ENC1_MOUSE
ID ENC1_MOUSE Reviewed; 589 AA.
AC O35709; Q8C7V2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ectoderm-neural cortex protein 1;
DE Short=ENC-1;
GN Name=Enc1; Synonyms=Enc-1;
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].
RC STRAIN=Swiss albino; TISSUE=Brain;
RX PubMed=9096139; DOI=10.1523/jneurosci.17-09-03038.1997;
RA Hernandez M.-C., Andres-Barquin P.J., Martinez S., Bulfone A.,
RA Rubenstein J.L.R., Israel M.A.;
RT "ENC-1: a novel mammalian kelch-related gene specifically expressed in the
RT nervous system encodes an actin-binding protein.";
RL J. Neurosci. 17:3038-3051(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and 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).
CC -!- FUNCTION: Actin-binding protein involved in the regulation of neuronal
CC process formation and in differentiation of neural crest cells. Down-
CC regulates transcription factor NF2L2/NRF2 by decreasing the rate of
CC protein synthesis and not via a ubiquitin-mediated proteasomal
CC degradation mechanism (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to RB1. Hypophosphorylated RB1 associates with ENC1
CC during neuronal differentiation, while hyperphosphorylated RB1
CC associates with ENC1 in undifferentiating cells. Part of a complex that
CC contains CUL3, RBX1 and ENC1 (By similarity). Interacts indirectly with
CC KEAP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm.
CC Cytoplasm, cytoskeleton. Note=Interacts with the actin cytoskeleton.
CC -!- TISSUE SPECIFICITY: Primarily expressed in the nervous system.
CC -!- DEVELOPMENTAL STAGE: Expression is highly dynamic but mostly restricted
CC to the nervous system. Outside the nervous system, expression is
CC detected in the rostral-most somitomere of the presomitic mesoderm, at
CC the times corresponding to the epithelialization that precedes somite
CC formation. First detected in the brain and spinal cord of 12 PC
CC embryos.
CC -!- PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and
CC RBX1 and probably targeted for proteasome-independent degradation.
CC Quinone-induced oxidative stress increases its ubiquitination (By
CC similarity). {ECO:0000250}.
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DR EMBL; U65079; AAB64206.1; -; mRNA.
DR EMBL; AK049187; BAC33597.1; -; mRNA.
DR EMBL; AK132173; BAE21011.1; -; mRNA.
DR EMBL; CH466567; EDL00871.1; -; Genomic_DNA.
DR EMBL; BC049186; AAH49186.1; -; mRNA.
DR EMBL; BC058098; AAH58098.1; -; mRNA.
DR CCDS; CCDS26710.1; -.
DR RefSeq; NP_031956.3; NM_007930.4.
DR AlphaFoldDB; O35709; -.
DR SMR; O35709; -.
DR BioGRID; 199448; 1.
DR STRING; 10090.ENSMUSP00000038783; -.
DR iPTMnet; O35709; -.
DR PhosphoSitePlus; O35709; -.
DR MaxQB; O35709; -.
DR PaxDb; O35709; -.
DR PeptideAtlas; O35709; -.
DR PRIDE; O35709; -.
DR ProteomicsDB; 275660; -.
DR Antibodypedia; 24333; 274 antibodies from 36 providers.
DR DNASU; 13803; -.
DR Ensembl; ENSMUST00000041623; ENSMUSP00000038783; ENSMUSG00000041773.
DR GeneID; 13803; -.
DR KEGG; mmu:13803; -.
DR UCSC; uc007rod.2; mouse.
DR CTD; 8507; -.
DR MGI; MGI:109610; Enc1.
DR VEuPathDB; HostDB:ENSMUSG00000041773; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00950000182983; -.
DR HOGENOM; CLU_004253_14_6_1; -.
DR InParanoid; O35709; -.
DR OMA; DSMKMSV; -.
DR OrthoDB; 709680at2759; -.
DR PhylomeDB; O35709; -.
DR TreeFam; TF329218; -.
DR BioGRID-ORCS; 13803; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Enc1; mouse.
DR PRO; PR:O35709; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O35709; protein.
DR Bgee; ENSMUSG00000041773; Expressed in barrel cortex and 269 other tissues.
DR Genevisible; O35709; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:InterPro.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR030562; ENC1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24410:SF5; PTHR24410:SF5; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 4.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW Kelch repeat; Nucleus; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..589
FT /note="Ectoderm-neural cortex protein 1"
FT /id="PRO_0000119069"
FT DOMAIN 46..114
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 296..340
FT /note="Kelch 1"
FT REPEAT 341..388
FT /note="Kelch 2"
FT REPEAT 389..444
FT /note="Kelch 3"
FT REPEAT 446..492
FT /note="Kelch 4"
FT REPEAT 494..538
FT /note="Kelch 5"
FT REPEAT 539..585
FT /note="Kelch 6"
FT CONFLICT 182
FT /note="N -> S (in Ref. 1; AAB64206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 66113 MW; 21EA2CA07EE66B86 CRC64;
MSVSVHENRK SRASSGSINI YLFHKSSYAD SVLTHLNLLR QQRLFTDVLL HAGNRTFPCH
RAVLAACSRY FEAMFSGGLK ESQDSEVNFD NSIHPEVLEL LLDYAYSSRV IINEENAESL
LEAGDMLEFQ DIRDACAEFL EKNLHPTNCL GMLLLSDAHQ CTKLYELSWR MCLSNFQTIR
KNEDFLQLPQ DMVVQLLSSE ELETEDERLV YESAMNWISY DLKKRYCYLP ELLQTVRLAL
LPAIYLMENV AMEELITKQR KSKEIVEEAI RCKLKILQND GVVTSLCARP RKTGHALFLL
GGQTFMCDKL YLVDQKAKEI IPKADIPSPR KEFSACAIGC KVYITGGRGS ENGVSKDVWV
YDTLHEEWSK AAPMLVARFG HGSAELKHCL YVVGGHTAAT GCLPASPSVS LKQVEQYDPT
TNKWTMVAPL REGVSNAAVV SAKLKLFAFG GTSVSHDKLP KVQCYDQCEN RWSVPATCPQ
PWRYTAAAVL GNQIFIMGGD TEFSACSAYK FNSETYQWTK VGDVTAKRMS CHAVASGNKL
YVVGGYFGIQ RCKTLDCYDP TLDVWNSITT VPYSLIPTAF VSTWKHLPS
