ZFHX3_MOUSE
ID ZFHX3_MOUSE Reviewed; 3726 AA.
AC Q61329;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 174.
DE RecName: Full=Zinc finger homeobox protein 3;
DE AltName: Full=AT motif-binding factor 1;
DE AltName: Full=AT-binding transcription factor 1;
DE AltName: Full=Alpha-fetoprotein enhancer-binding protein;
DE AltName: Full=Zinc finger homeodomain protein 3;
DE Short=ZFH-3;
GN Name=Zfhx3; Synonyms=Atbf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/MK X ICR; TISSUE=Brain;
RX PubMed=8654949; DOI=10.1016/0378-1119(95)00740-7;
RA Ido A., Miura Y., Watanabe M., Sakai M., Inoue Y., Miki T., Hashimoto T.,
RA Morinaga T., Nishi S., Tamaoki T.;
RT "Cloning of the cDNA encoding the mouse ATBF1 transcription factor.";
RL Gene 168:227-231(1996).
RN [2]
RP INTERACTION WITH FNBP3.
RX PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA Bedford M.T., Chan D.C., Leder P.;
RT "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-
RT rich ligands.";
RL EMBO J. 16:2376-2383(1997).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11312261; DOI=10.1074/jbc.m010378200;
RA Berry F.B., Miura Y., Mihara K., Kaspar P., Sakata N.,
RA Hashimoto-Tamaoki T., Tamaoki T.;
RT "Positive and negative regulation of myogenic differentiation of C2C12
RT cells by isoforms of the multiple homeodomain zinc finger transcription
RT factor ATBF1.";
RL J. Biol. Chem. 276:25057-25065(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2904, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP PHOSPHORYLATION AT SER-1600; SER-2634; SER-2795; SER-2804; SER-2900;
RP SER-3434; SER-3443; SER-3616 AND SER-3700, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
RX PubMed=23022192; DOI=10.1016/j.bbrc.2012.09.092;
RA Zhang S., Kim T.S., Dong Y., Kanazawa S., Kawaguchi M., Gao N., Minato H.,
RA Takegami T., Nojima T., Asai K., Miura Y.;
RT "AT motif binding factor 1 (ATBF1) is highly phosphorylated in embryonic
RT brain and protected from cleavage by calpain-1.";
RL Biochem. Biophys. Res. Commun. 427:537-541(2012).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF VAL-1963.
RX PubMed=26232227; DOI=10.1016/j.cell.2015.06.060;
RA Parsons M.J., Brancaccio M., Sethi S., Maywood E.S., Satija R.,
RA Edwards J.K., Jagannath A., Couch Y., Finelli M.J., Smyllie N.J., Esapa C.,
RA Butler R., Barnard A.R., Chesham J.E., Saito S., Joynson G., Wells S.,
RA Foster R.G., Oliver P.L., Simon M.M., Mallon A.M., Hastings M.H.,
RA Nolan P.M.;
RT "The regulatory factor ZFHX3 modifies circadian function in SCN via an AT
RT motif-driven axis.";
RL Cell 162:607-621(2015).
CC -!- FUNCTION: Transcriptional regulator which can act as an activator or a
CC repressor. Inhibits the enhancer element of the AFP gene by binding to
CC its AT-rich core sequence. In concert with SMAD-dependent TGF-beta
CC signaling can repress the transcription of AFP via its interaction with
CC SMAD2/3 (By similarity). Regulates the circadian locomotor rhythms via
CC transcriptional activation of neuropeptidergic genes which are
CC essential for intercellular synchrony and rhythm amplitude in the
CC suprachiasmatic nucleus (SCN) of the brain (PubMed:26232227). Regulator
CC of myoblasts differentiation through the binding to the AT-rich
CC sequence of MYF6 promoter and promoter repression. Down-regulates the
CC MUC5AC promoter in gastric cancer. In association with RUNX3, up-
CC regulates CDKN1A promoter activity following TGF-beta stimulation (By
CC similarity). {ECO:0000250|UniProtKB:Q15911,
CC ECO:0000269|PubMed:26232227}.
CC -!- SUBUNIT: Interacts with ALKBH4 and PIAS3 (By similarity). Interacts
CC with FNBP3. Interacts with ESR1, RUNX3, TRIM25, SMAD2 and SMAD3 (By
CC similarity). {ECO:0000250|UniProtKB:Q15911,
CC ECO:0000269|PubMed:9171351}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15911}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q15911}. Note=Translocates from the cytoplasm to
CC the nucleus following TGF-beta stimulation. Expressed in nuclear body
CC (NB)-like dots in the nucleus some of which overlap or closely
CC associate with PML body. {ECO:0000250|UniProtKB:Q15911}.
