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   15-FEB-2017, entry version 93.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
RT   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.,
RA   Shiina M., Ogata K., Hsu C., Clarke N.F., Darras B.T., Farrar M.A.,
RA   Hashem A., Manton N.D., Muntoni F., North K.N., Sandaradura S.A.,
RA   Nishino I., Hayashi Y.K., Sewry C.A., Thompson E.M., Yau K.S.,
RA   Brownstein C.A., Yu T.W., Allcock R.J., Davis M.R.,
RA   Wallgren-Pettersson C., Matsumoto N., Alkuraya F.S., Laing N.G.,
RA   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
CC       differentiation. Regulates proliferation and differentiation of
CC       myoblasts and plays a role in myofibril assembly by promoting
CC       lateral fusion of adjacent thin fibrils into mature, wide
CC       myofibrils. Required for pseudopod elongation in transformed
CC       cells. {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:21368295,
CC       ECO:0000269|PubMed:22562206}.
CC   -!- SUBUNIT: Interacts with NRAP. Part of a complex that contains
CC       CUL3, RBX1 and KLHL41. Interacts with LASP1.
CC       {ECO:0000250|UniProtKB:O60662, 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
CC       line {ECO:0000269|PubMed:22562206}. Sarcoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:24268659}. Endoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:24268659}. Note=Predominantly
CC       cytoplasmic but can colocalize with F-actin at the membrane
CC       ruffle-like structures at the tips of transformation-specific
CC       pseudopodia.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle. Localized between laterally
CC       fusing myofibrils in skeletal muscle (at protein level). Expressed
CC       at a lower 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
CC       expressed in the developing heart at these embryonic stages.
CC       {ECO:0000269|PubMed:22562206}.
CC   -!- PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3
CC       and RBX1 and probably targeted for proteasome-independent
CC       degradation. Quinone-induced oxidative stress increases its
CC       ubiquitination. {ECO:0000250|UniProtKB:O60662}.
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DR   EMBL; AL929083; CAM24293.1; -; 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   UniGene; Mm.178784; -.
DR   ProteinModelPortal; A2AUC9; -.
DR   SMR; A2AUC9; -.
DR   BioGrid; 230702; 2.
DR   STRING; 10090.ENSMUSP00000097627; -.
DR   iPTMnet; A2AUC9; -.
DR   PhosphoSitePlus; A2AUC9; -.
DR   MaxQB; A2AUC9; -.
DR   PaxDb; A2AUC9; -.
DR   PeptideAtlas; A2AUC9; -.
DR   PRIDE; A2AUC9; -.
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   eggNOG; KOG4441; Eukaryota.
DR   eggNOG; ENOG410XNX8; LUCA.
DR   GeneTree; ENSGT00870000136401; -.
DR   HOGENOM; HOG000231966; -.
DR   HOVERGEN; HBG052215; -.
DR   InParanoid; A2AUC9; -.
DR   KO; K10473; -.
DR   OMA; FFQLDNV; -.
DR   OrthoDB; EOG090B046G; -.
DR   PhylomeDB; A2AUC9; -.
DR   TreeFam; TF351653; -.
DR   PRO; PR:A2AUC9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000075307; -.
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:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0031430; C:M band; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
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:0031275; P:regulation of lateral pseudopodium assembly; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IDA:UniProtKB.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IBA:GO_Central.
DR   Gene3D; 2.120.10.80; -; 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.
DR   PANTHER; PTHR24412:SF260; PTHR24412:SF260; 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; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Endoplasmic reticulum; Kelch repeat; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Sarcoplasmic reticulum; Ubl conjugation.
FT   CHAIN         1    606       Kelch-like protein 41.
FT                                /FTId=PRO_0000421252.
FT   DOMAIN       33    100       BTB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00037}.
FT   DOMAIN      135    237       BACK.
FT   REPEAT      346    398       Kelch 1.
FT   REPEAT      399    447       Kelch 2.
FT   REPEAT      448    495       Kelch 3.
FT   REPEAT      497    542       Kelch 4.
FT   REPEAT      544    599       Kelch 5.
FT   MOD_RES       3      3       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9ER30}.
FT   CONFLICT    404    404       A -> S (in Ref. 3; AAI50699).
FT                                {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
//