KCD16_MOUSE
ID KCD16_MOUSE Reviewed; 427 AA.
AC Q5DTY9; Q78Y50;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=BTB/POZ domain-containing protein KCTD16;
GN Name=Kctd16; Synonyms=Gm1267, Kiaa1317;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-427.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-427.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-112, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-137; SER-143 AND
RP SER-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [6]
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: Homopentamer; forms an open pentamer (By similarity). In
CC contrast to other BTB domain-containing proteins, does not interact
CC with CUL3 (By similarity). Interacts as a tetramer with GABRB1 and
CC GABRB2 (PubMed:20400944). {ECO:0000250|UniProtKB:Q68DU8,
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 {ECO:0000269|PubMed:20400944}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, mainly in the hippocampus.
CC {ECO:0000269|PubMed:20400944}.
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DR EMBL; AC098707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220381; BAD90438.1; -; mRNA.
DR EMBL; AK005863; BAB24283.1; -; mRNA.
DR CCDS; CCDS50264.1; -.
DR RefSeq; NP_080411.1; NM_026135.1.
DR RefSeq; XP_017173425.1; XM_017317936.1.
DR RefSeq; XP_017173426.1; XM_017317937.1.
DR RefSeq; XP_017173427.1; XM_017317938.1.
DR RefSeq; XP_017173428.1; XM_017317939.1.
DR AlphaFoldDB; Q5DTY9; -.
DR SMR; Q5DTY9; -.
DR BioGRID; 238715; 5.
DR CORUM; Q5DTY9; -.
DR IntAct; Q5DTY9; 5.
DR MINT; Q5DTY9; -.
DR STRING; 10090.ENSMUSP00000089547; -.
DR ChEMBL; CHEMBL4523323; -.
DR iPTMnet; Q5DTY9; -.
DR PhosphoSitePlus; Q5DTY9; -.
DR SwissPalm; Q5DTY9; -.
DR MaxQB; Q5DTY9; -.
DR PaxDb; Q5DTY9; -.
DR PeptideAtlas; Q5DTY9; -.
DR PRIDE; Q5DTY9; -.
DR ProteomicsDB; 301759; -.
DR Antibodypedia; 45626; 85 antibodies from 16 providers.
DR DNASU; 383348; -.
DR Ensembl; ENSMUST00000091927; ENSMUSP00000089547; ENSMUSG00000051401.
DR Ensembl; ENSMUST00000236889; ENSMUSP00000158201; ENSMUSG00000051401.
DR GeneID; 383348; -.
DR KEGG; mmu:383348; -.
DR UCSC; uc012bch.1; mouse.
DR CTD; 57528; -.
DR MGI; MGI:1914659; Kctd16.
DR VEuPathDB; HostDB:ENSMUSG00000051401; -.
DR eggNOG; KOG2723; Eukaryota.
DR GeneTree; ENSGT00940000156071; -.
DR HOGENOM; CLU_057051_1_0_1; -.
DR InParanoid; Q5DTY9; -.
DR OMA; PKRDMAN; -.
DR OrthoDB; 1579292at2759; -.
DR PhylomeDB; Q5DTY9; -.
DR TreeFam; TF315332; -.
DR BioGRID-ORCS; 383348; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Kctd16; mouse.
DR PRO; PR:Q5DTY9; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q5DTY9; protein.
DR Bgee; ENSMUSG00000051401; Expressed in spermatid and 96 other tissues.
DR ExpressionAtlas; Q5DTY9; baseline and differential.
DR Genevisible; Q5DTY9; 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; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
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 Cell membrane; Cell projection; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..427
FT /note="BTB/POZ domain-containing protein KCTD16"
FT /id="PRO_0000248594"
FT DOMAIN 25..98
FT /note="BTB"
FT MOD_RES 112
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 317
FT /note="Q -> E (in Ref. 3; BAB24283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 48972 MW; C19AFA955BD30585 CRC64;
MALSGNCSRY YPRDQGAAVP NSFPEVIELN VGGQVYFTRH STLISIPHSL LWKMFSPKRD
TANDLAKDSK GRFFIDRDGF LFRYILDYLR DRQVVLPDHF PERGRLKREA EYFQLPDLVK
LLAPEDVKQS PDEFCHSDFE DASQGSDTRI CPPSSLLPHD RKWGFITVGY RGSCTLGREG
QADAKFRRVP RILVCGRISL AKEVFGETLN ESRDPDRAPE RYTSRFYLKF KHLERAFDML
SECGFHMVAC NSSVTASFVN QYTEDKIWSS YTEYVFYREP SRWSSSHCDC CCKNGKGDKG
ESGTSCNDLS TSSCDSQSEA SSPQETVICG PVTRQSNIQT LDRPIKKGPV QLIQQSEMRR
KSDLLRTLTS GSRESNISSK KKAAKEKLSI EEELEKCIQD FLKIKIPDRF PERKHPWQSE
LLRKYHL
