FBSP1_RAT
ID FBSP1_RAT Reviewed; 230 AA.
AC P0CH38;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=F-box/SPRY domain-containing protein 1;
DE AltName: Full=F-box only protein 45;
DE Flags: Fragment;
GN Name=Fbxo45;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19996097; DOI=10.1074/jbc.m109.046284;
RA Tada H., Okano H.J., Takagi H., Shibata S., Yao I., Matsumoto M., Saiga T.,
RA Nakayama K.I., Kashima H., Takahashi T., Setou M., Okano H.;
RT "Fbxo45, a novel ubiquitin ligase, regulates synaptic activity.";
RL J. Biol. Chem. 285:3840-3849(2010).
CC -!- FUNCTION: Component of E3 ubiquitin ligase complexes (By similarity).
CC Required for normal neuromuscular synaptogenesis, axon pathfinding and
CC neuronal migration (By similarity). Plays a role in the regulation of
CC neurotransmission at mature neurons. May control synaptic activity by
CC controlling UNC13A via ubiquitin dependent pathway (By similarity).
CC Specifically recognizes TP73, promoting its ubiquitination and
CC degradation (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19996097}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms a complex with MYCBP2 and SKP1 but does not appear to
CC form an authentic SCF (SKP1-CUL1-F-box protein) complex. Interacts (via
CC B30.2/SPRY domain) with TP73 (via SAM domain); leading to its
CC ubiquitination and degradation. Interacts (via SRY domain) with UNC13A;
CC leading to its degradation by the proteasome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:19996097}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:19996097}.
CC -!- SIMILARITY: Belongs to the FBXO45/Fsn family. {ECO:0000305}.
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DR AlphaFoldDB; P0CH38; -.
DR SMR; P0CH38; -.
DR STRING; 10116.ENSRNOP00000002391; -.
DR PaxDb; P0CH38; -.
DR PRIDE; P0CH38; -.
DR RGD; 1311861; Fbxo45.
DR eggNOG; KOG3953; Eukaryota.
DR InParanoid; P0CH38; -.
DR PhylomeDB; P0CH38; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0021960; P:anterior commissure morphogenesis; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR GO; GO:0021800; P:cerebral cortex tangential migration; ISO:RGD.
DR GO; GO:0021957; P:corticospinal tract morphogenesis; ISO:RGD.
DR GO; GO:0060384; P:innervation; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:0060386; P:synapse assembly involved in innervation; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR CDD; cd12907; SPRY_Fbox; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035784; SPRY_FBXO45.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell projection; Developmental protein; Membrane;
KW Neurogenesis; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Ubl conjugation pathway.
FT CHAIN <1..230
FT /note="F-box/SPRY domain-containing protein 1"
FT /id="PRO_0000397032"
FT DOMAIN 36..228
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT NON_TER 1
SQ SEQUENCE 230 AA; 25759 MW; F79E400168164EAB CRC64;
LASRALVCKH WYRCLHGDEN SEVWRSLCAR SLEEAMRTDI LCNLPSYKAK VRAFQHAFST
NDCSRNVYIK KNGFTLHRNP IAQSTDGART KIGFSEGRHA WEVWWEGPLG TVAVIGIATK
RAPMQCQGYV ALLGSDDQSW GWNLVDNNLL HNGEVNGSFP QCNNAPKYQI GERIRVILDM
EDKTLAFERG YEFLGVAFRG LPKACLYPAV SAVYGNTEVT LVYLGKPLDG
