D4ABB4 (FXL15_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
F-box/LRR-repeat protein 15

Gene names

Name:

Fbxl15

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Substrate recognition component of a (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation. Also mediates ubiquitination of SMURF2 and WWP2 By similarity. Required for bone mass maintenance. Ref.3
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL15) composed of CUL1, SKP1, RBX1 and FBXL15 By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the FBXL15 family. Contains 1 F-box domain. Contains 5 LRR (leucine-rich) repeats.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Domain	Leucine-rich repeat Repeat
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB bone mineralization Inferred from mutant phenotype Ref.3. Source: UniProtKB dorsal/ventral pattern formation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of BMP signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB protein ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	SCF ubiquitin ligase complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 300	300	F-box/LRR-repeat protein 15		PRO_0000410905
Regions
	Domain	19 – 66	48	F-box
	Repeat	141 – 162	22	LRR 1
	Repeat	167 – 188	22	LRR 2
	Repeat	194 – 215	22	LRR 3
	Repeat	220 – 241	22	LRR 4
	Repeat	246 – 267	22	LRR 5
	Region	113 – 269	157	Interaction with SMURF1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	D4ABB4 [UniParc]. Last modified April 20, 2010. Version 1. Checksum: 43FE513A84A5E1F0	FASTA	300	33,180
	10 20 30 40 50 60 MEPPMEQSGG EQEPGAVRLL DLPWEDVLLP HVLNWVPLRQ LLRLQRVSRA FRALVQLHLA 70 80 90 100 110 120 RLRRFDAAQV GPQIPRAALV RLLRDAEGLQ ELALAPCHEW LLDEDLVPVL ARNPQLRSVA 130 140 150 160 170 180 LAGCGQLSRR ALGALAEGCP RLQRISLAHC DWVDGLALRG LADRCPALEE LDLTACRQLK 190 200 210 220 230 240 DEAIVYLAQR RGAGLRSLSL AVNANVGDTA VQELARNCPQ LEHLDLTGCL RVGSDGVRTL 250 260 270 280 290 300 AEYCPALRSL RVRHCHHVAE PSLSRLRKRG VDIDVEPPLH QALVLLQDMA GFAPFVNLQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1." Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L. EMBO J. 30:2675-2689(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC096363 Genomic DNA. No translation available. CH473986 Genomic DNA. Translation: EDL94345.1.
IPI	IPI00370390.
RefSeq	NP_001101073.1. NM_001107603.1.
UniGene	Rn.49395.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	D4ABB4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000026471; ENSRNOP00000026471; ENSRNOG00000019509.
GeneID	309453.
KEGG	rno:309453.
Organism-specific databases
CTD	79176.
RGD	1306444. Fbxl15.
Phylogenomic databases
GeneTree	ENSGT00700000104313.
KO	K10281.
OMA	CEWVDSL.
OrthoDB	EOG47PX6H.
Enzyme and pathway databases
UniPathway	UPA00143.
Family and domain databases
InterPro	IPR001810. F-box_dom_cyclin-like. [Graphical view]
Pfam	PF00646. F-box. 1 hit. [Graphical view]
SUPFAM	SSF81383. F-box_dom_Skp2-like. 1 hit.
PROSITE	PS50181. FBOX. False negative. PS51450. LRR. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	660814.

Entry information

Entry name

FXL15_RAT

Accession

Primary (citable) accession number: D4ABB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 28, 2011
Last sequence update:	April 20, 2010
Last modified:	March 6, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program