F-box/LRR-repeat protein 17 (F-box and leucine-rich repeat protein 17) (F-box only protein 13)
1_MGHLL 6_ SKEPR 11_ NRPSQ 16_ KRPRC 21_ CSWCR 26_ RRRPL 31_ LRLPR 36_ RTPAK 41_ VPPQP 46_ AAPRS 51_ RDCFF 56_ RGPCM 61_ LCFIV 66_ HSPGA 71_ PAPAG 76_ PEEEP 81_ PLSPP 86_ PRDGA 91_ YAAAS 96_ SSQHL 101_ ARRYA 106_ ALAAE 111_ DCAAA 116_ ARRFL 121_ LSSAA 126_ AAAAA 131_ AASAS 136_ SPASC 141_ CKELG 146_ LAAAA 151_ AWEQQ 156_ GRSLF 161_ LASLG 166_ PVRFL 171_ GPPAA 176_ VQLFR 181_ GPTPS 186_ PAELP 191_ TPPEM 196_ VCKRK 201_ GAGVP 206_ ACTPC 211_ KQPRC 216_ GGGGC 221_ GGGGG 226_ GGGGG 231_ GPAGG 236_ GASPP 241_ RPPDA 246_ GCCQA 251_ PEQPP 256_ QPLCP 261_ PPSSP 266_ TSEGA 271_ PTEAG 276_ GDAVR 281_ AGGTA 286_ PLSAQ 291_ QQHEC 296_ GDADC 301_ RESPE 306_ NPCDC 311_ HREPP 316_ PETPD 321_ INQLP 326_ PSILL 331_ KIFSN 336_ LSLDE 341_ RCLSA 346_ SLVCK 351_ YWRDL 356_ CLDFQ 361_ FWKQL 366_ DLSSR 371_ QQVTD 376_ ELLEK 381_ IASRS 386_ QNIIE 391_ INISD 396_ CRSMS 401_ DNGVC 406_ VLAFK 411_ CPGLL 416_ RYTAY 421_ RCKQL 426_ SDTSI 431_ IAVAS 436_ HCPLL 441_ QKVHV 446_ GNQDK 451_ LTDEG 456_ LKQLG 461_ SKCRE 466_ LKDIH 471_ FGQCY 476_ KISDE 481_ GMIVI 486_ AKGCL 491_ KLQRI 496_ YMQEN 501_ KLVTD 506_ QSVKA 511_ FAEHC 516_ PELQY 521_ VGFMG 526_ CSVTS 531_ KGVIH 536_ LTKLR 541_ NLSSL 546_ DLRHI 551_ TELDN 556_ ETVME 561_ IVKRC 566_ KNLSS 571_ LNLCL 576_ NWIIN 581_ DRCVE 586_ VIAKE 591_ GQNLK 596_ ELYLV 601_ SCKIT 606_ DYALI 611_ AIGRY 616_ SMTIE 621_ TVDVG 626_ WCKEI 631_ TDQGA 636_ TLIAQ 641_ SSKSL 646_ RYLGL 651_ MRCDK 656_ VNEVT 661_ VEQLV 666_ QQYPH 671_ ITFST 676_ VLQDC 681_ KRTLE 686_ RAYQM 691_ GWTPN 696_MSAAS
1: Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteasome (PubMed:30190310). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (By similarity). The SCF(FBXL17) complex mediates ubiquitination and degradation of BACH1 (PubMed:24035498, PubMed:30190310). The SCF(FBXL17) complex is also involved in the regulation of the hedgehog/smoothened (Hh) signaling pathway by mediating the ubiquitination and degradation of SUFU, allowing the release of GLI1 from SUFU for proper Hh signal transduction (PubMed:27234298). The SCF(FBXL17) complex mediates ubiquitination and degradation of PRMT1 (By similarity)