ID   Q4V8C6_RAT              Unreviewed;       485 AA.
AC   Q4V8C6;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Suppressor of fused homolog {ECO:0000256|PIRNR:PIRNR011844};
GN   Name=Sufu {ECO:0000313|EMBL:AAH97447.1, ECO:0000313|RGD:1559462};
GN   ORFNames=rCG_57679 {ECO:0000313|EMBL:EDL94350.1};
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 {ECO:0000313|EMBL:AAH97447.1};
RN   [1] {ECO:0000313|EMBL:AAH97447.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000313|EMBL:AAH97447.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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] {ECO:0000313|EMBL:EDL94350.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDL94350.1};
RX   PubMed=15632090; DOI=10.1101/gr.2889405;
RA   Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA   Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA   Istrail S., Li P., Sutton G.;
RT   "Gene and alternative splicing annotation with AIR.";
RL   Genome Res. 15:54-66(2005).
RN   [3] {ECO:0000313|EMBL:EDL94350.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDL94350.1};
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA   Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA   Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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   EMBL; BC097447; AAH97447.1; -; mRNA.
DR   EMBL; CH473986; EDL94350.1; -; Genomic_DNA.
DR   RefSeq; NP_001020070.1; NM_001024899.1.
DR   AlphaFoldDB; Q4V8C6; -.
DR   SMR; Q4V8C6; -.
DR   STRING; 10116.ENSRNOP00000026987; -.
DR   PhosphoSitePlus; Q4V8C6; -.
DR   PaxDb; 10116-ENSRNOP00000026987; -.
DR   GeneID; 361769; -.
DR   KEGG; rno:361769; -.
DR   UCSC; RGD:1559462; rat.
DR   AGR; RGD:1559462; -.
DR   CTD; 51684; -.
DR   RGD; 1559462; Sufu.
DR   VEuPathDB; HostDB:ENSRNOG00000019807; -.
DR   eggNOG; ENOG502QT57; Eukaryota.
DR   HOGENOM; CLU_033906_0_0_1; -.
DR   OrthoDB; 5385318at2759; -.
DR   TreeFam; TF324548; -.
DR   Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-RNO-5610787; Hedgehog 'off' state.
DR   Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR   Proteomes; UP000234681; Chromosome 1.
DR   Bgee; ENSRNOG00000019807; Expressed in testis and 18 other cell types or tissues.
DR   GO; GO:0005929; C:cilium; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:1990788; C:GLI-SUFU complex; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0035904; P:aorta development; ISO:RGD.
DR   GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR   GO; GO:0001947; P:heart looping; ISO:RGD.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR   GO; GO:2001040; P:positive regulation of cellular response to drug; IEP:RGD.
DR   GO; GO:0043588; P:skin development; ISO:RGD.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; ISO:RGD.
DR   GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; ISO:RGD.
DR   GO; GO:0007286; P:spermatid development; IEP:RGD.
DR   GO; GO:0021513; P:spinal cord dorsal/ventral patterning; ISO:RGD.
DR   GO; GO:0003281; P:ventricular septum development; ISO:RGD.
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   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR011844};
KW   Developmental protein {ECO:0000256|PIRNR:PIRNR011844};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR011844}.
FT   DOMAIN          64..240
FT                   /note="Suppressor of fused-like"
FT                   /evidence="ECO:0000259|Pfam:PF05076"
FT   DOMAIN          254..474
FT                   /note="Suppressor of fused C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12470"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  54081 MW;  E4E70580C797155D CRC64;
     MAELRPSVAP GPAAPPASGP SAPPAFASLF PPGLHAIYGE CRRLYPDQPN PLQVTAIVKY
     WLGGPDPLDY VSMYRNMGSP SANIPEHWHY ISFGLSDLYG DNRVHEFTGT DGPSGFGFEL
     TFRLKRETGE SAPPTWPAEL MQGLARYVFQ SENTFCSGDH VSWHSPLDNS ESRIQHMLLT
     EDPQMQPVQT PFGVVTFLQI VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR
     GETIFEIDPH LQQERVDKGI ETDGSNLSGV SAKCAWDDLS RPPEDDEDSR SICLGTQPRR
     LSGKDTEQIR ETLRRGLEIN SKPVLPPINS QRQNGLTYDR APSRKDSLGS DISTAVIPHE
     LIRTRQLESV HLKFNQESGA LIPLCLRGRL LHGRHFTYKS ITGDMAITFV STGVEGAFAT
     EEHPYAAHGP WLQILLTEEF VEKMLEDLED LTSPEEFKLP KEYSWPEKKL KVSILPDVVF
     DSPLH
//