KLH24_MOUSE
ID KLH24_MOUSE Reviewed; 600 AA.
AC Q8BRG6; Q3TQG0; Q78J30; Q8BQU1; Q9D5K3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Kelch-like protein 24;
DE AltName: Full=Kainate receptor-interacting protein for GluR6;
DE Short=KRIP6;
GN Name=Klhl24;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Corpora quadrigemina, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-600.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27798626; DOI=10.1038/ng.3701;
RA Lin Z., Li S., Feng C., Yang S., Wang H., Ma D., Zhang J., Gou M., Bu D.,
RA Zhang T., Kong X., Wang X., Sarig O., Ren Y., Dai L., Liu H., Zhang J.,
RA Li F., Hu Y., Padalon-Brauch G., Vodo D., Zhou F., Chen T., Deng H.,
RA Sprecher E., Yang Y., Tan X.;
RT "Stabilizing mutations of KLHL24 ubiquitin ligase cause loss of keratin 14
RT and human skin fragility.";
RL Nat. Genet. 48:1508-1516(2016).
CC -!- FUNCTION: Controls KRT14 levels during keratinocytes differentiation
CC (PubMed:27798626). As part of the BCR(KLHL24) E3 ubiquitin ligase
CC complex, mediates ubiquitination of KRT14 (By similarity). Specifically
CC reduces kainate receptor-mediated currents in hippocampal neurons, most
CC probably by modulating channel properties (By similarity).
CC {ECO:0000250|UniProtKB:Q56A24, ECO:0000250|UniProtKB:Q6TFL4,
CC ECO:0000269|PubMed:27798626}.
CC -!- SUBUNIT: Forms homodimers. Interacts with GRIK2 (By similarity).
CC Component of the BCR(KLHL24) E3 ubiquitin ligase complex, composed of
CC CUL3, RBX1 and KLHL24. Interacts with CUL3. Interacts with KRT14 (By
CC similarity). {ECO:0000250|UniProtKB:Q56A24,
CC ECO:0000250|UniProtKB:Q6TFL4}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250|UniProtKB:Q6TFL4}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q56A24}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q56A24, ECO:0000250|UniProtKB:Q6TFL4}. Cell
CC junction, desmosome {ECO:0000250|UniProtKB:Q6TFL4}. Cell junction,
CC adherens junction {ECO:0000250|UniProtKB:Q6TFL4}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:27798626}.
CC -!- PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal
CC degradation and is necessary to control KLHL24 levels.
CC {ECO:0000250|UniProtKB:Q6TFL4}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21407.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29759.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE37423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK015239; BAB29759.2; ALT_INIT; mRNA.
DR EMBL; AK044892; BAC32131.1; -; mRNA.
DR EMBL; AK046446; BAC32732.1; -; mRNA.
DR EMBL; AK163616; BAE37423.1; ALT_INIT; mRNA.
DR EMBL; BC021407; AAH21407.2; ALT_INIT; mRNA.
DR CCDS; CCDS28042.1; -.
DR RefSeq; NP_083712.4; NM_029436.3.
DR RefSeq; XP_006522750.1; XM_006522687.3.
DR AlphaFoldDB; Q8BRG6; -.
DR SMR; Q8BRG6; -.
DR BioGRID; 217740; 6.
DR STRING; 10090.ENSMUSP00000023509; -.
DR PhosphoSitePlus; Q8BRG6; -.
DR EPD; Q8BRG6; -.
DR MaxQB; Q8BRG6; -.
DR PaxDb; Q8BRG6; -.
DR PRIDE; Q8BRG6; -.
DR ProteomicsDB; 265000; -.
DR Antibodypedia; 54833; 87 antibodies from 14 providers.
DR DNASU; 75785; -.
DR Ensembl; ENSMUST00000023509; ENSMUSP00000023509; ENSMUSG00000062901.
DR GeneID; 75785; -.
DR KEGG; mmu:75785; -.
DR UCSC; uc007yph.1; mouse.
DR CTD; 54800; -.
DR MGI; MGI:1923035; Klhl24.
DR VEuPathDB; HostDB:ENSMUSG00000062901; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000154345; -.
DR HOGENOM; CLU_004253_14_6_1; -.
DR InParanoid; Q8BRG6; -.
DR OMA; QTFNKQE; -.
DR OrthoDB; 279729at2759; -.
DR PhylomeDB; Q8BRG6; -.
DR TreeFam; TF351654; -.
DR BioGRID-ORCS; 75785; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Klhl24; mouse.
DR PRO; PR:Q8BRG6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BRG6; protein.
DR Bgee; ENSMUSG00000062901; Expressed in metanephric mesenchyme and 237 other tissues.
DR ExpressionAtlas; Q8BRG6; baseline and differential.
DR Genevisible; Q8BRG6; MM.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030057; C:desmosome; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000312; P:regulation of kainate selective glutamate receptor activity; IEA:InterPro.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030596; KLHL24.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF215; PTHR24412:SF215; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 5.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell projection; Cytoplasm; Kelch repeat;
KW Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..600
FT /note="Kelch-like protein 24"
FT /id="PRO_0000261595"
FT DOMAIN 66..133
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 168..270
FT /note="BACK"
FT REPEAT 314..363
FT /note="Kelch 1"
FT REPEAT 365..407
FT /note="Kelch 2"
FT REPEAT 408..454
FT /note="Kelch 3"
FT REPEAT 456..502
FT /note="Kelch 4"
FT REPEAT 504..544
FT /note="Kelch 5"
FT REPEAT 546..592
FT /note="Kelch 6"
FT CONFLICT 8
FT /note="R -> T (in Ref. 1; BAB29759)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="D -> N (in Ref. 1; BAC32131)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="D -> N (in Ref. 1; BAC32732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 68364 MW; E12633EBBCD69086 CRC64;
MVLILGRRLN REDLGVRDSP ATKRKVFEMD PKSLTGHEYF DFSSGSSHAE NILQIFNEFR
DSRLFTDVII CVEGKEFPCH RAVLSACSSY FRAMFCNDHR ESREMLVEIN GILAEAMECF
LQYVYTGKVK ITTENVQYLF ETSSLFQISV LRDACAKFLE EQLDPCNCLG IQRFADTHSL
KTLFTKCKTF ALQTFEDVSQ HEEFLELDKD ELIDYICSDE LVIGKEEMVF EAVMRWVYRA
VDLRRPLLHE LLTHVRLPLL HPNYFVQTVE VDQLIQNSPE CYQLLHEARR YHILGNEMMS
PRTRPRRSTG YSEVIVVVGG CERVGGFNLP YTECYDPVTG EWKSLAKLPE FTKSEYAVCA
LRNDILVSGG RINSRDVWIY NSQLNIWIRV ASLNKGRWRH KMAVLLGKVY VVGGYDGQNR
LSSVECYDSF SNRWTEVAPL KEAVSSPAVT SCIGKLFVIG GGPDDNTCSD KVQSYDPETN
SWLLRAAIPI AKRCITAVSL NNLIYVAGGL TKAVYCYDPV EDYWMHVQNT FSRQENCGMS
VCNGKIYILG GRRENGEATD TILCYDPATS IITGVAAMPR PVSYHGCVTI HRYNEKCFKL
