KCD17_HUMAN
ID KCD17_HUMAN Reviewed; 321 AA.
AC Q8N5Z5; B0QYA9; B0QYB0; O95517;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=BTB/POZ domain-containing protein KCTD17;
GN Name=KCTD17;
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 GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-321 (ISOFORMS 1 AND 2), AND
RP VARIANT GLY-51.
RC TISSUE=Brain, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-321 (ISOFORM 2).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP FUNCTION, INTERACTION WITH TCHP AND CUL3, AND SUBUNIT.
RX PubMed=25270598; DOI=10.1038/ncomms6081;
RA Kasahara K., Kawakami Y., Kiyono T., Yonemura S., Kawamura Y., Era S.,
RA Matsuzaki F., Goshima N., Inagaki M.;
RT "Ubiquitin-proteasome system controls ciliogenesis at the initial step of
RT axoneme extension.";
RL Nat. Commun. 5:5081-5081(2014).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN DYT26,
RP VARIANT DYT26 HIS-145, AND CHARACTERIZATION OF VARIANT DYT26 HIS-145.
RX PubMed=25983243; DOI=10.1016/j.ajhg.2015.04.008;
RA Mencacci N.E., Rubio-Agusti I., Zdebik A., Asmus F., Ludtmann M.H.,
RA Ryten M., Plagnol V., Hauser A.K., Bandres-Ciga S., Bettencourt C.,
RA Forabosco P., Hughes D., Soutar M.M., Peall K., Morris H.R., Trabzuni D.,
RA Tekman M., Stanescu H.C., Kleta R., Carecchio M., Zorzi G., Nardocci N.,
RA Garavaglia B., Lohmann E., Weissbach A., Klein C., Hardy J., Pittman A.M.,
RA Foltynie T., Abramov A.Y., Gasser T., Bhatia K.P., Wood N.W.;
RT "A missense mutation in KCTD17 causes autosomal dominant myoclonus-
RT dystonia.";
RL Am. J. Hum. Genet. 96:938-947(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 20-131, 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: Is a positive regulator of ciliogenesis, playing a crucial
CC role in the initial steps of axoneme extension. It acts as a substrate-
CC adapter for CUL3-RING ubiquitin ligase complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of TCHP, a
CC protein involved in ciliogenesis down-regulation (PubMed:25270598). May
CC be involved in endoplasmic reticulum calcium ion homeostasis
CC (PubMed:25983243). {ECO:0000269|PubMed:25270598,
CC ECO:0000269|PubMed:25983243}.
CC -!- SUBUNIT: Homopentamer; forms an closed pentamer (PubMed:28963344).
CC Interacts with CUL3; interaction is direct and forms a 5:5
CC heterodecamer (PubMed:28963344). Interacts with TCHP (PubMed:25270598).
CC Interacts with CUL3, as part of the BCR(KCTD17) E3 ubiquitin ligase
CC complex, at least composed of CUL3, KCTD17 and RBX1 (PubMed:25270598).
CC {ECO:0000269|PubMed:25270598, ECO:0000269|PubMed:28963344}.
CC -!- INTERACTION:
CC Q8N5Z5; P02768-3: ALB; NbExp=3; IntAct=EBI-743960, EBI-25830928;
CC Q8N5Z5; Q92870-2: APBB2; NbExp=3; IntAct=EBI-743960, EBI-21535880;
CC Q8N5Z5; P55212: CASP6; NbExp=3; IntAct=EBI-743960, EBI-718729;
CC Q8N5Z5; P28329-3: CHAT; NbExp=3; IntAct=EBI-743960, EBI-25837549;
CC Q8N5Z5; O94985-2: CLSTN1; NbExp=3; IntAct=EBI-743960, EBI-16041593;
CC Q8N5Z5; P99999: CYCS; NbExp=3; IntAct=EBI-743960, EBI-446479;
CC Q8N5Z5; Q14565: DMC1; NbExp=4; IntAct=EBI-743960, EBI-930865;
CC Q8N5Z5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-743960, EBI-10976677;
CC Q8N5Z5; O95363: FARS2; NbExp=3; IntAct=EBI-743960, EBI-2513774;
CC Q8N5Z5; P22607: FGFR3; NbExp=3; IntAct=EBI-743960, EBI-348399;
CC Q8N5Z5; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-743960, EBI-10226858;
CC Q8N5Z5; P21333-2: FLNA; NbExp=3; IntAct=EBI-743960, EBI-9641086;
CC Q8N5Z5; P06396: GSN; NbExp=3; IntAct=EBI-743960, EBI-351506;
CC Q8N5Z5; O00291: HIP1; NbExp=3; IntAct=EBI-743960, EBI-473886;
CC Q8N5Z5; P54652: HSPA2; NbExp=3; IntAct=EBI-743960, EBI-356991;
CC Q8N5Z5; O43464: HTRA2; NbExp=3; IntAct=EBI-743960, EBI-517086;
