KLH24_RAT
ID KLH24_RAT Reviewed; 600 AA.
AC Q56A24; Q812D9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Kelch-like protein 24;
DE AltName: Full=Kainate receptor-interacting protein for GluR6;
DE Short=KRIP6;
DE AltName: Full=Protein DRE1;
GN Name=Klhl24; Synonyms=Dre1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nomoto S., Ikeda K., Zhao J., Kayama F.;
RT "Identification of DRE1 which is downregulated in uterus when immature rats
RT are injected estrogen subctaneously.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH GRIK2, HOMODIMERIZATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17254796; DOI=10.1016/j.mcn.2006.12.003;
RA Laezza F., Wilding T.J., Sequeira S., Coussen F., Zhang X.Z.,
RA Hill-Robinson R., Mulle C., Huettner J.E., Craig A.M.;
RT "KRIP6: a novel BTB/kelch protein regulating function of kainate
RT receptors.";
RL Mol. Cell. Neurosci. 34:539-550(2007).
CC -!- FUNCTION: Necessary to maintain the balance between intermediate
CC filament stability and degradation, a process that is essential for
CC skin integrity (By similarity). As part of the BCR(KLHL24) E3 ubiquitin
CC ligase complex, mediates ubiquitination of KRT14 and controls its
CC levels during keratinocytes differentiation (By similarity).
CC Specifically reduces kainate receptor-mediated currents in hippocampal
CC neurons, most probably by modulating channel properties
CC (PubMed:17254796). {ECO:0000250|UniProtKB:Q6TFL4,
CC ECO:0000269|PubMed:17254796}.
CC -!- SUBUNIT: Forms homodimers. Interacts with GRIK2 (PubMed:17254796).
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:Q6TFL4,
CC ECO:0000269|PubMed:17254796}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:17254796}. Cell
CC projection, axon {ECO:0000269|PubMed:17254796}. Cytoplasm
CC {ECO:0000269|PubMed:17254796}. Cell junction, desmosome
CC {ECO:0000250|UniProtKB:Q6TFL4}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q6TFL4}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:17254796}.
CC -!- DEVELOPMENTAL STAGE: In 3-week postnatal brain, prominent in the cortex
CC and in the hippocampus. In the hippocampal formation, detectable in the
CC CA1-CA3 pyramidal cells and in the granule cell layer of the dentate
CC gyrus. In the cerebral cortex, expressed in all layers (I-VI) (at
CC protein level). In 10 week old animals, tends to segregate in CA3
CC regions. {ECO:0000269|PubMed:17254796}.
CC -!- PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal
CC degradation and is necessary to control KLHL24 levels.
CC {ECO:0000250|UniProtKB:Q6TFL4}.
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DR EMBL; AB101615; BAC56128.1; -; mRNA.
DR EMBL; BC092204; AAH92204.1; -; mRNA.
DR RefSeq; NP_852138.2; NM_181473.2.
DR AlphaFoldDB; Q56A24; -.
DR SMR; Q56A24; -.
DR STRING; 10116.ENSRNOP00000050815; -.
DR PaxDb; Q56A24; -.
DR Ensembl; ENSRNOT00000052120; ENSRNOP00000050815; ENSRNOG00000033372.
DR GeneID; 303803; -.
DR KEGG; rno:303803; -.
DR CTD; 54800; -.
DR RGD; 727971; Klhl24.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000154345; -.
DR InParanoid; Q56A24; -.
DR OrthoDB; 279729at2759; -.
DR PhylomeDB; Q56A24; -.
DR PRO; PR:Q56A24; -.
DR Proteomes; UP000002494; Chromosome 11.
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 1: Evidence at protein 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_0000261596"
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; BAC56128)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="H -> D (in Ref. 1; BAC56128)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="N -> F (in Ref. 1; BAC56128)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="D -> H (in Ref. 1; BAC56128)"
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
