ID KLHL3_DANRE Reviewed; 601 AA.
AC E7F6F9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Kelch-like protein 3;
GN Name=klhl3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex that acts as a regulator of ion transport in
CC the distal nephron. The BCR(KLHL3) complex acts by mediating
CC ubiquitination and degradation of WNK1 and WNK4, two activators of Na-
CC Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of
CC kidney, thereby regulating NaCl reabsorption.
CC {ECO:0000250|UniProtKB:Q9UH77}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9UH77}.
CC -!- SUBUNIT: Component of the BCR(KLHL3) E3 ubiquitin ligase complex, at
CC least composed of cul3 and klhl3 and rbx1.
CC {ECO:0000250|UniProtKB:Q9UH77}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UH77}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9UH77}.
CC -!- SIMILARITY: Belongs to the KLHL3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX005228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E7F6F9; -.
DR SMR; E7F6F9; -.
DR STRING; 7955.ENSDARP00000142614; -.
DR PaxDb; 7955-ENSDARP00000073620; -.
DR AGR; ZFIN:ZDB-GENE-120203-4; -.
DR ZFIN; ZDB-GENE-120203-4; klhl3.
DR eggNOG; KOG4441; Eukaryota.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; E7F6F9; -.
DR PhylomeDB; E7F6F9; -.
DR TreeFam; TF329218; -.
DR Reactome; R-DRE-8951664; Neddylation.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:E7F6F9; -.
DR Proteomes; UP000000437; Genome assembly.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0072156; P:distal tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0050801; P:monoatomic ion homeostasis; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0070294; P:renal sodium ion absorption; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd18513; BACK_KLHL3; 1.
DR CDD; cd18235; BTB_POZ_KLHL2-like; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 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; IPR030578; KLHL3_BACK.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412; KELCH PROTEIN; 1.
DR PANTHER; PTHR24412:SF179; KELCH-LIKE PROTEIN 3; 1.
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; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cytoplasm; Cytoskeleton; Kelch repeat; Reference proteome;
KW Repeat; Ubl conjugation pathway.
FT CHAIN 1..601
FT /note="Kelch-like protein 3"
FT /id="PRO_0000417533"
FT DOMAIN 63..130
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 165..268
FT /note="BACK"
FT REPEAT 316..361
FT /note="Kelch 1"
FT REPEAT 362..408
FT /note="Kelch 2"
FT REPEAT 410..455
FT /note="Kelch 3"
FT REPEAT 456..504
FT /note="Kelch 4"
FT REPEAT 505..551
FT /note="Kelch 5"
FT REPEAT 553..599
FT /note="Kelch 6"
SQ SEQUENCE 601 AA; 66868 MW; 5C8A62170CA8A3F5 CRC64;
MVLWGFFLRF RFFLTCGRNC IQKTLDSQDD AKDPGLHTFS HTHMRKAFLL MNDLRSHSRK
MLCDVLLVAG EVEIPAHRVV LASCSPYFCA MFTGDMSESK ANHVEIRDVD GQTLLKLVDY
IYSAEIEVSE ENVQVLLPAA SLLQLMDVRQ VCCDFLQTQL HPTNCLGIRA FADLHACTVL
LSQAHAYAAE QHFTDVMVGE EFMALSLQQV CSLISSDKLT VSTEEKVFEA MVAWIKHDKE
ARLEHMPKLM EHVRLPLLSR DYLVQIVEEE PLIKNNNTCK DFLIEAMKYH LLPADQRHLI
KTDRTRPRTP ISLPKVMMVV GGQAPKAIRS VECYDFQEDR WYQVADLPSR RCRAGVVYMA
GKVYAVGGFN GSLRVRTVDV YDGLKDQWSS IPSMQERRST LGAAVLGDLL YAVGGFDGST
GLSSVEAYNP KANEWMFVAP MNTRRSSVGV GVVDGKLYAV GGYDGASRQC LSTVEEFNPV
SNKWCYVSDM STRRSGAGVG VLSGQLYAAG GHDGPLVRKS VEVYDPTTNT WRQVCDMNMC
RRNAGVCAIN GLLYVIGGDD GSCNLSSVEY YDPAADKWSL IPTNMSNGRS YAGVSVIDKP
L
//