CC Q8N5Z5; P42858: HTT; NbExp=3; IntAct=EBI-743960, EBI-466029;
CC Q8N5Z5; Q92993: KAT5; NbExp=3; IntAct=EBI-743960, EBI-399080;
CC Q8N5Z5; Q8N5Z5: KCTD17; NbExp=2; IntAct=EBI-743960, EBI-743960;
CC Q8N5Z5; P13473-2: LAMP2; NbExp=3; IntAct=EBI-743960, EBI-21591415;
CC Q8N5Z5; O43561-2: LAT; NbExp=3; IntAct=EBI-743960, EBI-8070286;
CC Q8N5Z5; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-743960, EBI-11742507;
CC Q8N5Z5; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-743960, EBI-473196;
CC Q8N5Z5; O43639: NCK2; NbExp=3; IntAct=EBI-743960, EBI-713635;
CC Q8N5Z5; Q8TCB6: OR51E1; NbExp=3; IntAct=EBI-743960, EBI-12141505;
CC Q8N5Z5; Q16512: PKN1; NbExp=3; IntAct=EBI-743960, EBI-602382;
CC Q8N5Z5; D3DTS7: PMP22; NbExp=3; IntAct=EBI-743960, EBI-25882629;
CC Q8N5Z5; P62937-2: PPIA; NbExp=3; IntAct=EBI-743960, EBI-25884072;
CC Q8N5Z5; P23284: PPIB; NbExp=3; IntAct=EBI-743960, EBI-359252;
CC Q8N5Z5; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-743960, EBI-5280197;
CC Q8N5Z5; P41219: PRPH; NbExp=3; IntAct=EBI-743960, EBI-752074;
CC Q8N5Z5; P63000: RAC1; NbExp=3; IntAct=EBI-743960, EBI-413628;
CC Q8N5Z5; P62826: RAN; NbExp=3; IntAct=EBI-743960, EBI-286642;
CC Q8N5Z5; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-743960, EBI-9090795;
CC Q8N5Z5; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-743960, EBI-2623095;
CC Q8N5Z5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-743960, EBI-5235340;
CC Q8N5Z5; O75716: STK16; NbExp=9; IntAct=EBI-743960, EBI-749295;
CC Q8N5Z5; Q9H5I1: SUV39H2; NbExp=2; IntAct=EBI-743960, EBI-723127;
CC Q8N5Z5; Q13148: TARDBP; NbExp=6; IntAct=EBI-743960, EBI-372899;
CC Q8N5Z5; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-743960, EBI-717399;
CC Q8N5Z5; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-743960, EBI-741480;
CC Q8N5Z5; P31930: UQCRC1; NbExp=3; IntAct=EBI-743960, EBI-1052596;
CC Q8N5Z5; P61981: YWHAG; NbExp=3; IntAct=EBI-743960, EBI-359832;
CC Q8N5Z5; Q96BH6; NbExp=3; IntAct=EBI-743960, EBI-25872486;
CC Q8N5Z5-2; O75716: STK16; NbExp=3; IntAct=EBI-10189368, EBI-749295;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25983243}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N5Z5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5Z5-2; Sequence=VSP_020072;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Highest expression is
CC observed in the putamen and the thalamus.
CC {ECO:0000269|PubMed:25983243}.
CC -!- DISEASE: Dystonia 26, myoclonic (DYT26) [MIM:616398]: A form of
CC dystonia, a disorder defined by the presence of sustained involuntary
CC muscle contraction, often leading to abnormal postures. DYT26 is an
CC autosomal dominant, progressive disorder characterized by a combination
CC of non-epileptic myoclonic jerks and dystonia. Affected individuals
CC manifest myoclonic jerks in the upper limbs during the first or second
CC decade of life, and later develop dystonia with predominant involvement
CC of the craniocervical regions and sometimes the trunk and/or lower
CC limbs. {ECO:0000269|PubMed:25983243}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25403.1; Type=Miscellaneous discrepancy; Note=The sequence differs in the N-terminus for unknown reasons.; Evidence={ECO:0000305};
CC Sequence=AAH31038.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL022314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60139.1; -; Genomic_DNA.
DR EMBL; BC025403; AAH25403.1; ALT_SEQ; mRNA.
DR EMBL; BC031038; AAH31038.1; ALT_INIT; mRNA.
DR EMBL; AK022304; BAB14007.1; -; mRNA.
DR RefSeq; NP_001269613.1; NM_001282684.1. [Q8N5Z5-1]
DR RefSeq; NP_001269614.1; NM_001282685.1.
DR RefSeq; NP_001269615.1; NM_001282686.1.
DR RefSeq; NP_078957.2; NM_024681.3. [Q8N5Z5-2]
DR PDB; 5A6R; X-ray; 2.85 A; A/B/C/D/E=20-131.
DR PDBsum; 5A6R; -.
