ID   FBX30_RAT               Reviewed;         742 AA.
AC   Q5XI67;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=F-box only protein 30;
GN   Name=Fbxo30;
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 MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
CC   -!- PTM: May be neddylated. Neddylation may be required for E3 ligase
CC       activity (By similarity). {ECO:0000250}.
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DR   EMBL; BC083823; AAH83823.1; -; mRNA.
DR   RefSeq; NP_001007691.1; NM_001007690.1.
DR   RefSeq; XP_006227702.1; XM_006227640.3.
DR   AlphaFoldDB; Q5XI67; -.
DR   SMR; Q5XI67; -.
DR   STRING; 10116.ENSRNOP00000019918; -.
DR   iPTMnet; Q5XI67; -.
DR   PhosphoSitePlus; Q5XI67; -.
DR   jPOST; Q5XI67; -.
DR   PaxDb; Q5XI67; -.
DR   PRIDE; Q5XI67; -.
DR   Ensembl; ENSRNOT00000019918; ENSRNOP00000019918; ENSRNOG00000014852.
DR   GeneID; 308283; -.
DR   KEGG; rno:308283; -.
DR   UCSC; RGD:1359367; rat.
DR   CTD; 84085; -.
DR   RGD; 1359367; Fbxo30.
DR   eggNOG; ENOG502QTD9; Eukaryota.
DR   GeneTree; ENSGT00950000183204; -.
DR   HOGENOM; CLU_013357_0_0_1; -.
DR   InParanoid; Q5XI67; -.
DR   OMA; HTPSFKF; -.
DR   OrthoDB; 1009974at2759; -.
DR   PhylomeDB; Q5XI67; -.
DR   TreeFam; TF343227; -.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5XI67; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000014852; Expressed in testis and 19 other tissues.
DR   Genevisible; Q5XI67; RN.
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..742
FT                   /note="F-box only protein 30"
FT                   /id="PRO_0000119920"
FT   DOMAIN          607..653
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   ZN_FING         49..108
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   REGION          214..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   742 AA;  82011 MW;  93BBE53E36E621C2 CRC64;
     MEEEVQQHSH CVNCVSRRCM TRPEPGVSCD LIGCPLVCGA VFHSCKADEH RLLCPFERVP
     CLNSNFGCPF TLARNKVAEH LEMCPASVVC CTMEWNRWPV SYSDRKSYES LSRDADEVSQ
     LDMALALQDQ RMLLESLKVA TMMSKATGKI SKPREQISVN SSVQEVPRAN GLVSADEESY
     GALYEATVET TRSLAAALDI LNSATRDIGM LNTSLQGTTN EMDEESNRES SQDRNAKDQD
     HLDEGEIGAV GGIDYTGTSQ NAQAEQNGSS DLLCNLNTSS YDTSALCNGF PLEKMCTQVK
     DQDQNFHGDS TESNITNGDC VEADGTSEPP SSLLVAEQLK EGSALPDSTY QHILMPDEDD
     DEDLCWKKDL GDSKDVNGSP LSHATSFKFL SNSWYIPKED KAVDTSDLEV AEDPMGLQGI
     DLITAALLFC LGDSPGGRGI SDSRMVDVYH VDFGTQTFSL PSAILATNTM VGEIASASAC
     DHANPQLSNP SPFQTLGLDL VLECVARYQP KQRSMFTFVC GQLFRRKEFS SHFKNVHGDI
     HAGLNGWMEQ RCPLAYYGCT YSQRRFCPST QGAKIIHDRH LRSFGVQPCV STALEEPSRN
     CVLGLRSDHL SSLPFEVLQH IAGFLDGFSL CQLACVSRLM RDICGSLLQS RGMVILQWGK
     KKYPEGNSSW QIKEKVWRFS TAFCSVNDWK FADILSMADH LKKCSYNVIE KREEAIPLPC
     MCVTRELTKE GRSLRSVLKP VL