KLH41_MOUSE
ID KLH41_MOUSE Reviewed; 606 AA.
AC A2AUC9; B2RWT7;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Kelch-like protein 41;
DE AltName: Full=Kelch repeat and BTB domain-containing protein 10;
GN Name=Klhl41; Synonyms=Kbtbd10;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18178185; DOI=10.1016/j.yexcr.2007.12.009;
RA Greenberg C.C., Connelly P.S., Daniels M.P., Horowits R.;
RT "Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly
RT intermediates in cultured mouse cardiomyocytes.";
RL Exp. Cell Res. 314:1177-1191(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21368295; DOI=10.1152/ajpcell.00321.2010;
RA Paxton C.W., Cosgrove R.A., Drozd A.C., Wiggins E.L., Woodhouse S.,
RA Watson R.A., Spence H.J., Ozanne B.W., Pell J.M.;
RT "BTB-Kelch protein Krp1 regulates proliferation and differentiation of
RT myoblasts.";
RL Am. J. Physiol. 300:C1345-C1355(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=22562206; DOI=10.1387/ijdb.113327lp;
RA du Puy L., Beqqali A., van Tol H.T., Monshouwer-Kloots J., Passier R.,
RA Haagsman H.P., Roelen B.A.;
RT "Sarcosin (Krp1) in skeletal muscle differentiation: gene expression
RT profiling and knockdown experiments.";
RL Int. J. Dev. Biol. 56:301-309(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=24268659; DOI=10.1016/j.ajhg.2013.10.020;
RA Gupta V.A., Ravenscroft G., Shaheen R., Todd E.J., Swanson L.C., Shiina M.,
RA Ogata K., Hsu C., Clarke N.F., Darras B.T., Farrar M.A., Hashem A.,
RA Manton N.D., Muntoni F., North K.N., Sandaradura S.A., Nishino I.,
RA Hayashi Y.K., Sewry C.A., Thompson E.M., Yau K.S., Brownstein C.A.,
RA Yu T.W., Allcock R.J., Davis M.R., Wallgren-Pettersson C., Matsumoto N.,
RA Alkuraya F.S., Laing N.G., Beggs A.H.;
RT "Identification of KLHL41 mutations implicates BTB-Kelch-mediated
RT ubiquitination as an alternate pathway to myofibrillar disruption in
RT nemaline myopathy.";
RL Am. J. Hum. Genet. 93:1108-1117(2013).
CC -!- FUNCTION: Involved in skeletal muscle development and differentiation.
CC Regulates proliferation and differentiation of myoblasts and plays a
CC role in myofibril assembly by promoting lateral fusion of adjacent thin
CC fibrils into mature, wide myofibrils. Required for pseudopod elongation
CC in transformed cells. {ECO:0000269|PubMed:18178185,
CC ECO:0000269|PubMed:21368295, ECO:0000269|PubMed:22562206}.
CC -!- SUBUNIT: Interacts with NRAP. Part of a complex that contains CUL3,
CC RBX1 and KLHL41. Interacts with LASP1. {ECO:0000250|UniProtKB:O60662,
CC ECO:0000250|UniProtKB:Q9ER30}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18178185,
CC ECO:0000269|PubMed:22562206}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18178185}. Cell projection, pseudopodium
CC {ECO:0000250|UniProtKB:Q9ER30}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q9ER30}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:22562206}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24268659}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24268659}. Note=Predominantly cytoplasmic but can
CC colocalize with F-actin at the membrane ruffle-like structures at the
CC tips of transformation-specific pseudopodia.
CC -!- TISSUE SPECIFICITY: Skeletal muscle. Localized between laterally fusing
CC myofibrils in skeletal muscle (at protein level). Expressed at a lower
CC level in the heart compared to skeletal muscle.
CC {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:22562206}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the myotome part of the mature
CC somites in embryos from embryonic day 9.5 onwards. It is not expressed
CC in the developing heart at these embryonic stages.
CC {ECO:0000269|PubMed:22562206}.
CC -!- PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and
CC RBX1 and probably targeted for proteasome-independent degradation.
CC Quinone-induced oxidative stress increases its ubiquitination.
CC {ECO:0000250|UniProtKB:O60662}.
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DR EMBL; AL929083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27039.1; -; Genomic_DNA.
DR EMBL; BC150698; AAI50699.1; -; mRNA.
