KCTD8_MOUSE
ID KCTD8_MOUSE Reviewed; 476 AA.
AC Q50H33; Q8BR74; Q8C4C2; Q8C906; Q8C9B0; Q8CAA9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=BTB/POZ domain-containing protein KCTD8;
GN Name=Kctd8;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Odeh H.M., Mitchem K.L., Kohrman D.C.;
RT "Conserved paralogous segments on mouse chromosome 5 and 18.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Hypothalamus;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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).
RN [5]
RP FUNCTION, INTERACTION WITH GABRB1 AND GABRB2, AND TETRAMERIZATION.
RX PubMed=20400944; DOI=10.1038/nature08964;
RA Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA Bettler B.;
RT "Native GABA(B) receptors are heteromultimers with a family of auxiliary
RT subunits.";
RL Nature 465:231-235(2010).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Auxiliary subunit of GABA-B receptors that determine the
CC pharmacology and kinetics of the receptor response. Increases agonist
CC potency and markedly alter the G-protein signaling of the receptors by
CC accelerating onset and promoting desensitization.
CC {ECO:0000269|PubMed:20400944}.
CC -!- SUBUNIT: Interacts as a tetramer with GABRB1 and GABRB2.
CC {ECO:0000269|PubMed:20400944}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250}.
CC Postsynaptic cell membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q50H33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q50H33-2; Sequence=VSP_020761, VSP_020762;
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DR EMBL; AY615967; AAU25822.1; -; mRNA.
DR EMBL; AK039167; BAC30262.2; -; mRNA.
DR EMBL; AK042569; BAC31296.1; -; mRNA.
DR EMBL; AK043351; BAC31527.1; -; mRNA.
DR EMBL; AK045439; BAC32368.1; -; mRNA.
DR EMBL; AK082563; BAC38532.1; -; mRNA.
DR EMBL; BC116940; AAI16941.1; -; mRNA.
DR EMBL; BC116942; AAI16943.1; -; mRNA.
DR CCDS; CCDS19320.1; -. [Q50H33-1]
DR RefSeq; NP_780728.3; NM_175519.5. [Q50H33-1]
DR AlphaFoldDB; Q50H33; -.
DR SMR; Q50H33; -.
DR BioGRID; 232480; 3.
DR CORUM; Q50H33; -.
DR IntAct; Q50H33; 1.
DR MINT; Q50H33; -.
DR STRING; 10090.ENSMUSP00000055326; -.
DR ChEMBL; CHEMBL4523317; -.
DR iPTMnet; Q50H33; -.
DR PhosphoSitePlus; Q50H33; -.
DR MaxQB; Q50H33; -.
DR PaxDb; Q50H33; -.
DR PeptideAtlas; Q50H33; -.
DR PRIDE; Q50H33; -.
DR ProteomicsDB; 263513; -. [Q50H33-1]
DR ProteomicsDB; 263514; -. [Q50H33-2]
DR Antibodypedia; 23721; 84 antibodies from 16 providers.
DR DNASU; 243043; -.
DR Ensembl; ENSMUST00000054095; ENSMUSP00000055326; ENSMUSG00000037653. [Q50H33-1]
DR Ensembl; ENSMUST00000087231; ENSMUSP00000084484; ENSMUSG00000037653. [Q50H33-2]
DR GeneID; 243043; -.
DR KEGG; mmu:243043; -.
DR UCSC; uc008xqj.1; mouse. [Q50H33-1]
DR CTD; 386617; -.
DR MGI; MGI:2443804; Kctd8.
DR VEuPathDB; HostDB:ENSMUSG00000037653; -.
DR eggNOG; KOG2723; Eukaryota.
DR GeneTree; ENSGT00940000161041; -.
DR HOGENOM; CLU_057051_1_0_1; -.
DR InParanoid; Q50H33; -.
DR OMA; MFSPCRG; -.
DR OrthoDB; 1579292at2759; -.
DR PhylomeDB; Q50H33; -.
DR TreeFam; TF315332; -.
DR BioGRID-ORCS; 243043; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Kctd8; mouse.
DR PRO; PR:Q50H33; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q50H33; protein.
DR Bgee; ENSMUSG00000037653; Expressed in habenula and 95 other tissues.
DR Genevisible; Q50H33; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IGI:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR Pfam; PF02214; BTB_2; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Membrane;
KW Methylation; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Synapse.
FT CHAIN 1..476
FT /note="BTB/POZ domain-containing protein KCTD8"
FT /id="PRO_0000251482"
FT DOMAIN 44..122
FT /note="BTB"
FT REGION 331..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 80
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 325..346
FT /note="PPQKIVSPKQEHEDRKRDKVTD -> KETAQRNCFSHFIHHMRVDGKA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020761"
FT VAR_SEQ 347..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020762"
FT CONFLICT 45
FT /note="V -> I (in Ref. 2; BAC31296)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..83
FT /note="GA -> RAP (in Ref. 2; BAC31296)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="K -> E (in Ref. 2; BAC38532)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="E -> K (in Ref. 2; BAC30262)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="D -> Y (in Ref. 2; BAC32368)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> Y (in Ref. 2; BAC32368)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="N -> K (in Ref. 2; BAC31527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52768 MW; 26EC9C5A673A53DF CRC64;
MALKDTGSGG STILPISEMV SASSSPGAPL AAAPGPCAPS PFPEVVELNV GGQVYVTKHS
TLLSVPDSTL ASMFSPSSPR GGARRRGDLP RDSRARFFID RDGFLFRYVL DYLRDKQLAL
PEHFPEKERL LREAEFFQLT DLVKLLSPKV TKQNSLNDEC CQSDLEDNVS QGSSDALLLR
GAAAGAPSGS GAHGVSGVVG GGSAPDKRSG FLTLGYRGSY TTVRDNQADA KFRRVARIMV
CGRIALAKEV FGDTLNESRD PDRQPEKYTS RFYLKFTYLE QAFDRLSEAG FHMVACNSSG
TAAFVNQYRD DKIWSSYTEY IFFRPPQKIV SPKQEHEDRK RDKVTDKGSE SGTSCNELST
SSCDSHSEAS TPQDNPANTQ QAAAHQPNTL TLDRPSRKAP VQWMPPPDKR RNSELFQSLI
SKSRETNLSK KKVCEKLSVE EEMKKCIQDF KKIHIPDCFP ERKRQWQSEL LQKYGL
