KCD12_MOUSE
ID KCD12_MOUSE Reviewed; 327 AA.
AC Q6WVG3; Q3T9E3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=BTB/POZ domain-containing protein KCTD12;
DE AltName: Full=Pfetin;
DE AltName: Full=Predominantly fetal expressed T1 domain;
GN Name=Kctd12; Synonyms=Pfet1;
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 [GENOMIC DNA].
RC STRAIN=Czech II;
RX PubMed=15357420; DOI=10.1007/s10162-003-4042-x;
RA Resendes B.L., Kuo S.F., Robertson N.G., Giersch A.B., Honrubia D.,
RA Ohara O., Adams J.C., Morton C.C.;
RT "Isolation from cochlea of a novel human intronless gene with predominant
RT fetal expression.";
RL J. Assoc. Res. Otolaryngol. 5:185-202(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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-153, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-173; THR-198 AND
RP SER-202, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [7]
RP FUNCTION, INTERACTION WITH GABRB1 AND GABRB2, TETRAMERIZATION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
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).
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
CC {ECO:0000269|PubMed:20400944}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:20400944}. Note=Colocalizes with GABRB1.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, mainly in the hippocampus
CC and cerebellum. {ECO:0000269|PubMed:20400944}.
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DR EMBL; AY267461; AAP92150.1; -; Genomic_DNA.
DR EMBL; AK172581; BAE43079.1; -; mRNA.
DR CCDS; CCDS70611.1; -.
DR RefSeq; NP_808383.3; NM_177715.4.
DR AlphaFoldDB; Q6WVG3; -.
DR SMR; Q6WVG3; -.
DR BioGRID; 232062; 15.
DR CORUM; Q6WVG3; -.
DR IntAct; Q6WVG3; 3.
DR MINT; Q6WVG3; -.
DR STRING; 10090.ENSMUSP00000139261; -.
DR ChEMBL; CHEMBL4523353; -.
DR iPTMnet; Q6WVG3; -.
DR PhosphoSitePlus; Q6WVG3; -.
DR SwissPalm; Q6WVG3; -.
DR EPD; Q6WVG3; -.
DR jPOST; Q6WVG3; -.
DR MaxQB; Q6WVG3; -.
DR PeptideAtlas; Q6WVG3; -.
DR PRIDE; Q6WVG3; -.
DR ProteomicsDB; 269186; -.
DR DNASU; 239217; -.
DR GeneID; 239217; -.
DR KEGG; mmu:239217; -.
DR UCSC; uc007uwe.1; mouse.
DR CTD; 115207; -.
DR MGI; MGI:2145823; Kctd12.
DR eggNOG; KOG2723; Eukaryota.
DR InParanoid; Q6WVG3; -.
DR OrthoDB; 1579292at2759; -.
DR PhylomeDB; Q6WVG3; -.
DR BioGRID-ORCS; 239217; 1 hit in 66 CRISPR screens.
DR ChiTaRS; Kctd12; mouse.
DR PRO; PR:Q6WVG3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6WVG3; protein.
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; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO: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 Acetylation; Cell membrane; Cell projection; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96CX2"
FT CHAIN 2..327
FT /note="BTB/POZ domain-containing protein KCTD12"
FT /id="PRO_0000191296"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96CX2"
FT MOD_RES 119
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CX2"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 7
FT /note="A -> T (in Ref. 2; BAE43079)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="F -> L (in Ref. 2; BAE43079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 35892 MW; 0C84A1AB0CDFEAF5 CRC64;
MALADSARGL PNGGGGGGGS GSSSSSAEPP LFPDIVELNV GGQVYVTRRC TVVSVPDSLL
WRMFTQQQPQ ELARDSKGRF FLDRDGFFFR YILDYLRDLQ LVLPDYFPER SRLQREAEYF
ELPELVRRLG APQQPGPGPP PPHSRRGVHK EGSLGDELLP LGYAEPEPQE GASAGAPSPT
LELASRSPSG GAAGPLLTPS QSLDGSRRSG YITIGYRGSY TIGRDAQADA KFRRVARITV
CGKTSLAKEV FGDTLNESRD PDRPPERYTS RYYLKFNFLE QAFDKLSESG FHMVACSSTG
TCAFASSTDQ SEDKIWTSYT EYVFCRE