CC -!- TISSUE SPECIFICITY: Expressed in suprachiasmatic nucleus (SCN) of the
CC brain (at protein level). Expressed in skeletal muscle. Levels of
CC expression are high in myoblasts but low in differentiated muscle.
CC {ECO:0000269|PubMed:11312261, ECO:0000269|PubMed:26232227}.
CC -!- PTM: Phosphorylated at Ser-2634 in embryonic and adult brain.
CC Phosphorylated at Ser-1600, Ser-2795, Ser-2804, Ser-2900, Ser-3434,
CC Ser-3443, Ser-3616 and Ser-3700 in the embryonic brain only.
CC Hpyerphosphorylated in embryonic brain and phosphorylation decreases
CC its sensitivity to calpain-mediated proteolysis.
CC {ECO:0000269|PubMed:23022192}.
CC -!- PTM: Adult brain-derived ZFHX3 is sensitive, but embryonic brain-
CC derived ZFHX3 is resistant to calpain 1-mediated proteolysis.
CC {ECO:0000269|PubMed:23022192}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q15911}.
CC -!- PTM: Nuclear localization is essential for its sumoylation.
CC {ECO:0000250|UniProtKB:Q15911}.
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DR EMBL; D26046; BAA05046.1; -; mRNA.
DR SMR; Q61329; -.
DR IntAct; Q61329; 4.
DR MINT; Q61329; -.
DR STRING; 10090.ENSMUSP00000044612; -.
DR iPTMnet; Q61329; -.
DR PhosphoSitePlus; Q61329; -.
DR MaxQB; Q61329; -.
DR PaxDb; Q61329; -.
DR PeptideAtlas; Q61329; -.
DR PRIDE; Q61329; -.
DR ProteomicsDB; 275348; -.
DR MGI; MGI:99948; Zfhx3.
DR eggNOG; KOG1146; Eukaryota.
DR InParanoid; Q61329; -.
DR PhylomeDB; Q61329; -.
DR Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription.
DR ChiTaRS; Zfhx3; mouse.
DR PRO; PR:Q61329; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61329; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:ARUK-UCL.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IMP:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0071559; P:response to transforming growth factor beta; ISS:UniProtKB.
DR CDD; cd00086; homeodomain; 4.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00046; Homeodomain; 4.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 23.
DR SMART; SM00451; ZnF_U1; 7.
DR SUPFAM; SSF46689; SSF46689; 4.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00027; HOMEOBOX_1; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Myogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..3726
FT /note="Zinc finger homeobox protein 3"
FT /id="PRO_0000046931"
FT ZN_FING 79..103
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..305
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 641..664
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 672..695
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 727..751
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 805..829
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 946..969
FT /note="C2H2-type 7; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 985..1009
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1041..1065
FT /note="C2H2-type 9; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1089..1113
FT /note="C2H2-type 10; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1233..1256
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1262..1285
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1370..1395
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1411..1433
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1439..1462
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1555..1579
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1606..1630
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1990..2013
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2152..2211
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 2249..2308
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2335..2358
FT /note="C2H2-type 19; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2539..2561
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2650..2709
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2720..2743
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2952..3011
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 3032..3056
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 3552..3576
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2037..2089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2211..2249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2383..2405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2429..2529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2628..2656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2780..2805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2850..2877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2920..2955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3145..3274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3415..3476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3588..3726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2624..2626
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT COMPBIAS 21..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..493
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1882..1904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2040..2084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2444..2479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2480..2506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2507..2529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2780..2794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2920..2940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3145..3195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3196..3226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3235..3263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3415..3431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3438..3452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3602..3619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3654..3682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 2634
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 2795
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 2804
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 2900
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 2904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3434
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 3443
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 3457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT MOD_RES 3616
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT MOD_RES 3700
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23022192"
FT CROSSLNK 2356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT CROSSLNK 2815
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT CROSSLNK 2815
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT CROSSLNK 3262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q15911"
FT MUTAGEN 1963
FT /note="V->F: In short circuit/sci mutant; shorter circadian
FT period, homozygous lethality during embryonic development
FT and diminished ability to activate the transcription of
FT circadian-related neuropeptides."
