ID KLH25_XENLA Reviewed; 589 AA.
AC Q6DFF7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Kelch-like protein 25 {ECO:0000305};
GN Name=klhl25 {ECO:0000250|UniProtKB:Q9H0H3};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex involved in various processes, such as
CC translation homeostasis and lipid synthesis. The BCR(KLHL25) ubiquitin
CC ligase complex acts by mediating ubiquitination of hypophosphorylated
CC eif4ebp1 (4E-BP1): ubiquitination and subsequent degradation of
CC hypophosphorylated EIF4EBP1 (4E-BP1) probably serves as a homeostatic
CC mechanism to maintain translation and prevent eIF4E inhibition when
CC eIF4E levels are low. The BCR(KLHL25) complex also acts as a regulator
CC of lipid synthesis by mediating ubiquitination and degradation of ACLY,
CC thereby inhibiting lipid synthesis. {ECO:0000250|UniProtKB:Q9H0H3}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H0H3}.
CC -!- SUBUNIT: Component of the BCR(KLHL25) E3 ubiquitin ligase complex, at
CC least composed of cul3, klhl25 and rbx1.
CC {ECO:0000250|UniProtKB:Q9H0H3}.
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DR EMBL; BC076781; AAH76781.1; -; mRNA.
DR RefSeq; NP_001082572.1; NM_001089103.1.
DR AlphaFoldDB; Q6DFF7; -.
DR SMR; Q6DFF7; -.
DR DNASU; 398575; -.
DR GeneID; 398575; -.
DR KEGG; xla:398575; -.
DR AGR; Xenbase:XB-GENE-964642; -.
DR CTD; 398575; -.
DR Xenbase; XB-GENE-964642; klhl25.L.
DR OMA; TVSACTW; -.
DR OrthoDB; 5472491at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398575; Expressed in testis and 17 other cell types or tissues.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; ISS:UniProtKB.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd18254; BTB_POZ_KLHL25; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
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; IPR030565; KLHL25_BTB_POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412; KELCH PROTEIN; 1.
DR PANTHER; PTHR24412:SF488; KELCH-LIKE PROTEIN 20; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 4.
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; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Kelch repeat; Reference proteome; Repeat; Translation regulation;
KW Ubl conjugation pathway.
FT CHAIN 1..589
FT /note="Kelch-like protein 25"
FT /id="PRO_0000272311"
FT DOMAIN 46..114
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 149..250
FT /note="BACK"
FT REPEAT 296..340
FT /note="Kelch 1"
FT REPEAT 341..388
FT /note="Kelch 2"
FT REPEAT 389..444
FT /note="Kelch 3"
FT REPEAT 446..492
FT /note="Kelch 4"
FT REPEAT 494..538
FT /note="Kelch 5"
FT REPEAT 539..585
FT /note="Kelch 6"
SQ SEQUENCE 589 AA; 66081 MW; 3178443A9CA9B083 CRC64;
MSVSVHENRK SRTSTGSMNI SLYHKLSHSE CVLNHLNTMR KQRLFTDMTL WAGNRSFPCH
RAVLAACSPY FEAMFSNGLR ESLDNTVNFH NSLHPEVLEL LLDFAYSSKI IINEENAESL
LEAGDMLQFH DVRDAACEFL EKNLYPSNCL GMMILSDAHQ CQRLYELSLR MCLSNFATLH
NTEDFSSLSK DMLLDLISSD ELEIEDEQVV FNAVLHWVKE DLDKRKDYFP ELLRNVRLAL
LPSELLKEAV VCEDLIIADE RSKLIMDEAV QCKKKILQND GVVTSLCAKP RKAGHTLLIL
GGQTFMCDKI YQLDHKAKEI IPKADLPSPR KEFSACAIGC KVYITGGRGS ENGVSKDVWV
YDTIHEEWSK SAPMLIARFG HGSAELDNCL YVVGGHTAVA GVFPASPSVS LKQVEKYDPL
PNKWTMMAPL RDGVSNAAVV SAKLKLFVFG GTSIHRDRVS KVQFYDPHEN RWSIKAECPQ
PWRYTAAAVL GSQIFIMGGD TEFTAASAYR FDCETNLWTR IGDMTAKRMS CHALASGNKV
YVVGGYFGTQ RCKTLDCYDP TSDSWNSITS VPYSLIPTAF VSTWKHLPA
//