KLH25_RAT
ID KLH25_RAT Reviewed; 589 AA.
AC Q4KLM4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Kelch-like protein 25;
DE AltName: Full=Ectoderm-neural cortex protein 2;
DE Short=ENC-2;
GN Name=Klhl25; Synonyms=Enc2;
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 [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex required for translational homeostasis. The
CC BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination
CC of hypophosphorylated EIF4EBP1 (4E-BP1): ubiquitination and subsequent
CC degradation of hypophosphorylated EIF4EBP1 (4E-BP1) probably serves as
CC a homeostatic mechanism to maintain translation and prevent eIF4E
CC inhibition when eIF4E levels are low. The BCR(KLHL25) complex does not
CC target EIF4EBP1 (4E-BP1) when it is hyperphosphorylated or associated
CC with eIF4E (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(KLHL25) E3 ubiquitin ligase complex, at
CC least composed of CUL3, KLHL25 and RBX1. Interacts with EIF4EBP1 (when
CC hypophosphorylated) (By similarity). {ECO:0000250}.
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DR EMBL; BC099111; AAH99111.1; -; mRNA.
DR RefSeq; NP_001034095.1; NM_001039006.1.
DR RefSeq; XP_006229441.1; XM_006229379.2.
DR RefSeq; XP_006229442.1; XM_006229380.2.
DR RefSeq; XP_006229443.1; XM_006229381.3.
DR RefSeq; XP_008757727.1; XM_008759505.2.
DR AlphaFoldDB; Q4KLM4; -.
DR SMR; Q4KLM4; -.
DR STRING; 10116.ENSRNOP00000014553; -.
DR PhosphoSitePlus; Q4KLM4; -.
DR PaxDb; Q4KLM4; -.
DR PRIDE; Q4KLM4; -.
DR Ensembl; ENSRNOT00000014553; ENSRNOP00000014553; ENSRNOG00000010959.
DR Ensembl; ENSRNOT00000097328; ENSRNOP00000089869; ENSRNOG00000010959.
DR Ensembl; ENSRNOT00000111640; ENSRNOP00000097538; ENSRNOG00000010959.
DR Ensembl; ENSRNOT00000112874; ENSRNOP00000090402; ENSRNOG00000010959.
DR Ensembl; ENSRNOT00000112989; ENSRNOP00000091951; ENSRNOG00000010959.
DR GeneID; 293023; -.
DR KEGG; rno:293023; -.
DR UCSC; RGD:1310815; rat.
DR CTD; 64410; -.
DR RGD; 1310815; Klhl25.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00950000182983; -.
DR HOGENOM; CLU_004253_14_6_1; -.
DR InParanoid; Q4KLM4; -.
DR OMA; KIYQVDQ; -.
DR OrthoDB; 709680at2759; -.
DR PhylomeDB; Q4KLM4; -.
DR TreeFam; TF329218; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q4KLM4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000010959; Expressed in liver and 19 other tissues.
DR Genevisible; Q4KLM4; RN.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 Gene3D; 2.120.10.80; -; 2.
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; IPR030565; KLHL25.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24410:SF10; PTHR24410:SF10; 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; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 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_0000272310"
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 493..538
FT /note="Kelch 5"
FT REPEAT 539..585
FT /note="Kelch 6"
SQ SEQUENCE 589 AA; 65840 MW; 98D72FC65AAAC97D CRC64;
MSVSVHETRK SRSSTGSMNI SVFHKASHPD CVLAHLNTLR KHCMFTDVTL WAGDRAFPCH
RAVLAASSRY FEAMFSHGLR ESRDDTVNFQ DNLHPEVLEL LLDFAYSSRI VINEENAESL
LEAGDMLQFH DVRDAAAEFL EKNLSPSNCL GMMVLSDAHQ CRRLYEFSCR MSLVHFETVR
QSEDFNSLSR DTLLDLISRD ELETEDERVV FEAILQWVKH DLEQRKVHLP LLLRNVRLAL
LPSDCLKKAV SGEALLMADE CTKLIIDEAF RCKTKILLND GVVTSPFARP RKAGHTLLIL
GGQTFMCDKI YQVDHKAKEI IPKADLPSPR KEFSASAIGC KVYVTGGRGS ENGVSKDVWV
YDTVHEEWSK AAPMLIARFG HGSAELENCL YVVGGHTSLA GIFPASPSVS LKQVEKYDPG
DNKWTMVAPM RDGVSNAAVV SAKLKLFVFG GTSIHRDMVS KVQCFDPSDN RWTIKAECPQ
PWRYTAAAVL GSQIFIMGGD TEYTAASAYR FDCETNQWTR IGDMTAKRMS CHAVASGNKL
YVVGGYFGTQ RCKTLDCYDP TSDTWNCITS VPYSLIPTAF VSTWKHLPA