FT /evidence="ECO:0000269|PubMed:26232227"
SQ SEQUENCE 3726 AA; 406570 MW; 915ACBE588A72C98 CRC64;
MEGCDSPVVS GKDNGCGIPQ HRQWTELNSA HLPDKPSSME QPTGESHGPL DSLRAPFNER
LADSSTSAGP PAEPASKEVS CNECSASFSS LQTYMEHHCP GTHPPPALRE ESASDTSEEG
EEESDVENLA GEIVYQPDGS AYIVESLSQL AQSGAACGSS SGSGAVPSLF LNSLPGVGGK
QGDPSCAAPV YPQIINTSHI ASSFGKWFEG SDPAFPNTSA LAGLSPVLHS FRVFDVRHKS
NKDYLNSDGS AKSSCVSKDV PNNVDLSKFD GFVLYGKRKP ILMCFLCKLS FGYVRSFVTH
AVHDHRMTLS EEERKLLSNK NISAIIQGIG KDKEPLVSFL EPKNKNFQHP LVSTGNLIGP
GHSFYGKFSG IRMEGEEALP AVAAAGPEQP QAGLLTPSTL LNLGGLTSSV LKTPITSVPL
GPLASSPTKS SEGKDSGAAE GDKQESGGHQ DCFSEKVEPA EEEEAEEEEE EEEEAEEEEE
EEEEEEEEEE EASKGLFPND LEEELEDSPS EESGPPAGGT TKKDLALSNP SISNSPLMPN
VLQTLSRGPA STTSNSASNF VVFDGANRRS RLSFNSEGVR ANVAEGRRLD FADESANKDS
ATAPEPNEST EGDDGGFVPH HQHAGSLCEL GVGESPSGSG VECPKCDTVL GSSRSLGGHM
TMMHSRNSCK TLKCPKCNWH YKYQQTLEAH MKEKHPEPGG SCVYCKSGQP HPRLARGESY
TCGYKPFRCE VCNYSTTTKG NLSIHMQSDK HLNNMQNLQN GGGEQVFSHS AGAAAAAAAA
AAAAANIGSS WGAPSPTKPK TKPTWRCEVC DYETNVARNL RIHMTSEKHM HNMMLLQQNM
TQIQHNRHLG LGSLPSPAEA ELYQYYLAQN MNLPNLKMDS TASDAQFMMS GFQLDPTGPM
AAMTPALVGG EIPLDMRLGG GQLVSEELMN LGESFIQTND PSLKLFQCAV CNKFTTDNLD
MLGLHMNVER SLSEDEWKAV MGDSYQCKLC RYNTQLKANF QLHCKTDKHV QKYQLVAHIK
EGGKANEWRL KCVAIGNPVH LKCNACDYYT NSLEKLRLHT VNSRHEASLK LYKHLQQHES
GVEGESCYYH CVLCNYSTKA KLNLIQHVRS MKHQRSESLR KLQRLQKGLP EEDEDLGQIF
TIRRCPSTDP EEPVEDAEGP SEASADPEEL AKDQGSGSEE GQSKRAASSS QAEKELTDSP
ATTKRTSFPG SSETPLSSKR PKASEEIKPE QMYQCPYCKY SNADVNRLRV HAMTQHSVQP
LLRCPLCQDM LNNKIHLQLH LTHLHSVAPD CVEKLIMTVT APEMVMPSSM FLPAAAADRD
GNSTLEEVGK QPEASEDPGK NILPPASMEH GGDLKPTSAD PSCGREDSGF LCWKKGCNQV
FKTSATLQTH FNEVHAKRPQ LPVSDRHVYK YRCNQCSLAF KTIEKLQLHS QYHVIRAATM
CCLCQRSFRT FQALKKHLET SHLELSEADI QQLYGGLLAN GDLLAMGDPT LAEDHTIIVE
EDKEEESDLE DKQSPTGSDS GSVQEDSGSE PKRALPFRKG PNFTMEKFLD PSRPYKCTVC
KESFTQKNIL LVHYNSVSHL HKLKRALQES ATGQPEPTSS PDNKPFKCNT CNVAYSQSST
LEIHMRSVLH QTKARAAKLE AASGNSNGTG NSGGVSLSSS TPSPVGSSGA NNTFTATNPS
SAAMAPSVNA LSQVPPESVV MPPLGNPISA NIASPSEPKE ANRKKLADMI ASRQQQQQQQ
QQQQQQAQTL AQAQAQVQAH LQQELQQQAA LIQSQLFNPT LLPHFPMTTE TLLQLQQQQH
