KCD16_HUMAN
ID KCD16_HUMAN Reviewed; 428 AA.
AC Q68DU8; Q9P2M9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=BTB/POZ domain-containing protein KCTD16;
DE AltName: Full=Potassium channel tetramerization domain-containing protein 16;
GN Name=KCTD16; Synonyms=KIAA1317;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 16-133, AND SUBUNIT.
RX PubMed=28963344; DOI=10.1042/bcj20170527;
RA Pinkas D.M., Sanvitale C.E., Bufton J.C., Sorrell F.J., Solcan N.,
RA Chalk R., Doutch J., Bullock A.N.;
RT "Structural complexity in the KCTD family of Cullin3-dependent E3 ubiquitin
RT ligases.";
RL Biochem. J. 474:3747-3761(2017).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q5DTY9}.
CC -!- SUBUNIT: Homopentamer; forms an open pentamer (PubMed:28963344). In
CC contrast to other BTB domain-containing proteins, does not interact
CC with CUL3 (PubMed:28963344). Interacts as a tetramer with GABRB1 and
CC GABRB2. {ECO:0000250|UniProtKB:Q5DTY9, ECO:0000269|PubMed:28963344}.
CC -!- INTERACTION:
CC Q68DU8; P05067-4: APP; NbExp=3; IntAct=EBI-20768174, EBI-302641;
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane. Postsynaptic cell
CC membrane {ECO:0000250|UniProtKB:Q5DTY9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB037738; BAA92555.1; ALT_INIT; mRNA.
DR EMBL; CR749266; CAH18122.1; -; mRNA.
DR EMBL; BC111962; AAI11963.1; -; mRNA.
DR EMBL; BC113435; AAI13436.1; -; mRNA.
DR CCDS; CCDS34260.1; -.
DR RefSeq; NP_065819.1; NM_020768.3.
DR RefSeq; XP_005268549.1; XM_005268492.2.
DR RefSeq; XP_005268550.1; XM_005268493.2.
DR RefSeq; XP_006714852.1; XM_006714789.2.
DR RefSeq; XP_011535973.1; XM_011537671.2.
DR PDB; 5A15; X-ray; 2.76 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=16-133.
DR PDB; 6I0Q; X-ray; 2.30 A; A=22-124.
DR PDB; 6M8R; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J=23-124.
DR PDB; 6OCP; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=22-134.
DR PDB; 6OCR; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=22-134.
DR PDB; 6OCT; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=22-134.
DR PDB; 6QB7; X-ray; 2.23 A; A/B/C/D/E=126-286.
DR PDBsum; 5A15; -.
DR PDBsum; 6I0Q; -.
DR PDBsum; 6M8R; -.
DR PDBsum; 6OCP; -.
DR PDBsum; 6OCR; -.
DR PDBsum; 6OCT; -.
DR PDBsum; 6QB7; -.
DR AlphaFoldDB; Q68DU8; -.
DR SMR; Q68DU8; -.
DR BioGRID; 121587; 10.
DR CORUM; Q68DU8; -.
DR IntAct; Q68DU8; 2.
DR STRING; 9606.ENSP00000426548; -.
DR ChEMBL; CHEMBL4523340; -.
DR GuidetoPHARMACOLOGY; 1920; -.
DR GlyGen; Q68DU8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q68DU8; -.
DR PhosphoSitePlus; Q68DU8; -.
DR BioMuta; KCTD16; -.
DR DMDM; 74708941; -.
DR jPOST; Q68DU8; -.
DR MassIVE; Q68DU8; -.
DR MaxQB; Q68DU8; -.
DR PaxDb; Q68DU8; -.
DR PeptideAtlas; Q68DU8; -.
DR PRIDE; Q68DU8; -.
DR ProteomicsDB; 66102; -.
DR Antibodypedia; 45626; 85 antibodies from 16 providers.
DR DNASU; 57528; -.
DR Ensembl; ENST00000507359.3; ENSP00000426548.1; ENSG00000183775.11.
DR Ensembl; ENST00000512467.6; ENSP00000424151.1; ENSG00000183775.11.
DR GeneID; 57528; -.
DR KEGG; hsa:57528; -.
DR MANE-Select; ENST00000512467.6; ENSP00000424151.1; NM_020768.4; NP_065819.1.
DR UCSC; uc003lnm.2; human.
DR CTD; 57528; -.
DR DisGeNET; 57528; -.
DR GeneCards; KCTD16; -.
DR HGNC; HGNC:29244; KCTD16.
DR HPA; ENSG00000183775; Tissue enriched (brain).
DR MIM; 613423; gene.
DR neXtProt; NX_Q68DU8; -.
DR OpenTargets; ENSG00000183775; -.
DR PharmGKB; PA134973546; -.
DR VEuPathDB; HostDB:ENSG00000183775; -.
DR eggNOG; KOG2723; Eukaryota.
DR GeneTree; ENSGT00940000156071; -.
DR HOGENOM; CLU_057051_1_0_1; -.
DR InParanoid; Q68DU8; -.
DR OMA; PKRDMAN; -.
DR OrthoDB; 1579292at2759; -.
DR PhylomeDB; Q68DU8; -.
DR TreeFam; TF315332; -.
DR PathwayCommons; Q68DU8; -.
DR SignaLink; Q68DU8; -.
DR BioGRID-ORCS; 57528; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; KCTD16; human.
DR GenomeRNAi; 57528; -.
DR Pharos; Q68DU8; Tbio.
DR PRO; PR:Q68DU8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q68DU8; protein.
DR Bgee; ENSG00000183775; Expressed in Brodmann (1909) area 23 and 83 other tissues.
DR Genevisible; Q68DU8; HS.
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; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
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 3D-structure; Cell membrane; Cell projection; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..428
FT /note="BTB/POZ domain-containing protein KCTD16"
FT /id="PRO_0000248593"
FT DOMAIN 25..98
FT /note="BTB"
FT MOD_RES 112
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTY9"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTY9"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTY9"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTY9"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTY9"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:6OCR"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:6OCR"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:6OCR"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:6OCR"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6OCR"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6OCR"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:6OCR"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:6OCR"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:6OCR"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:6QB7"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6QB7"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:6QB7"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6QB7"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:6QB7"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:6QB7"
FT STRAND 246..260
FT /evidence="ECO:0007829|PDB:6QB7"
FT STRAND 266..278
FT /evidence="ECO:0007829|PDB:6QB7"
SQ SEQUENCE 428 AA; 49138 MW; 3D50005146B1383A CRC64;
MALSGNCSRY YPREQGSAVP NSFPEVVELN VGGQVYFTRH STLISIPHSL LWKMFSPKRD
TANDLAKDSK GRFFIDRDGF LFRYILDYLR DRQVVLPDHF PEKGRLKREA EYFQLPDLVK
LLTPDEIKQS PDEFCHSDFE DASQGSDTRI CPPSSLLPAD RKWGFITVGY RGSCTLGREG
QADAKFRRVP RILVCGRISL AKEVFGETLN ESRDPDRAPE RYTSRFYLKF KHLERAFDML
SECGFHMVAC NSSVTASFIN QYTDDKIWSS YTEYVFYREP SRWSPSHCDC CCKNGKGDKE
GESGTSCNDL STSSCDSQSE ASSPQETVIC GPVTRQTNIQ TLDRPIKKGP VQLIQQSEMR
RKSDLLRTLT SGSRESNMSS KKKAVKEKLS IEEELEKCIQ DFLKIKIPDR FPERKHPWQS
ELLRKYHL
