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Database: UniProt
Entry: Q91VW9
LinkDB: Q91VW9
Original site: Q91VW9 
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   19-MAR-2014, entry version 107.
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   RefSeq; NP_001139250.1; NM_001145778.1.
DR   RefSeq; NP_076174.3; NM_023685.4.
DR   RefSeq; XP_006516852.1; XM_006516789.1.
DR   RefSeq; XP_006516853.1; XM_006516790.1.
DR   UniGene; Mm.296071; -.
DR   ProteinModelPortal; Q91VW9; -.
DR   SMR; Q91VW9; 43-135, 288-533.
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; ENSGT00740000114850; -.
DR   HOGENOM; HOG000234619; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q91VW9; -.
DR   KO; K09229; -.
DR   OrthoDB; EOG79GT5W; -.
DR   TreeFam; TF350830; -.
DR   NextBio; 336842; -.
DR   PRO; PR:Q91VW9; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; SSF109640; 1.
DR   SUPFAM; SSF47353; SSF47353; 1.
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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