ID   KLH20_PONAB             Reviewed;         609 AA.
AC   Q5R7B8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 3.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Kelch-like protein 20;
GN   Name=KLHL20;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860200; CAH92342.1; -; mRNA.
DR   RefSeq; NP_001127542.1; NM_001134070.2.
DR   AlphaFoldDB; Q5R7B8; -.
DR   SMR; Q5R7B8; -.
DR   STRING; 9601.ENSPPYP00000000573; -.
DR   GeneID; 100174619; -.
DR   KEGG; pon:100174619; -.
DR   CTD; 27252; -.
DR   eggNOG; KOG4441; Eukaryota.
DR   InParanoid; Q5R7B8; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Unplaced.
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_0000285811"
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;  68042 MW;  FAA98DF16AFE482E 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
     YSTQERRPQL 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 VVNGQLMAVR GFDGTTYLKT IEVFDPDANT WRLYGGMNYR RLGGGVGVIK
     MTHCESHIW