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SNAI3_MOUSE
ID   SNAI3_MOUSE             Reviewed;         287 AA.
AC   Q9QY31; Q3U3U2; Q496S5; Q8C244;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Zinc finger protein SNAI3;
DE   AltName: Full=Protein snail homolog 3;
DE   AltName: Full=Snail-related gene from muscle cells;
DE   AltName: Full=Zinc finger protein 293;
GN   Name=Snai3; Synonyms=Smuc, Zfp293;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX   PubMed=10606664; DOI=10.1093/nar/28.2.626;
RA   Kataoka H., Murayama T., Yokode M., Mori S., Sano H., Ozaki H., Yokota Y.,
RA   Nishikawa S., Kita T.;
RT   "A novel snail-related transcription factor Smuc regulates basic helix-
RT   loop-helix transcription factor activities via specific E-box motifs.";
RL   Nucleic Acids Res. 28:626-633(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH;
RA   Seki K., Fujimori T., Nabeshima Y., Robertson E.J.;
RT   "Molecular cloning of a novel mouse snail-related gene.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Thymus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC   -!- FUNCTION: Seems to inhibit myoblast differentiation. Transcriptional
CC       repressor of E-box-dependent transactivation of downstream myogenic
CC       bHLHs genes. Binds preferentially to the canonical E-box sequences 5'-
CC       CAGGTG-3' and 5'-CACCTG-3'. {ECO:0000269|PubMed:10606664}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10606664}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and thymus.
CC       Lower expression in heart, lung and spleen.
CC       {ECO:0000269|PubMed:10606664}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 7 dpc, higher expression observed in
CC       stages 15 dpc and 18 dpc. {ECO:0000269|PubMed:10606664}.
CC   -!- DOMAIN: Binds E-box via C2H2-type zinc finger domain.
CC   -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF133714; AAF22956.1; -; mRNA.
DR   EMBL; AF195655; AAQ13827.1; -; mRNA.
DR   EMBL; AK042234; BAC31201.1; -; mRNA.
DR   EMBL; AK089285; BAC40828.1; -; mRNA.
DR   EMBL; AK153633; BAE32128.1; -; mRNA.
DR   EMBL; AK154585; BAE32693.1; -; mRNA.
DR   EMBL; BC100724; AAI00725.1; -; mRNA.
DR   EMBL; BC100726; AAI00727.1; -; mRNA.
DR   EMBL; BC100727; AAI00728.1; -; mRNA.
DR   CCDS; CCDS22739.1; -.
DR   RefSeq; NP_038942.1; NM_013914.2.
DR   AlphaFoldDB; Q9QY31; -.
DR   SMR; Q9QY31; -.
DR   STRING; 10090.ENSMUSP00000006762; -.
DR   PhosphoSitePlus; Q9QY31; -.
DR   PaxDb; Q9QY31; -.
DR   PRIDE; Q9QY31; -.
DR   ProteomicsDB; 261591; -.
DR   Antibodypedia; 17289; 131 antibodies from 26 providers.
DR   DNASU; 30927; -.
DR   Ensembl; ENSMUST00000006762; ENSMUSP00000006762; ENSMUSG00000006587.
DR   GeneID; 30927; -.
DR   KEGG; mmu:30927; -.
DR   UCSC; uc009nsw.1; mouse.
DR   CTD; 333929; -.
DR   MGI; MGI:1353563; Snai3.
DR   VEuPathDB; HostDB:ENSMUSG00000006587; -.
DR   eggNOG; KOG2462; Eukaryota.
DR   GeneTree; ENSGT00940000154511; -.
DR   HOGENOM; CLU_002678_42_3_1; -.
DR   InParanoid; Q9QY31; -.
DR   OMA; PWDRSSA; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9QY31; -.
DR   TreeFam; TF315515; -.
DR   BioGRID-ORCS; 30927; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Snai3; mouse.
DR   PRO; PR:Q9QY31; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9QY31; protein.
DR   Bgee; ENSMUSG00000006587; Expressed in epithelium of urethra and 74 other tissues.
DR   Genevisible; Q9QY31; MM.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..287
FT                   /note="Zinc finger protein SNAI3"
FT                   /id="PRO_0000330038"
FT   ZN_FING         147..169
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         178..200
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         204..226
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         232..254
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         260..282
FT                   /note="C2H2-type 5; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..20
FT                   /note="SNAG domain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        75
FT                   /note="N -> S (in Ref. 4; AAI00727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="H -> Y (in Ref. 3; BAC40828)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  31636 MW;  02E42A6FE8BAFD48 CRC64;
     MPRSFLVKTH SSHRVPNYGK LETLREANGS CSACKELAGS RHLPDEEAPC NPSDPLQPWD
     STSAVACISL PLLPNHRETL GVSGPEPQET SWVGPRAAQA PSVTLKDSFT LPPLLVLPTR
     WPPILGPDGA LNEHLRAEGT SRVPGSFECI HCHRPYHTLA GLARHQQLHC HLPTGRAFTC
     RYCDKEYASL GALKMHIRTH TLPCICKVCG KAFSRPWLLQ GHIRTHTGEK PYTCSHCSRA
     FADRSNLRAH LQTHVGTKKY RCAVCPKAFS RMSLLARHEE AGCCPGP
 
 
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