KCTD5_MOUSE
ID KCTD5_MOUSE Reviewed; 234 AA.
AC Q8VC57; Q3UPC0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=BTB/POZ domain-containing protein KCTD5;
GN Name=Kctd5;
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=129/SvJ;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 INTERACTION WITH CRY1.
RX PubMed=27123980; DOI=10.1371/journal.pone.0154263;
RA Hirano A., Nakagawa T., Yoshitane H., Oyama M., Kozuka-Hata H.,
RA Lanjakornsiripan D., Fukada Y.;
RT "USP7 and TDP-43: pleiotropic regulation of cryptochrome protein stability
RT paces the oscillation of the mammalian circadian clock.";
RL PLoS ONE 11:E0154263-E0154263(2016).
CC -!- FUNCTION: Its interaction with CUL3 suggests that it may act as a
CC substrate adapter in some E3 ligase complex (By similarity). Does not
CC affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2
CC and Kv3.4/KCNC4 (By similarity). {ECO:0000250|UniProtKB:Q9NXV2}.
CC -!- SUBUNIT: Homopentamer (By similarity). Interacts (via C-terminus) with
CC GRASP55/GORASP2. Interacts with CUL3 and with ubiquitinated proteins
CC (By similarity). Interacts with CRY1 (PubMed:27123980).
CC {ECO:0000250|UniProtKB:Q9NXV2, ECO:0000269|PubMed:27123980}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NXV2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NXV2}. Nucleus {ECO:0000250|UniProtKB:Q9NXV2}.
CC Note=Predominantly cytoplasmic, translocated to the nucleus upon
CC interaction with Rep proteins. {ECO:0000250|UniProtKB:Q9NXV2}.
CC -!- DOMAIN: The BTB (POZ) domain is atypical and mediates the formation of
CC a homopentamer instead of a homotetramer (By similarity).
CC Homopentamerization is due to the presence of 4 residues in the BTB
CC (POZ) domain: Leu-56, Gly-100, Val-112 and Ala-118 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NXV2}.
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DR EMBL; AY162410; AAO17163.1; -; Genomic_DNA.
DR EMBL; AK143644; BAE25476.1; -; mRNA.
DR EMBL; BC021777; AAH21777.1; -; mRNA.
DR CCDS; CCDS28473.1; -.
DR RefSeq; NP_081284.2; NM_027008.2.
DR AlphaFoldDB; Q8VC57; -.
DR SMR; Q8VC57; -.
DR BioGRID; 213321; 87.
DR IntAct; Q8VC57; 87.
DR STRING; 10090.ENSMUSP00000017090; -.
DR iPTMnet; Q8VC57; -.
DR PhosphoSitePlus; Q8VC57; -.
DR EPD; Q8VC57; -.
DR MaxQB; Q8VC57; -.
DR PaxDb; Q8VC57; -.
DR PRIDE; Q8VC57; -.
DR ProteomicsDB; 263422; -.
DR DNASU; 69259; -.
DR GeneID; 69259; -.
DR KEGG; mmu:69259; -.
DR UCSC; uc008auh.2; mouse.
DR CTD; 54442; -.
DR MGI; MGI:1916509; Kctd5.
DR eggNOG; KOG2715; Eukaryota.
DR InParanoid; Q8VC57; -.
DR OrthoDB; 1333587at2759; -.
DR PhylomeDB; Q8VC57; -.
DR TreeFam; TF313754; -.
DR BioGRID-ORCS; 69259; 19 hits in 76 CRISPR screens.
DR ChiTaRS; Kctd5; mouse.
DR PRO; PR:Q8VC57; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VC57; protein.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 Acetylation; Cytoplasm; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NXV2"
FT CHAIN 2..234
FT /note="BTB/POZ domain-containing protein KCTD5"
FT /id="PRO_0000191292"
FT DOMAIN 44..146
FT /note="BTB"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXV2"
FT CONFLICT 148
FT /note="R -> K (in Ref. 2; BAE25476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26164 MW; 915F4796A139755E CRC64;
MAENHCELLP PAPSGLGAGL GGGLCRRCSA GMGALAQRPG GVSKWVRLNV GGTYFLTTRQ
TLCRDPKSFL YRLCQADPDL DSDKDETGAY LIDRDPTYFG PVLNYLRHGK LVINKDLAEE
GVLEEAEFYN ITSLIKLVKD KIRERDSRIS QMPVKHVYRV LQCQEEELTQ MVSTMSDGWK
FEQLVSIGSS YNYGNEDQAE FLCVVSKELH NTPYGTTSEP SEKAKILQER GSRM
