KLH20_BOVIN
ID KLH20_BOVIN Reviewed; 609 AA.
AC Q08DK3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Kelch-like protein 20;
GN Name=KLHL20;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex involved in interferon response and
CC anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin
CC ligase complex mediates the ubiquitination of DAPK1, leading to its
CC degradation by the proteasome, thereby acting as a negative regulator
CC of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also
CC specifically mediates 'Lys-33'-linked ubiquitination. Involved in
CC anterograde Golgi to endosome transport by mediating 'Lys-33'-linked
CC ubiquitination of CORO7, promoting interaction between CORO7 and EPS15,
CC thereby facilitating actin polymerization and post-Golgi trafficking.
CC Also acts as a regulator of endothelial migration during angiogenesis
CC by controlling the activation of Rho GTPases. The BCR(KLHL20) E3
CC ubiquitin ligase complex acts as a regulator of neurite outgrowth by
CC mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2M5}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(KLHL20) E3 ubiquitin ligase complex, at
CC least composed of CUL3, KLHL20 and RBX1. Interacts with PDZ-
CC RhoGEF/ARHGEF11, DAPK1, PML and CORO7. Interacts with F-actin.
CC Interacts with IFN-gamma (IFNG) (By similarity). Interacts (via kelch
CC repeats) with IVNS1ABP (via kelch repeats); this interaction blocks the
CC assembly of CUL3-KLHL20 complex (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2M5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Nucleus {ECO:0000250}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection,
CC dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in
CC normal conditions. Following IFN-alpha or IFN-gamma treatment, it is
CC relocalized and sequestrated to the PML nuclear bodies, preventing
CC DAPK1 ubiquitination (By similarity). {ECO:0000250}.
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DR EMBL; BC123702; AAI23703.1; -; mRNA.
DR RefSeq; NP_001070303.1; NM_001076835.1.
DR RefSeq; XP_005217118.1; XM_005217061.1.
DR RefSeq; XP_005217119.1; XM_005217062.3.
DR AlphaFoldDB; Q08DK3; -.
DR SMR; Q08DK3; -.
DR IntAct; Q08DK3; 2.
DR STRING; 9913.ENSBTAP00000033909; -.
DR PaxDb; Q08DK3; -.
DR Ensembl; ENSBTAT00000034007; ENSBTAP00000033909; ENSBTAG00000024485.
DR Ensembl; ENSBTAT00000072303; ENSBTAP00000066607; ENSBTAG00000024485.
DR GeneID; 511387; -.
DR KEGG; bta:511387; -.
DR CTD; 27252; -.
DR VEuPathDB; HostDB:ENSBTAG00000024485; -.
DR VGNC; VGNC:30649; KLHL20.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155161; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; Q08DK3; -.
DR OMA; NSWSPIV; -.
DR OrthoDB; 731760at2759; -.
DR TreeFam; TF329218; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000024485; Expressed in midbrain and 103 other tissues.
DR ExpressionAtlas; Q08DK3; baseline and differential.
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:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0019964; F:interferon-gamma binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1990390; P:protein K33-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
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; IPR030594; KLHL17/KLHL20.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF454; PTHR24412:SF454; 2.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
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 Actin-binding; Cell projection; Cytoplasm; Golgi apparatus; Kelch repeat;
KW Nucleus; Protein transport; Reference proteome; Repeat; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..609
FT /note="Kelch-like protein 20"
FT /id="PRO_0000278666"
FT DOMAIN 68..135
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 170..272
FT /note="BACK"
FT REPEAT 319..365
FT /note="Kelch 1"
FT REPEAT 367..413
FT /note="Kelch 2"
FT REPEAT 414..460
FT /note="Kelch 3"
FT REPEAT 462..507
FT /note="Kelch 4"
FT REPEAT 509..554
FT /note="Kelch 5"
FT REPEAT 556..601
FT /note="Kelch 6"
SQ SEQUENCE 609 AA; 67955 MW; FA05E3FE8341B422 CRC64;
MEGKPMRRCT NIRPGETGMD VTSRCTLGDP NKLPEGVPQP ARMPYISDKH PRQTLEVINL
LRKHRELCDV VLVVGAKKIY AHRVILSACS PYFRAMFTGE LAESRQTEVV IRDIDERAME
LLIDFAYTSQ ITVEEGNVQT LLPAACLLQL AEIQEACCEF LKRQLDPSNC LGIRAFADTH
SCRELLRIAD KFTQHNFQEV MESEEFMLLP ANQLIDIISS DELNVRSEEQ VFNAVMAWVK
YSIQERRPQL PQVLQHVRLP LLSPKFLVGT VGSDPLIKSD EECRDLVDEA KNYLLLPQER
PLMQGPRTRP RKPIRCGEVL FAVGGWCSGD AISSVERYDP QTNEWRMVAS MSKRRCGVGV
SVLDDLLYAV GGHDGSSYLN SVERYDPKTN QWSSDVAPTS TCRTSVGVAV LGGFLYAVGG
QDGVSCLNIV ERYDPKENKW TRVASMSTRR LGVAVAVLGG FLYAVGGSDG TSPLNTVERY
NPQENRWHTI APMGTRRKHL GCAVYQDMIY AVGGRDDTTE LSSAERYNPR TNQWSPVVAM
TSRRSGVGLA VVNGQLMAVG GFDGTTYLKT IEVFDPDANT WRLYGGMNYR RLGGGVGVIK
MTHCESHIW
