KLH41_RAT
ID KLH41_RAT Reviewed; 606 AA.
AC Q9ER30;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Kelch-like protein 41;
DE AltName: Full=Kel-like protein 23;
DE AltName: Full=Kelch repeat and BTB domain-containing protein 10;
DE AltName: Full=Kelch-related protein 1;
DE AltName: Full=Sarcosin;
GN Name=Klhl41; Synonyms=Kbtbd10, Krp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Fibroblast;
RX PubMed=10713668; DOI=10.1038/sj.onc.1203433;
RA Spence H.J., Johnston I.P., Ewart K., Buchanan S.J., Fitzgerald U.,
RA Ozanne B.W.;
RT "Krp1, a novel kelch related protein that is involved in pseudopod
RT elongation in transformed cells.";
RL Oncogene 19:1266-1276(2000).
RN [2]
RP INTERACTION WITH NRAP.
RX PubMed=12692149; DOI=10.1242/jcs.00425;
RA Lu S., Carroll S.L., Herrera A.H., Ozanne B., Horowits R.;
RT "New N-RAP-binding partners alpha-actinin, filamin and Krp1 detected by
RT yeast two-hybrid screening: implications for myofibril assembly.";
RL J. Cell Sci. 116:2169-2178(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 289-606, AND INTERACTION WITH
RP LASP1.
RX PubMed=19726686; DOI=10.1074/jbc.m109.023259;
RA Gray C.H., McGarry L.C., Spence H.J., Riboldi-Tunnicliffe A., Ozanne B.W.;
RT "Novel beta-propeller of the BTB-Kelch protein Krp1 provides a binding site
RT for Lasp-1 that is necessary for pseudopodial extension.";
RL J. Biol. Chem. 284:30498-30507(2009).
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:0000250|UniProtKB:A2AUC9,
CC ECO:0000269|PubMed:10713668}.
CC -!- SUBUNIT: Interacts with NRAP. Part of a complex that contains CUL3,
CC RBX1 and KLHL41. Interacts with LASP1. {ECO:0000250,
CC ECO:0000269|PubMed:12692149, ECO:0000269|PubMed:19726686}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10713668}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10713668}. Cell projection,
CC pseudopodium {ECO:0000269|PubMed:10713668}. Cell projection, ruffle
CC {ECO:0000269|PubMed:10713668}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000250|UniProtKB:A2AUC9}. Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O60662}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O60662}. 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: Primarily expressed in skeletal muscle. Also found
CC in heart and lung.
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; AJ293948; CAC08185.1; -; mRNA.
DR RefSeq; NP_476539.1; NM_057191.1.
DR PDB; 2WOZ; X-ray; 2.00 A; A=289-606.
DR PDBsum; 2WOZ; -.
DR AlphaFoldDB; Q9ER30; -.
DR SMR; Q9ER30; -.
DR IntAct; Q9ER30; 2.
DR STRING; 10116.ENSRNOP00000009969; -.
DR iPTMnet; Q9ER30; -.
DR PhosphoSitePlus; Q9ER30; -.
DR PaxDb; Q9ER30; -.
DR PRIDE; Q9ER30; -.
DR Ensembl; ENSRNOT00000009969; ENSRNOP00000009969; ENSRNOG00000007461.
DR GeneID; 117537; -.
DR KEGG; rno:117537; -.
DR UCSC; RGD:620852; rat.
DR CTD; 10324; -.
DR RGD; 620852; Klhl41.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000158859; -.
DR HOGENOM; CLU_004253_14_4_1; -.
DR InParanoid; Q9ER30; -.
DR OMA; FQSYFFQ; -.
DR OrthoDB; 946131at2759; -.
DR PhylomeDB; Q9ER30; -.
DR TreeFam; TF351653; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR EvolutionaryTrace; Q9ER30; -.
DR PRO; PR:Q9ER30; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000007461; Expressed in skeletal muscle tissue and 14 other tissues.
DR Genevisible; Q9ER30; RN.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031430; C:M band; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0031143; C:pseudopodium; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030239; P:myofibril assembly; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:0031269; P:pseudopodium assembly; IMP:RGD.
DR GO; GO:0045661; P:regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:2000291; P:regulation of myoblast proliferation; ISS:UniProtKB.
DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0045214; P:sarcomere organization; IEA:InterPro.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISS: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 3D-structure; Cell projection; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Kelch repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Sarcoplasmic reticulum; Ubl conjugation.
FT CHAIN 1..606
FT /note="Kelch-like protein 41"
FT /id="PRO_0000119089"
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:0007744|PubMed:22673903"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:2WOZ"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:2WOZ"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 399..407
FT /evidence="ECO:0007829|PDB:2WOZ"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:2WOZ"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:2WOZ"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 496..504
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 507..516
FT /evidence="ECO:0007829|PDB:2WOZ"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:2WOZ"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:2WOZ"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:2WOZ"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:2WOZ"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:2WOZ"
SQ SEQUENCE 606 AA; 68213 MW; 08DB54E9298DEACE CRC64;
MDSQRELAEE LRLYQSTLLQ DGLKDLLEEK KFIDCTLKAG DKSFPCHRLI LSACSPYFRE
YFLSEIEEEK KKEMALDNVD PAILDLIIKY LYSASIDLND GNVQDIFALS SRFQIPSVFT
VCVSYLQKRL APGNCLAILR LGLLLDCPRL AISAREFVSD RFVQICKEED FMQLSPQELI
SVISNDSLNV EKEEVVFEAV MKWVRTDKEN RAKNLSEVFD CIRFRLMAEK YFKDHVEKDD
IIKSNPEVQK KIKVLKDAFA GKLPEPSKSA EKGGTGEVNG DVGDEDLLPG YLNDIPRHGM
FVKDLILLVN DTAAVAYDPM ENECYLTALA EQIPRNHSSI VTQQNQVYVV GGLYVDEENK
DQPLQSYFFQ LDNVSSEWVG LPPLPSARCL FGLGEVDDKI YVVAGKDLQT EASLDSVLCY
DPVAAKWSEV KNLPIKVYGH NVISHNGMIY CLGGKTDDKK CTNRVFIYNP KKGDWKDLAP
MKTPRSMFGV AIHKGKIVIA GGVTEDGLSA SVEAFDLKTN KWEVMTEFPQ ERSSISLVSL
AGSLYAIGGF AMIQLESKEF APTEVNDIWK YEDDKKEWAG MLKEIRYASG ASCLATRLNL
FKLSKL