DR AlphaFoldDB; Q8N5Z5; -.
DR SMR; Q8N5Z5; -.
DR BioGRID; 122848; 125.
DR IntAct; Q8N5Z5; 94.
DR MINT; Q8N5Z5; -.
DR STRING; 9606.ENSP00000385096; -.
DR iPTMnet; Q8N5Z5; -.
DR PhosphoSitePlus; Q8N5Z5; -.
DR BioMuta; KCTD17; -.
DR DMDM; 205371782; -.
DR EPD; Q8N5Z5; -.
DR jPOST; Q8N5Z5; -.
DR MassIVE; Q8N5Z5; -.
DR MaxQB; Q8N5Z5; -.
DR PeptideAtlas; Q8N5Z5; -.
DR PRIDE; Q8N5Z5; -.
DR ProteomicsDB; 72116; -. [Q8N5Z5-1]
DR ProteomicsDB; 72117; -. [Q8N5Z5-2]
DR Antibodypedia; 11878; 119 antibodies from 20 providers.
DR DNASU; 79734; -.
DR Ensembl; ENST00000402077.8; ENSP00000384391.4; ENSG00000100379.18.
DR Ensembl; ENST00000403888.8; ENSP00000385096.4; ENSG00000100379.18.
DR GeneID; 79734; -.
DR KEGG; hsa:79734; -.
DR UCSC; uc010gxb.5; human. [Q8N5Z5-1]
DR CTD; 79734; -.
DR DisGeNET; 79734; -.
DR GeneCards; KCTD17; -.
DR HGNC; HGNC:25705; KCTD17.
DR HPA; ENSG00000100379; Tissue enhanced (brain).
DR MalaCards; KCTD17; -.
DR MIM; 616386; gene.
DR MIM; 616398; phenotype.
DR neXtProt; NX_Q8N5Z5; -.
DR Orphanet; 36899; Myoclonus-dystonia syndrome.
DR PharmGKB; PA142671638; -.
DR VEuPathDB; HostDB:ENSG00000100379; -.
DR eggNOG; KOG2715; Eukaryota.
DR HOGENOM; CLU_070830_2_0_1; -.
DR InParanoid; Q8N5Z5; -.
DR OMA; SCHACCY; -.
DR OrthoDB; 1333587at2759; -.
DR PhylomeDB; Q8N5Z5; -.
DR TreeFam; TF313754; -.
DR PathwayCommons; Q8N5Z5; -.
DR SignaLink; Q8N5Z5; -.
DR BioGRID-ORCS; 79734; 11 hits in 1069 CRISPR screens.
DR GenomeRNAi; 79734; -.
DR Pharos; Q8N5Z5; Tbio.
DR PRO; PR:Q8N5Z5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8N5Z5; protein.
DR Bgee; ENSG00000100379; Expressed in putamen and 162 other tissues.
DR ExpressionAtlas; Q8N5Z5; baseline and differential.
DR Genevisible; Q8N5Z5; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR GO; GO:0097602; F:cullin family protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
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; Alternative splicing; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Disease variant; Dystonia; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..321
FT /note="BTB/POZ domain-containing protein KCTD17"
FT /id="PRO_0000247841"
FT DOMAIN 31..101
FT /note="BTB"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..246
FT /evidence="ECO:0000255"
FT COMPBIAS 219..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 245..268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020072"
FT VARIANT 51
FT /note="R -> G (in dbSNP:rs17852877)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027157"
FT VARIANT 145
FT /note="R -> H (in DYT26; does not affect cytoplasmic
FT subcellular location; dbSNP:rs786205860)"
FT /evidence="ECO:0000269|PubMed:25983243"
FT /id="VAR_073806"
FT CONFLICT 6
FT /note="P -> R (in Ref. 3; AAH31038)"
FT /evidence="ECO:0000305"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:5A6R"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5A6R"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:5A6R"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:5A6R"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5A6R"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5A6R"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:5A6R"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:5A6R"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:5A6R"
SQ SEQUENCE 321 AA; 35670 MW; DB80D4B4BD8CB7E7 CRC64;
MQTPRPAMRM EAGEAAPPAG AGGRAAGGWG KWVRLNVGGT VFLTTRQTLC REQKSFLSRL
CQGEELQSDR DETGAYLIDR DPTYFGPILN FLRHGKLVLD KDMAEEGVLE EAEFYNIGPL
IRIIKDRMEE KDYTVTQVPP KHVYRVLQCQ EEELTQMVST MSDGWRFEQL VNIGSSYNYG
SEDQAEFLCV VSKELHSTPN GLSSESSRKT KSTEEQLEEQ QQQEEEVEEV EVEQVQVEAD
AQEKAQSSQD PANLFSLPPL PPPPLPAGGS RPHPLRPEAE LAVRASPRPL ARPQSCHPCC
YKPEAPGCEA PDHLQGLGVP I
