KL40B_DANRE
ID KL40B_DANRE Reviewed; 618 AA.
AC E9QJ30;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Kelch-like protein 40b;
DE AltName: Full=Kelch repeat and BTB domain-containing protein 5b;
GN Name=klhl40b; Synonyms=kbtbd5b;
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).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23746549; DOI=10.1016/j.ajhg.2013.05.004;
RA Ravenscroft G., Miyatake S., Lehtokari V.L., Todd E.J., Vornanen P.,
RA Yau K.S., Hayashi Y.K., Miyake N., Tsurusaki Y., Doi H., Saitsu H.,
RA Osaka H., Yamashita S., Ohya T., Sakamoto Y., Koshimizu E., Imamura S.,
RA Yamashita M., Ogata K., Shiina M., Bryson-Richardson R.J., Vaz R.,
RA Ceyhan O., Brownstein C.A., Swanson L.C., Monnot S., Romero N.B.,
RA Amthor H., Kresoje N., Sivadorai P., Kiraly-Borri C., Haliloglu G.,
RA Talim B., Orhan D., Kale G., Charles A.K., Fabian V.A., Davis M.R.,
RA Lammens M., Sewry C.A., Manzur A., Muntoni F., Clarke N.F., North K.N.,
RA Bertini E., Nevo Y., Willichowski E., Silberg I.E., Topaloglu H.,
RA Beggs A.H., Allcock R.J., Nishino I., Wallgren-Pettersson C., Matsumoto N.,
RA Laing N.G.;
RT "Mutations in KLHL40 are a frequent cause of severe autosomal-recessive
RT nemaline myopathy.";
RL Am. J. Hum. Genet. 93:6-18(2013).
CC -!- FUNCTION: ubstrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex (By similarity). Required for skeletal muscle
CC development (PubMed:23746549). {ECO:0000250|UniProtKB:Q9D783,
CC ECO:0000269|PubMed:23746549}.
CC -!- SUBUNIT: Component of the BCR(KLHL40) E3 ubiquitin ligase complex.
CC {ECO:0000250|UniProtKB:Q9D783}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D783}.
CC Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q9D783}.
CC Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:Q9D783}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle. Detected in the eye
CC at much lower levels. {ECO:0000269|PubMed:23746549}.
CC -!- DEVELOPMENTAL STAGE: At 16 and 24 hpf, restricted to muscle precursor
CC cells in somites. Also detected at 48 hpf.
CC {ECO:0000269|PubMed:23746549}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in a
CC curved trunk and small head at 48 hpf. Morphants show disruption of
CC skeletal muscle patterning with an irregular, wavy appearance of the
CC striated myofibers and extensive gaps between the myofibers. Myofibers
CC show disorganized and irregular patterns with small aggregates of
CC alpha-actinin, suggesting nemaline bodies. Animals exhibit sporadic
CC muscle tremor and coordinated swimming is not observed.
CC {ECO:0000269|PubMed:23746549}.
CC -!- SIMILARITY: Belongs to the KLHL40 family. {ECO:0000305}.
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DR EMBL; BX571770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001334076.1; XM_001334040.6.
DR AlphaFoldDB; E9QJ30; -.
DR SMR; E9QJ30; -.
DR STRING; 7955.ENSDARP00000012991; -.
DR PaxDb; E9QJ30; -.
DR PeptideAtlas; E9QJ30; -.
DR Ensembl; ENSDART00000010488; ENSDARP00000012991; ENSDARG00000019125.
DR GeneID; 795319; -.
DR KEGG; dre:795319; -.
DR CTD; 795319; -.
DR ZFIN; ZDB-GENE-060227-1; klhl40b.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000156360; -.
DR HOGENOM; CLU_004253_14_4_1; -.
DR InParanoid; E9QJ30; -.
DR OMA; KWVGHDQ; -.
DR OrthoDB; 946131at2759; -.
DR PhylomeDB; E9QJ30; -.
DR TreeFam; TF351653; -.
DR PRO; PR:E9QJ30; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000019125; Expressed in muscle tissue and 11 other tissues.
DR GO; GO:0031672; C:A band; 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:0031674; C:I band; IEA:UniProtKB-SubCell.
DR GO; GO:0061061; P:muscle structure development; IMP:ZFIN.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:InterPro.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:ZFIN.
DR GO; GO:0098528; P:skeletal muscle fiber differentiation; ISS:UniProtKB.
DR GO; GO:0036268; P:swimming; IGI:ZFIN.
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; IPR030607; KLHL40.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF22; PTHR24412:SF22; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 3.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 4.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Kelch repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..618
FT /note="Kelch-like protein 40b"
FT /id="PRO_0000423864"
FT DOMAIN 33..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 135..237
FT /note="BACK"
FT REPEAT 356..408
FT /note="Kelch 1"
FT REPEAT 409..458
FT /note="Kelch 2"
FT REPEAT 459..506
FT /note="Kelch 3"
FT REPEAT 508..553
FT /note="Kelch 4"
FT REPEAT 555..608
FT /note="Kelch 5"
FT REGION 264..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 70347 MW; 885AFA940D17A862 CRC64;
MALPIDPMEE PRMYQQTLLQ DGLYDLLESD MMVDCVLKIK DKEFPCHRLV LAACSSYFRA
FFKSGVEESK QREIVLEDVE PGVMGIILKY LYTSNINVTE QNVQDIFALS NMLQIPSIFT
VCVSFLQKRL SLSNCLAIFR LGLMLDCPRL AISARNFACE RFQFITRDEE FLQLTPSELA
AVLASDSLNV ETEQDVFEAL IKWVGHDQEN RIGDLPDLLD CIRLRLVPRD YFVKNVEKHE
WLSSNPEITK KLQLVKDAHA GKLPELKKTK NKKSPSEEGQ KKGDEEEVEE EEEQEERLPG
ILNDNLRFGM FLRELIFLIN DSASVAYDPT GNDCYVASVS TQIPKNHCSL VTKENQIFVA
GGLFFDEQSK DEQIYSYFLQ FDPASSDWMG MPPIPSPRFL FGMGEAENFI FVIGGREMKE
GENILNTVMV YDRQFLKWAE SDPLPYLVYG HGVVSHNEMI YVIGGKGENK ECLNRVCAYD
IKTHQWKDLA PLNTARSLFG VTIHKNNIYV VAGVTDSGLT GSAEVYDIKT NKWSEFVEFP
QDRSSLSLVS VSGVLYAVGG FAMFPKEDSD DLMPLEMNDI WRYDESERTW SGILRENRYA
SGATVLGVRL NTLRLTKM