LLFPFYIPSA EFQLNPEVSL PVTSGALTLT GSGPGLLEDL KVQVQIPQQS HQQILQQQQQ
QSQLSLSQSH SALLQPSQHP EKKNKVVIKE KDKESQRERE GPEGAEGNTG PQESLPDASK
AKEKKDLAPG GGSEGTMLPP RIASDARGNA TKALLENFGF ELVIQYNENK QKAQKKNGKA
EQGGESLEKL ECDSCGKLFS NILILKSHQE HVHQNYFPFK QLERFAKQYR EHYDKLYPLR
PQTPEPPPPP PPPPPPPLPT APPQPASAPA IPASAPPITS PTIAPAQPSV PLTQLSMPME
LPIFSPLMMQ TMPLQTLPAQ LPPQLGPVEP LPADLAQLYQ HQLNPTLLQQ QNKRPRTRIT
DDQLRVLRQY FDINNSPSEE QIKEMADKSG LPQKVIKHWF RNTLFKERQR NKDSPYNFSN
PPITSLEELK IDSRPPSPEP QKQEYWGSKR SSRTRFTDYQ LRVLQDFFDA NAYPKDDEFE
QLSNLLNLPT RVIVVWFQNA RQKARKNYEN QGEGKDGERR ELTNDRYIRT SNLNYQCKKC
SLVFQRIFDL IKHQKKLCYK DEDEEGQDDS QNEDSMDAME ILTPTSSSCS TPMPSQAYST
PAPSAAAANT APSAFLQLTA ETDELATFNS KAEASDEKPK QADPPSAQPN QTQEKQGQPK
PEMQQQLEQL EQKTNAPQPK LPQPAAPSLP QPPPQAPPPQ CPLPQSSPSP SQLSHLPLKP
LHTSTPQQLA NLPPQLIPYQ CDQCKLAFPS FEHWQEHQQL HFLSAQNQFI HPQFLDRSLD
MPFMLFDPSN PLLASQLLSG AIPQIPASSA TSPSTPTSTM NTLKRKLEEK ASASPGENDS
GTGGEEPQRD KRLRTTITPE QLEILYQKYL LDSNPTRKML DHIAHEVGLK KRVVQVWFQN
TRARERKGQF RAVGPAQAHR RCPFCRALFK AKTALEAHIR SRHWHEAKRA GYNLTLSAML
LDCDGGLQMK GDIFDGTSFS HLPPSSSDGQ GVPLSPVSKT MELSPRTLLS PSSIKVEGIE
DFESPSMSSV NLNFDQTKLD NDDCSSVNTA ITDTTTGDEG NADNDSATGI ATETKSSAPN
EGLTKAAMMA MSEYEDRLSS GLVSPAPSFY SKEYDNEGTV DYSETSSLAD PCSPSPGASG
SAGKSGDGGD RPGQKRFRTQ MTNLQLKVLK SCFNDYRTPT MLECEVLGND IGLPKRVVQV
WFQNARAKEK KSKLSMAKHF GINQTSYEGP KTECTLCGIK YSARLSVRDH IFSQQHISKV
KDTIGSQLDK EKEYFDPATV RQLMAQQELD RIKKANEVLG LAAQQQGMFD NAPLQALNLP
TTYPALQGIP PVLLPGLNRP SLPGFTPANT ALTSPKPNLM GLPSTTVPSP GLPTSGLPNK
PSSASLSSPT PAQATMAMAP QPPPQPQQPQ PPVQQPPPPP AAQQIPAPQL TPQQQRKDKD
GEKGKEKEKA HKGKGEPLPV PKKEKGEAPP AGTGTISAPL PAMEYAVDPA QLQALQAALT
SDPTALLTSQ FLPYFVPGFS PYYAPQIPGA LQSGYLQPMY GMEGLFPYSP ALSRPLMGLS
PGSLLQQYQQ YQQSLQEAIQ QQQQQQQQQQ QQQQQQQRQL QQQQQQQQQK VQQQQQQQQQ
PKASQTPVPQ GAASPDKDPA KESPKPEEQK NVPRELSPLL PKPPEEPEAE SKSASADSLC
DPFIVPKVQY KLVCRKCQAG FGDEEAARSH LKSLCCFGQS VVNLQEMVLH VPTGSGGGGG
GGGGSGGGGG SYHCLACESA LCGEEALSQH LESALHKHRT ITRAARNAKE HPSLLPHSAC
FPDPSTASTS QSAAHSNDSP PPPSAAPSSS ASPHASRKSW PPVGSRASAA KPPSFPPLSS
SSTVTSSSCS TSGVQPSMPT DDYSEESDTD LSQKSDGPAS PVEGPKDPSC PKDSGLTSVG
TDTFRL
