ID A0A2Y9MQL6_DELLE Unreviewed; 485 AA.
AC A0A2Y9MQL6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Suppressor of fused homolog {ECO:0000256|PIRNR:PIRNR011844};
GN Name=SUFU {ECO:0000313|RefSeq:XP_022424624.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022424624.1};
RN [1] {ECO:0000313|RefSeq:XP_022424624.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022424624.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Negative regulator in the hedgehog signaling pathway. Down-
CC regulates GLI1-mediated transactivation of target genes. Part of a
CC corepressor complex that acts on DNA-bound GLI1. May also act by
CC linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the
CC proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this
CC effect is overcome by binding of STK36 to both SUFU and a GLI protein.
CC Negative regulator of beta-catenin signaling. Regulates the formation
CC of either the repressor form (GLI3R) or the activator form (GLI3A) of
CC the full-length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in
CC the cytoplasm and is maintained in a neutral state. Without the Hh
CC signal, the SUFU-GLI3 complex is recruited to cilia, leading to the
CC efficient processing of GLI3FL into GLI3R. When Hh signaling is
CC initiated, SUFU dissociates from GLI3FL and the latter translocates to
CC the nucleus, where it is phosphorylated, destabilized, and converted to
CC a transcriptional activator (GLI3A). {ECO:0000256|PIRNR:PIRNR011844}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR011844}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR011844}.
CC -!- SIMILARITY: Belongs to the SUFU family.
CC {ECO:0000256|PIRNR:PIRNR011844}.
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DR RefSeq; XP_022424624.1; XM_022568916.2.
DR AlphaFoldDB; A0A2Y9MQL6; -.
DR STRING; 9749.A0A2Y9MQL6; -.
DR Ensembl; ENSDLET00000014800; ENSDLEP00000013402; ENSDLEG00000009757.
DR InParanoid; A0A2Y9MQL6; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 3.30.1360.230; Sufu, C-terminal domain; 1.
DR InterPro; IPR020941; SUFU-like_domain.
DR InterPro; IPR024314; SUFU_C.
DR InterPro; IPR038489; SUFU_C_sf.
DR InterPro; IPR037181; SUFU_N.
DR InterPro; IPR007768; Suppressor_of_fused.
DR InterPro; IPR016591; Suppressor_of_fused_euk.
DR PANTHER; PTHR10928; SUPPRESSOR OF FUSED; 1.
DR PANTHER; PTHR10928:SF2; SUPPRESSOR OF FUSED HOMOLOG; 1.
DR Pfam; PF05076; SUFU; 1.
DR Pfam; PF12470; SUFU_C; 1.
DR PIRSF; PIRSF011844; Suppressor_of_fused_protein; 1.
DR SUPFAM; SSF103359; Suppressor of Fused, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR011844};
KW Developmental protein {ECO:0000256|PIRNR:PIRNR011844};
KW Nucleus {ECO:0000256|PIRNR:PIRNR011844};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 64..240
FT /note="Suppressor of fused-like"
FT /evidence="ECO:0000259|Pfam:PF05076"
FT DOMAIN 254..433
FT /note="Suppressor of fused C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12470"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 53736 MW; 5186C75A7A578909 CRC64;
MAELRPSGAP GPTAPPAPGP TAPPAFASLF PPGLHAIYGE CRRLYPDQPN PLQVTAIVKY
WLGGPDPLDY VSMYRNVGSP SANIPEHWHY ISFGLSDLYG DNRVHEFTGT DGPSGFGFEL
TFRLKRETGE SAPPTWPAEL MQGLARYVFQ SENTFCSGDH VSWHSPLDNS ESRIQHMLLT
EDPQMQPVQT PFGVVTFLQI VGVCTEELHA AQQWNGQGIL ELLRTVPIAG GPWLITDMRR
GETIFEIDPH LQQERVDKGI ETDGSNLSGV SAKCAWDDLS RPPEDDEDSR SICIGTQSRR
LSGKDTEQIR ETLRRGLEIN SKPVLPPINP QRQNGLTHDR APSRKDSLES DSSTAIIPHE
LIRTRQLESV HLKFNQESGA LIPLCLRGRL LHGRHFTYKS ITGDMAITFV STGVEGAFAT
EEHPYAAHGP WLQSQAAPRG PRELQEPEAP ELHRLFPQLH HNGESVPRES AQELLHHSCL
SPVSC
//
