KLF16_MOUSE
ID KLF16_MOUSE Reviewed; 251 AA.
AC P58334; Q3U3Y4; Q8C8S2;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Krueppel-like factor 16;
DE AltName: Full=Basic transcription element-binding protein 4;
DE Short=BTE-binding protein 4;
DE AltName: Full=Dopamine receptor-regulating factor;
DE AltName: Full=Transcription factor BTEB4;
GN Name=Klf16; Synonyms=Bteb4, Drrf;
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 TISSUE=Neuroblastoma;
RX PubMed=11390978; DOI=10.1073/pnas.121635798;
RA Hwang C.K., D'Souza U.M., Eisch A.J., Yajima S., Lammers C.-H., Yang Y.,
RA Lee S.-H., Kim Y.-M., Nestler E.J., Mouradian M.M.;
RT "Dopamine receptor regulating factor, DRRF: a zinc finger transcription
RT factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7558-7563(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Retina;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
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: Transcription factor that binds GC and GT boxes in the D1A,
CC D2 and D3 dopamine receptor promoters and displaces Sp1 and Sp3 from
CC these sequences. It modulates dopaminergic transmission in the brain by
CC repressing or activating transcription from several different promoters
CC depending on cellular context.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: High expression in brain; olfactory tubercle,
CC olfactory bulb, nucleus accumbens, striatum, hippocampal CA1 region,
CC amygdala, dentate gyrus and frontal cortex. Moderate expression in
CC hippocampal CA2-3 regions, piriform cortex, septum, and distinct
CC thalamic nuclei. Low expression in the cerebellum.
CC -!- DOMAIN: The Ala/Pro-rich domain may contain discrete activation and
CC repression subdomains and also can mediate protein-protein
CC interactions.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF283891; AAK66968.1; -; mRNA.
DR EMBL; AK044577; BAC31987.1; -; mRNA.
DR EMBL; AK154524; BAE32651.1; -; mRNA.
DR CCDS; CCDS24026.1; -.
DR RefSeq; NP_510962.2; NM_078477.2.
DR AlphaFoldDB; P58334; -.
DR SMR; P58334; -.
DR BioGRID; 228243; 1.
DR STRING; 10090.ENSMUSP00000048825; -.
DR iPTMnet; P58334; -.
DR PhosphoSitePlus; P58334; -.
DR EPD; P58334; -.
DR MaxQB; P58334; -.
DR PaxDb; P58334; -.
DR PRIDE; P58334; -.
DR ProteomicsDB; 263648; -.
DR Antibodypedia; 22829; 195 antibodies from 28 providers.
DR DNASU; 118445; -.
DR Ensembl; ENSMUST00000038558; ENSMUSP00000048825; ENSMUSG00000035397.
DR GeneID; 118445; -.
DR KEGG; mmu:118445; -.
DR UCSC; uc007gdt.1; mouse.
DR CTD; 83855; -.
DR MGI; MGI:2153049; Klf16.
DR VEuPathDB; HostDB:ENSMUSG00000035397; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163280; -.
DR HOGENOM; CLU_002678_33_2_1; -.
DR InParanoid; P58334; -.
DR OMA; HRCTFNG; -.
DR OrthoDB; 1308225at2759; -.
DR PhylomeDB; P58334; -.
DR TreeFam; TF351003; -.
DR BioGRID-ORCS; 118445; 11 hits in 73 CRISPR screens.
DR ChiTaRS; Klf16; mouse.
DR PRO; PR:P58334; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P58334; protein.
DR Bgee; ENSMUSG00000035397; Expressed in humerus cartilage element and 222 other tissues.
DR ExpressionAtlas; P58334; baseline and differential.
DR Genevisible; P58334; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; 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; IBA:GO_Central.
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:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IDA: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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..251
FT /note="Krueppel-like factor 16"
FT /id="PRO_0000047159"
FT ZN_FING 126..150
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 156..180
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 186..208
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 48..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXK1"
SQ SEQUENCE 251 AA; 25652 MW; 3F0D7739BF7B1FA4 CRC64;
MSAAVACVDY FAADVLMAIS SGAVVHRGRP GPEGAGPAAG LDVRATRREA TPPGTPGAPP
PPATAPGPGG ATAAPHLLAA SILADLRGGP VVATAASTAG GTSPVSSSSA ASSPSSGRAP
GAAKSHRCPF HGCAKAYYKS SHLKSHLRTH TGERPFACDW PGCDKKFARS DELARHHRTH
TGEKRFPCPL CTKRFTRSDH LTKHARRHPG FRPELLRRPG ARSVSPSDSL PCSLAGSPTP
SPVPSPAPAG L