DR CCDS; CCDS38136.1; -.
DR RefSeq; NP_001074556.1; NM_001081087.1.
DR AlphaFoldDB; A2AUC9; -.
DR SMR; A2AUC9; -.
DR BioGRID; 230702; 7.
DR CORUM; A2AUC9; -.
DR STRING; 10090.ENSMUSP00000097627; -.
DR iPTMnet; A2AUC9; -.
DR PhosphoSitePlus; A2AUC9; -.
DR MaxQB; A2AUC9; -.
DR PaxDb; A2AUC9; -.
DR PeptideAtlas; A2AUC9; -.
DR PRIDE; A2AUC9; -.
DR ProteomicsDB; 263630; -.
DR Antibodypedia; 35006; 208 antibodies from 26 providers.
DR Ensembl; ENSMUST00000100050; ENSMUSP00000097627; ENSMUSG00000075307.
DR GeneID; 228003; -.
DR KEGG; mmu:228003; -.
DR UCSC; uc008jyg.1; mouse.
DR CTD; 10324; -.
DR MGI; MGI:2683854; Klhl41.
DR VEuPathDB; HostDB:ENSMUSG00000075307; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000158859; -.
DR HOGENOM; CLU_004253_14_4_1; -.
DR InParanoid; A2AUC9; -.
DR OMA; FQSYFFQ; -.
DR OrthoDB; 946131at2759; -.
DR PhylomeDB; A2AUC9; -.
DR TreeFam; TF351653; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 228003; 2 hits in 73 CRISPR screens.
DR PRO; PR:A2AUC9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AUC9; protein.
DR Bgee; ENSMUSG00000075307; Expressed in knee joint and 82 other tissues.
DR Genevisible; A2AUC9; MM.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031143; C:pseudopodium; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030239; P:myofibril assembly; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0031269; P:pseudopodium assembly; ISO:MGI.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:2000291; P:regulation of myoblast proliferation; IMP:UniProtKB.
DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0045214; P:sarcomere organization; IEA:InterPro.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IDA:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:InterPro.
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; IPR030571; KLHL41.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF146; PTHR24412:SF146; 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 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Kelch repeat; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Ubl conjugation.
FT CHAIN 1..606
FT /note="Kelch-like protein 41"
FT /id="PRO_0000421252"
FT DOMAIN 33..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 135..237
FT /note="BACK"
FT REPEAT 346..398
FT /note="Kelch 1"
FT REPEAT 399..447
FT /note="Kelch 2"
FT REPEAT 448..495
FT /note="Kelch 3"
FT REPEAT 497..542
FT /note="Kelch 4"
FT REPEAT 544..599
FT /note="Kelch 5"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER30"
FT CONFLICT 404
FT /note="A -> S (in Ref. 3; AAI50699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 68190 MW; 952AEB63BBE84DDA CRC64;
MDSQRELAEE LRLYQSTLLQ DGLKDLLEEK KFIDCTLKAG DKSFPCHRLI LSACSPYFRE
YFLSEIEEEK KKEVALDNVD PAILDLIIKY LYSASIDLND GNVQDIFALS SRFQIPSVFT
VCVSYLQKRL APGNCLAILR LGLLLDCPRL AISAREFVSD RFVQICKEED FMQLSPQELI
SVISNDSLNV EKEEVVFEAV MKWVRTDKEN RAKNLSEVFD CIRFRLMAEK YFKDHVEKDD
IIKSNPEVQK KIKVLKDAFA GKLPEPSKNA EKAGAGEVNG DVGDEDLLPG YLNDIPRHGM
FVKDLILLVN DTAAVAYDPM ENECYLTALA EQIPRNHSSL VTQQNQVYVV GGLYVDEENK
DQPLQSYFFQ LDNVTSEWVG LPPLPSARCL FGLGEVDDKI YVVAGKDLQT EASLDSVLCY
DPVAAKWSEV KNLPIKVYGH NVISHNGMIY CLGGKTDDKK CTNRVFIYNP KKGDWKDLAP
MKTPRSMFGV AIHKGKIVIA GGVTEDGLSA SVEAFDLKTN KWEVMTEFPQ ERSSISLVSL
AGALYAIGGF AMIQLESKEF APTEVNDIWK YEDDKKEWAG MLKEIRYASG ASCLATRLNL
FKLSKL
