FBX30_MOUSE
ID FBX30_MOUSE Reviewed; 746 AA.
AC Q8BJL1; Q3UXU4; Q8CI21; Q9D9X5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=F-box only protein 30;
DE AltName: Full=Muscle ubiquitin ligase of SCF complex in atrophy-1;
DE Short=MUSA1;
GN Name=Fbxo30;
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=C57BL/6J; TISSUE=Testis, and Wolffian duct;
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].
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] OF 320-746.
RC STRAIN=FVB/N;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Spleen;
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 [5]
RP FUNCTION, IDENTIFICATION IN SCF COMPLEX, AUTOUBIQUITINATION, AND INDUCTION.
RX PubMed=24076600; DOI=10.1038/ng.2772;
RA Sartori R., Schirwis E., Blaauw B., Bortolanza S., Zhao J., Enzo E.,
RA Stantzou A., Mouisel E., Toniolo L., Ferry A., Stricker S., Goldberg A.L.,
RA Dupont S., Piccolo S., Amthor H., Sandri M.;
RT "BMP signaling controls muscle mass.";
RL Nat. Genet. 45:1309-1318(2013).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex. Required for muscle atrophy
CC following denervation. {ECO:0000269|PubMed:24076600}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC Interacts with SKP1, CUL1 and RBX1/ROC1. {ECO:0000269|PubMed:24076600}.
CC -!- INDUCTION: Up-regulated in denervated muscles (at protein level), with
CC highest expression levels around 14 days following denervation.
CC Negatively regulated by the bone morphogenetic protein (BMP) pathway.
CC {ECO:0000269|PubMed:24076600}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:24076600}.
CC -!- PTM: May be neddylated. Neddylation may be required for E3 ligase
CC activity, since it was observed only after purification with o-
CC phenanthroline (PubMed:24076600). {ECO:0000269|PubMed:24076600}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK006369; BAB24551.1; -; mRNA.
DR EMBL; AK083479; BAC38931.1; -; mRNA.
DR EMBL; AK135274; BAE22469.1; -; mRNA.
DR EMBL; CH466562; EDL03517.1; -; Genomic_DNA.
DR EMBL; BC037691; AAH37691.1; ALT_INIT; mRNA.
DR CCDS; CCDS23697.1; -.
DR RefSeq; NP_001161769.1; NM_001168297.1.
DR RefSeq; NP_082244.2; NM_027968.3.
DR RefSeq; XP_006512922.1; XM_006512859.3.
DR AlphaFoldDB; Q8BJL1; -.
DR SMR; Q8BJL1; -.
DR BioGRID; 214990; 2.
DR MINT; Q8BJL1; -.
DR STRING; 10090.ENSMUSP00000117687; -.
DR iPTMnet; Q8BJL1; -.
DR PhosphoSitePlus; Q8BJL1; -.
DR EPD; Q8BJL1; -.
DR MaxQB; Q8BJL1; -.
DR PaxDb; Q8BJL1; -.
DR PeptideAtlas; Q8BJL1; -.
DR PRIDE; Q8BJL1; -.
DR ProteomicsDB; 267350; -.
DR Antibodypedia; 33222; 53 antibodies from 14 providers.
DR Ensembl; ENSMUST00000070300; ENSMUSP00000068230; ENSMUSG00000047648.
DR Ensembl; ENSMUST00000129456; ENSMUSP00000117687; ENSMUSG00000047648.
DR GeneID; 71865; -.
DR KEGG; mmu:71865; -.
DR UCSC; uc007ejt.2; mouse.
DR CTD; 84085; -.
DR MGI; MGI:1919115; Fbxo30.
DR VEuPathDB; HostDB:ENSMUSG00000047648; -.
DR eggNOG; ENOG502QTD9; Eukaryota.
DR GeneTree; ENSGT00950000183204; -.
DR HOGENOM; CLU_013357_0_0_1; -.
DR InParanoid; Q8BJL1; -.
DR OMA; HTPSFKF; -.
DR OrthoDB; 1009974at2759; -.
DR PhylomeDB; Q8BJL1; -.
DR TreeFam; TF343227; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 71865; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fbxo30; mouse.
DR PRO; PR:Q8BJL1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BJL1; protein.
DR Bgee; ENSMUSG00000047648; Expressed in spermatid and 220 other tissues.
DR Genevisible; Q8BJL1; MM.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.40.150; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR031890; Fbxo30/Fbxo40.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001293; Znf_TRAF.
DR InterPro; IPR043013; Znf_TRAF_N.
DR PANTHER; PTHR15933; PTHR15933; 1.
DR Pfam; PF15966; F-box_4; 1.
DR Pfam; PF15965; zf-TRAF_2; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..746
FT /note="F-box only protein 30"
FT /id="PRO_0000119919"
FT DOMAIN 611..659
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT ZN_FING 49..110
FT /note="TRAF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT REGION 222..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI67"
FT CONFLICT 87
FT /note="S -> G (in Ref. 1; BAB24551)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="A -> P (in Ref. 1; BAC38931)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="C -> G (in Ref. 1; BAB24551)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="L -> S (in Ref. 1; BAB24551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 82687 MW; FD88404AFC9560D0 CRC64;
MEEEVQQHSH CMNCVSRRCM TRPEPGVSCD LIGCPLVCGA VFHSCKADEH RLLCPFERVA
CLNRNFGCPF TLARNKVAEH LEMCPASVVC CTMEWNRWPV SYSDRKSYES LSRDVDEVAQ
LDMALALQDQ RMLLESLKVA TMMSKATDKI SEPREQISVK SSVQEIPRTN GLVSVDEESY
GALYQATVET TRSLAAALDI LNSATRDIGM LNTSLHATAN EMDEENNKES FQDKNLKDQD
HLDEGEIGAV GGVDYSGTSQ NAQAEQNGSS DLLCDLNPSS NGTSALCNGF PLEKMCIQVK
GQDQNFHGDS TESNITNGDC VEADGTSEPS SSLVVPEQLR EISPFSALPD STFQQILMPD
EDDEKDLCWK KVDLGDLKDV NGSPFSHAPS FKFLSNSWYI PKEDKAVDTS DLEVAEDPMG
LQGIDLITAA LLFCLGDSPG GRGISDSRMT DVYHVDFGTQ TFSLPSAILA TNTMVGEIAS
ASACDHANPQ LSNPSPFQTL GLDLVLECVA RYQPKQRSMF TFVCGQLFRR KEFSSHFKNV
HGDIHAGLNG WMEQRCPLAY YGCTYSQRRF CPSTQGAKII HDRHLRSFGV QPCVSTVLEE
PSRNCVLGLR SDHLSSLPFE VLQHIAGFLD GFSLCQLACV SRLMRDVCGS LLQSRGMVIL
QWGKKKYPEG NSSWQIKEKV WRFSTAFCSV NDWKFADILS MADHLKNCSY NVIEKREEAI
PLPCMCVTRE LTKEGRSLRS VLKPVL
