee; Q91VW9; -.
DR Genevestigator; Q91VW9; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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-dependent; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral reproduction; IEA:InterPro.
DR Gene3D; 3.30.160.60; -; 7.
DR InterPro; IPR001909; Krueppel-associated_box.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR003309; Tscrpt_reg_SCAN.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF02023; SCAN; 1.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; Krueppel-associated_box; 1.
DR SUPFAM; SSF47353; Retrov_capsid_C; 1.
DR PROSITE; PS50805; KRAB; FALSE_NEG.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW Activator; Autophagy; Complete proteome; Cytoplasm; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 553 Zinc finger protein with KRAB and SCAN
FT domains 3.
FT /FTId=PRO_0000394861.
FT DOMAIN 51 133 SCAN box.
FT DOMAIN 213 273 KRAB.
FT ZN_FING 313 335 C2H2-type 1.
FT ZN_FING 341 363 C2H2-type 2.
FT ZN_FING 369 391 C2H2-type 3.
FT ZN_FING 397 419 C2H2-type 4.
FT ZN_FING 425 447 C2H2-type 5.
FT ZN_FING 479 501 C2H2-type 6.
FT ZN_FING 507 529 C2H2-type 7.
FT CONFLICT 32 32 S -> A (in Ref. 2; BAC27333/BAE20446).
FT CONFLICT 62 62 A -> T (in Ref. 1; AAG00602).
FT CONFLICT 67 67 Q -> R (in Ref. 2; BAE20446).
FT CONFLICT 538 538 V -> M (in Ref. 1; AAG00602).
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
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