LRC41_MOUSE
ID LRC41_MOUSE Reviewed; 807 AA.
AC Q8K1C9; A2A911; Q3U3S2; Q6IQY7; Q91VX4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Leucine-rich repeat-containing protein 41;
DE AltName: Full=Protein Muf1;
GN Name=Lrrc41; Synonyms=Muf1;
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 MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-807.
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Retina;
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 PARTIAL PROTEIN SEQUENCE, RECONSTRUCTION FROM ESTS, MUTAGENESIS OF LEU-46
RP AND CYS-50, AND IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEX WITH CUL5.
RX PubMed=11384984; DOI=10.1074/jbc.m103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can
RT assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
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).
CC -!- FUNCTION: Probable substrate recognition component of an ECS (Elongin
CC BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of an E3 ubiquitin-protein ligase complex with Elongin BC
CC (ELOB and ELOC), RBX1 and CUL5. Component of a probable ECS(LRRC41)
CC complex which contains CUL5, RNF7/RBX2, Elongin BC and LRRC41.
CC Interacts with CUL5, RNF7, ELOB and ELOC (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The Elongin BC complex binding domain is also known as BC-box
CC with the consensus [APST]-L-x(3)-C-x(3)-[AILV].
CC -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22976.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK154613; BAE32713.1; -; mRNA.
DR EMBL; AL627105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007169; AAH07169.1; -; mRNA.
DR EMBL; BC022976; AAH22976.2; ALT_INIT; mRNA.
DR EMBL; BC071258; AAH71258.1; -; mRNA.
DR CCDS; CCDS84786.1; -.
DR RefSeq; NP_705741.3; NM_153521.2.
DR AlphaFoldDB; Q8K1C9; -.
DR SMR; Q8K1C9; -.
DR BioGRID; 230994; 10.
DR IntAct; Q8K1C9; 4.
DR STRING; 10090.ENSMUSP00000030471; -.
DR iPTMnet; Q8K1C9; -.
DR PhosphoSitePlus; Q8K1C9; -.
DR EPD; Q8K1C9; -.
DR jPOST; Q8K1C9; -.
DR MaxQB; Q8K1C9; -.
DR PaxDb; Q8K1C9; -.
DR PeptideAtlas; Q8K1C9; -.
DR PRIDE; Q8K1C9; -.
DR ProteomicsDB; 290153; -.
DR Antibodypedia; 32783; 141 antibodies from 28 providers.
DR Ensembl; ENSMUST00000030471; ENSMUSP00000030471; ENSMUSG00000028703.
DR GeneID; 230654; -.
DR KEGG; mmu:230654; -.
DR UCSC; uc008ufx.1; mouse.
DR CTD; 10489; -.
DR MGI; MGI:2441984; Lrrc41.
DR VEuPathDB; HostDB:ENSMUSG00000028703; -.
DR eggNOG; ENOG502R5T0; Eukaryota.
DR GeneTree; ENSGT00390000015908; -.
DR HOGENOM; CLU_021836_0_0_1; -.
DR InParanoid; Q8K1C9; -.
DR OMA; PECRFRV; -.
DR OrthoDB; 322569at2759; -.
DR PhylomeDB; Q8K1C9; -.
DR TreeFam; TF335481; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 230654; 2 hits in 65 CRISPR screens.
DR ChiTaRS; Lrrc41; mouse.
DR PRO; PR:Q8K1C9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K1C9; protein.
DR Bgee; ENSMUSG00000028703; Expressed in spermatocyte and 241 other tissues.
DR Genevisible; Q8K1C9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR026137; Leu_rpt_41.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR15354; PTHR15354; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..807
FT /note="Leucine-rich repeat-containing protein 41"
FT /id="PRO_0000096646"
FT REPEAT 482..502
FT /note="LRR 1"
FT REPEAT 513..525
FT /note="LRR 2"
FT REPEAT 526..550
FT /note="LRR 3"
FT REPEAT 608..632
FT /note="LRR 4"
FT REPEAT 638..661
FT /note="LRR 5"
FT REPEAT 696..723
FT /note="LRR 6"
FT REPEAT 726..747
FT /note="LRR 7"
FT REGION 45..54
FT /note="Interaction with Elongin BC complex"
FT /evidence="ECO:0000250"
FT REGION 269..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15345"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15345"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15345"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15345"
FT MUTAGEN 46
FT /note="L->P: No association with Elongin BC complex; when
FT associated with F-50."
FT /evidence="ECO:0000269|PubMed:11384984"
FT MUTAGEN 50
FT /note="C->F: No association with Elongin BC complex; when
FT associated with P-46."
FT /evidence="ECO:0000269|PubMed:11384984"
FT CONFLICT 42..50
FT /note="APPALFELC -> RTRGSTHAS (in Ref. 3; AAH71258)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="G -> E (in Ref. 1; BAE32713)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="F -> Y (in Ref. 1; BAE32713)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="D -> G (in Ref. 1; BAE32713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 88180 MW; 79F6BBF2D4A33B97 CRC64;
MAAPEAWRAR SCWFCEVAAA TTMEATSREA APAKSSASGP SAPPALFELC GRAVSAHMGV
LESGVWALPG PILQSILPLL NIYYLERIEE TALKKGLSTQ AIWRRLWDEL MKTRPSSLES
VTCWRAKFME AFFSHVLRGT IDVSSDKRLC DQRFSPLLHS SRHVRQLTIC NMLQGATELV
AEPNRRVLET LASSLHTLKF RHLLFSDVAA QQSLRQLLHQ LIHHGAVSQV SLYSWPVPES
ALFILILTMS AGFWQPGPGS LPCRLCGEAS RGRAPSRDEG SLLLGSRRPR RDAAERCAAA
LMATRRKSEV KQMPRAVPPT RVTRRSTQES LAIGGTDSKL YLPATSYEAS GTKQPSAPAA
ASASSSTSSK RAPASSASQP KPLKRFKRAA GKKGPRTRQG SGAESEDLYD FVFIVAGEKE
DGEEMEIGEV ACGALDGSDP SCLGLPALEA SQRFRSISTL ELFTVPLSTE AALTLCHLLS
SWVSLESLTL SYNGLGSNIF RLLDSLRALS GQAGCRLRAL HLSDLFSPLP ILELTRAIVR
ALPLLRVLSI RVDHPSQRDN PAVPENAGPP GHIVGDEEIP ENCLEQLEMG FPRGAQPAPL
LCSVLKASGS LQQLSLDSAT FASPQDFGLV LQTLKEHNLS LKRLSFHDMN LADCQSEVLF
LLKNLTLQEI TFSFCRLFEK RPVQFLPEMV AAMKGNSTLK GLRLPGNRLG NAGLLALADV
FSEDSSSSLC QLDISSNCIK PDGLLEFAKR LERWGRGAFG HLRLFQNWLD QDAVTAREAI
RRLRATCHVV SDSWDSTQAF ADYVSTM
