FXL19_MOUSE
ID FXL19_MOUSE Reviewed; 674 AA.
AC Q6PB97; Q7TSH0; Q8BIB4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=F-box/LRR-repeat protein 19;
DE AltName: Full=F-box and leucine-rich repeat protein 19;
GN Name=Fbxl19;
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] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 165-674 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex (By similarity). Binds to DNA
CC containing unmethylated cytidine-phosphate-guanosine (CpG)
CC dinucleotides (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q6PCT2}.
CC -!- SUBUNIT: Directly interacts with SKP1 and CUL1.
CC {ECO:0000250|UniProtKB:Q6P050}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PB97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PB97-2; Sequence=VSP_013017;
CC Name=3;
CC IsoId=Q6PB97-3; Sequence=VSP_013016, VSP_013017;
CC -!- DOMAIN: The CXXC zinc finger mediates binding to DNA containing
CC unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides.
CC {ECO:0000250|UniProtKB:Q6PCT2}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK031431; BAC27400.1; -; mRNA.
DR EMBL; BC053109; AAH53109.1; -; mRNA.
DR EMBL; BC059812; AAH59812.1; -; mRNA.
DR CCDS; CCDS21877.1; -. [Q6PB97-1]
DR CCDS; CCDS90334.1; -. [Q6PB97-2]
DR RefSeq; NP_766336.2; NM_172748.2. [Q6PB97-1]
DR AlphaFoldDB; Q6PB97; -.
DR SMR; Q6PB97; -.
DR BioGRID; 231472; 6.
DR IntAct; Q6PB97; 1.
DR STRING; 10090.ENSMUSP00000033081; -.
DR iPTMnet; Q6PB97; -.
DR PhosphoSitePlus; Q6PB97; -.
DR EPD; Q6PB97; -.
DR jPOST; Q6PB97; -.
DR MaxQB; Q6PB97; -.
DR PaxDb; Q6PB97; -.
DR PeptideAtlas; Q6PB97; -.
DR PRIDE; Q6PB97; -.
DR ProteomicsDB; 267536; -. [Q6PB97-1]
DR ProteomicsDB; 267537; -. [Q6PB97-2]
DR ProteomicsDB; 267538; -. [Q6PB97-3]
DR Antibodypedia; 56437; 110 antibodies from 17 providers.
DR DNASU; 233902; -.
DR Ensembl; ENSMUST00000033081; ENSMUSP00000033081; ENSMUSG00000030811. [Q6PB97-1]
DR Ensembl; ENSMUST00000186207; ENSMUSP00000140303; ENSMUSG00000030811. [Q6PB97-1]
DR Ensembl; ENSMUST00000188580; ENSMUSP00000140021; ENSMUSG00000030811. [Q6PB97-3]
DR Ensembl; ENSMUST00000206893; ENSMUSP00000145616; ENSMUSG00000030811. [Q6PB97-2]
DR GeneID; 233902; -.
DR KEGG; mmu:233902; -.
DR UCSC; uc009jwo.1; mouse. [Q6PB97-1]
DR UCSC; uc009jwp.1; mouse. [Q6PB97-3]
DR CTD; 54620; -.
DR MGI; MGI:3039600; Fbxl19.
DR VEuPathDB; HostDB:ENSMUSG00000030811; -.
DR eggNOG; KOG1632; Eukaryota.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000161914; -.
DR HOGENOM; CLU_003540_0_2_1; -.
DR InParanoid; Q6PB97; -.
DR OMA; TEIPNCW; -.
DR OrthoDB; 324938at2759; -.
DR PhylomeDB; Q6PB97; -.
DR TreeFam; TF338452; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 233902; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Fbxl19; mouse.
DR PRO; PR:Q6PB97; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6PB97; protein.
DR Bgee; ENSMUSG00000030811; Expressed in embryonic brain and 194 other tissues.
DR ExpressionAtlas; Q6PB97; baseline and differential.
DR Genevisible; Q6PB97; MM.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:MGI.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 2.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Leucine-rich repeat; Metal-binding;
KW Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..674
FT /note="F-box/LRR-repeat protein 19"
FT /id="PRO_0000119869"
FT DOMAIN 398..444
FT /note="F-box"
FT REPEAT 472..497
FT /note="LRR 1"
FT REPEAT 498..521
FT /note="LRR 2"
FT REPEAT 561..586
FT /note="LRR 3"
FT REPEAT 587..616
FT /note="LRR 4"
FT REPEAT 617..641
FT /note="LRR 5"
FT REPEAT 642..674
FT /note="LRR 6"
FT ZN_FING 12..58
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT ZN_FING 65..131
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 130..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6PCT2"
FT VAR_SEQ 137..209
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013016"
FT VAR_SEQ 221..263
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013017"
FT CONFLICT 34
FT /note="H -> R (in Ref. 1; BAC27400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 674 AA; 73788 MW; 1986A31BA4E2A55A CRC64;
MSSSSRGPGA GARRRRTRCR RCRACVRTEC GDCHFCRDMK KFGGPGRMKQ SCLLRQCTAP
VLPHTAVCLL CGEAGKEDTV EGEDEKFSLS LMECTICNEI VHPGCLKMGK AEGVINSEIP
NCWECPRCTQ EGRTSKDAGE GPGRRRADNG EEGANLGGGW KLTEEPPPPP PLPRRKGPLP
AGPTPDDVPG PPKRKEREGG NEPPTPRKKV KGGRERHLKK VGGDACLLRG ADPGSPGLLP
PRVLNPSQAF SSCHPGLPPE NWEKPKPPIA SAEGPAVPSP SPQREKLERF KRMCQLLERV
PDTSSSSSDS DSDSDSSGTS LSEDEAPGEA RNGRRPARGS SGEKENRGGR RAIRPGTGGP
LLSWPLGPAP PPRPPQLERH VVRPPPRSPE PDTLPLAAGS DHPLPRAAWL RVFQHLGPRE
LCVCMRVCRT WSRWCYDKRL WPRMDLSRRK SLTPPMLSGV VRRQPRALDL SWTGVSKKQL
MWLLNRLQGL QELVLSGCSW LSVSALGSAP LPALRLLDLR WIEDVKDSQL RELLLPPPDT
KPGQTESRGR LQGVAELRLA GLELTDASLR LLLRHAPQLS ALDLSHCAHV GDPSVHLLTA
PTSPLRETLV HLNLAGCHRL TDHCLPLFRR CPRLRRLDLR SCRQLSPEAC ARLAAAGPPG
PFRCPEEKLL LKDS
