KLH20_MOUSE
ID KLH20_MOUSE Reviewed; 604 AA.
AC Q8VCK5; Q5DTH3; Q8BWA2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Kelch-like protein 20;
DE AltName: Full=Kelch-like ECT2-interacting protein;
GN Name=Klhl20; Synonyms=Kiaa4210, Kleip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=22511632; DOI=10.1167/iovs.12-9676;
RA Hahn N., Dietz C.T., Kuhl S., Vossmerbaeumer U., Kroll J.;
RT "KLEIP deficiency in mice causes progressive corneal neovascular
RT dystrophy.";
RL Invest. Ophthalmol. Vis. Sci. 53:3260-3268(2012).
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}.
CC -!- DISRUPTION PHENOTYPE: Approximately 50% of mice die until day 28 of
CC postnatal development (P28). Mice that survive beyond P28 are
CC indistinguishable at birth, but show a progressive corneal dystrophy,
CC associated with an epithelial hyperplasia and an altered corneal
CC epithelial cell differentiation. {ECO:0000269|PubMed:22511632}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90319.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220547; BAD90319.1; ALT_INIT; mRNA.
DR EMBL; AK053102; BAC35266.1; -; mRNA.
DR EMBL; BC019571; AAH19571.2; -; mRNA.
DR CCDS; CCDS35748.1; -.
DR RefSeq; NP_001034571.1; NM_001039482.1.
DR AlphaFoldDB; Q8VCK5; -.
DR SMR; Q8VCK5; -.
DR STRING; 10090.ENSMUSP00000107238; -.
DR iPTMnet; Q8VCK5; -.
DR PhosphoSitePlus; Q8VCK5; -.
DR EPD; Q8VCK5; -.
DR MaxQB; Q8VCK5; -.
DR PaxDb; Q8VCK5; -.
DR PRIDE; Q8VCK5; -.
DR ProteomicsDB; 264846; -.
DR Antibodypedia; 20562; 112 antibodies from 21 providers.
DR DNASU; 226541; -.
DR Ensembl; ENSMUST00000111611; ENSMUSP00000107238; ENSMUSG00000026705.
DR Ensembl; ENSMUST00000117467; ENSMUSP00000114044; ENSMUSG00000026705.
DR GeneID; 226541; -.
DR KEGG; mmu:226541; -.
DR UCSC; uc007dff.1; mouse.
DR CTD; 27252; -.
DR MGI; MGI:2444855; Klhl20.
DR VEuPathDB; HostDB:ENSMUSG00000026705; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155161; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; Q8VCK5; -.
DR OMA; NSWSPIV; -.
DR OrthoDB; 731760at2759; -.
DR PhylomeDB; Q8VCK5; -.
DR TreeFam; TF329218; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 226541; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8VCK5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VCK5; protein.
DR Bgee; ENSMUSG00000026705; Expressed in facial nucleus and 181 other tissues.
DR ExpressionAtlas; Q8VCK5; baseline and differential.
DR Genevisible; Q8VCK5; MM.
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; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; IPR011043; Gal_Oxase/kelch_b-propeller.
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; SSF50965; SSF50965; 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..604
FT /note="Kelch-like protein 20"
FT /id="PRO_0000119124"
FT DOMAIN 63..130
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 165..267
FT /note="BACK"
FT REPEAT 314..360
FT /note="Kelch 1"
FT REPEAT 362..408
FT /note="Kelch 2"
FT REPEAT 409..455
FT /note="Kelch 3"
FT REPEAT 457..502
FT /note="Kelch 4"
FT REPEAT 504..549
FT /note="Kelch 5"
FT REPEAT 551..596
FT /note="Kelch 6"
SQ SEQUENCE 604 AA; 67412 MW; 3A87B3DC714B1BC9 CRC64;
MRRCTNIRPG ETGMDVTSRC TLGDPNKLPE GVPQPARMPY ISDKHPRQTL EVINLLRKHR
ELCDVVLVVG AKKIYAHRVI LSACSPYFRA MFTGELAESR QTEVVIRDID ERAMELLIDF
AYTSQITVEE GNVQTLLPAA CLLQLAEIQE ACCEFLKRQL DPSNCLGIRA FADTHSCREL
LRIADKFTQH NFQEVMESEE FMLLPANQLI DIISSDELNV RSEEQVFNAV MAWVKYSIQE
RRPQLPQVLQ HVRLPLLSPK FLVGTVGSDP LIKSDEECRD LVDEAKNYLL LPQERPLMQG
PRTRPRKPIR CGEVLFAVGG WCSGDAISSV ERYDPQTNEW RMVASMSKRR CGVGVSVLDD
LLYAVGGHDG SSYLNSVERY DPKTNQWSSD VAPTSTCRTS VGVAVLGGFL YAVGGQDGVS
CLNIVERYDP KENKWTRVAS MSTRRLGVAV AVLGGFLYAV GGSDGTSPLN TVERYNPQEN
RWHTIAPMGT RRKHLGCAVY QDMIYAVGGR DDTTELSSAE RYNPRTNQWS PVVAMTSRRS
GVGLAVVNGQ LMAVGGFDGT TYLKTIEVFD PDANTWRLYG GMNYRRLGGG VGVIKMTHCE
SHIW
