FTF1B_DROME
ID FTF1B_DROME Reviewed; 808 AA.
AC Q05192; A4V0Z2; Q0E8N5; Q8INT8; Q9VID8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Nuclear hormone receptor FTZ-F1 beta;
DE AltName: Full=Nuclear hormone receptor HR39;
DE Short=dHR39;
DE AltName: Full=Nuclear receptor subfamily 5 group B member 1;
GN Name=Hr39; Synonyms=FTZ-F1-beta, FTZF1-beta, NR5-beta-1, NR5B1;
GN ORFNames=CG8676;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=8382937; DOI=10.1016/0925-4773(93)90084-b;
RA Ohno C.K., Petkovich M.;
RT "FTZ-F1 beta, a novel member of the Drosophila nuclear receptor family.";
RL Mech. Dev. 40:13-24(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8479913; DOI=10.1093/nar/21.7.1619;
RA Ayer S., Walker N., Mosammaparast M., Nelson J.P., Shilo B.-Z.,
RA Benyajati C.;
RT "Activation and repression of Drosophila alcohol dehydrogenase distal
RT transcription by two steroid hormone receptor superfamily members binding
RT to a common response element.";
RL Nucleic Acids Res. 21:1619-1627(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8164672; DOI=10.1128/mcb.14.5.3166-3175.1994;
RA Ohno C.K., Ueda H., Petkovich M.;
RT "The Drosophila nuclear receptors FTZ-F1 alpha and FTZ-F1 beta compete as
RT monomers for binding to a site in the fushi tarazu gene.";
RL Mol. Cell. Biol. 14:3166-3175(1994).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-98; SER-100; SER-106;
RP SER-127 AND SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Acts as a cofactor to fushi tarazu (ftz). Facilitates the
CC binding of ftz to DNA. Binds the sequence element 5'-YCYYGGYCR-3' in
CC the zebra element of ftz. Probably also functions as a receptor for a
CC yet unknown ligand. {ECO:0000269|PubMed:8164672,
CC ECO:0000269|PubMed:8382937, ECO:0000269|PubMed:8479913}.
CC -!- SUBUNIT: Monomer; forms a complex with ftz. {ECO:0000250}.
CC -!- INTERACTION:
CC Q05192; Q86BY9: rig; NbExp=2; IntAct=EBI-75048, EBI-422757;
CC Q05192; O96757: stumps; NbExp=3; IntAct=EBI-75048, EBI-74922;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=B;
CC IsoId=Q05192-1; Sequence=Displayed;
CC Name=C; Synonyms=DHR39-short;
CC IsoId=Q05192-2; Sequence=VSP_003718, VSP_003719;
CC -!- TISSUE SPECIFICITY: Expressed throughout the blastodermal layer in
CC early embryos. At later stages, strong expression is observed in the
CC brain, ventral cord and hindgut. {ECO:0000269|PubMed:8382937,
CC ECO:0000269|PubMed:8479913}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages.
CC {ECO:0000269|PubMed:8382937, ECO:0000269|PubMed:8479913}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR5
CC subfamily. {ECO:0000305}.
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DR EMBL; L06423; AAA28543.1; -; mRNA.
DR EMBL; L07551; AAA28464.1; -; mRNA.
DR EMBL; L07549; AAA28462.1; -; mRNA.
DR EMBL; L07550; AAA28463.1; -; mRNA.
DR EMBL; AE014134; AAN11107.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11108.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11109.1; -; Genomic_DNA.
DR EMBL; AY069676; AAL39821.1; -; mRNA.
DR PIR; S33708; S33708.
DR PIR; S33709; S33709.
DR RefSeq; NP_476932.1; NM_057584.5. [Q05192-1]
DR RefSeq; NP_476933.1; NM_057585.3. [Q05192-2]
DR RefSeq; NP_599123.1; NM_134296.3. [Q05192-1]
DR RefSeq; NP_724322.1; NM_165364.2. [Q05192-1]
DR AlphaFoldDB; Q05192; -.
DR SMR; Q05192; -.
DR BioGRID; 61349; 21.
DR IntAct; Q05192; 17.
DR STRING; 7227.FBpp0081008; -.
DR iPTMnet; Q05192; -.
DR PaxDb; Q05192; -.
DR DNASU; 35398; -.
DR EnsemblMetazoa; FBtr0081478; FBpp0081007; FBgn0261239. [Q05192-2]
DR EnsemblMetazoa; FBtr0081479; FBpp0081008; FBgn0261239. [Q05192-1]
DR EnsemblMetazoa; FBtr0081480; FBpp0081009; FBgn0261239. [Q05192-1]
DR EnsemblMetazoa; FBtr0081481; FBpp0081010; FBgn0261239. [Q05192-1]
DR GeneID; 35398; -.
DR KEGG; dme:Dmel_CG8676; -.
DR UCSC; CG8676-RD; d. melanogaster.
DR CTD; 35398; -.
DR FlyBase; FBgn0261239; Hr39.
DR VEuPathDB; VectorBase:FBgn0261239; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000153391; -.
DR HOGENOM; CLU_015032_0_0_1; -.
DR InParanoid; Q05192; -.
DR OMA; HSVLYPP; -.
DR PhylomeDB; Q05192; -.
DR Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-DME-4090294; SUMOylation of intracellular receptors.
DR SignaLink; Q05192; -.
DR BioGRID-ORCS; 35398; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Hr39; fly.
DR GenomeRNAi; 35398; -.
DR PRO; PR:Q05192; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261239; Expressed in saliva-secreting gland and 45 other tissues.
DR Genevisible; Q05192; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0035211; P:spermathecum morphogenesis; IMP:FlyBase.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR016355; NR5_fam.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR24086; PTHR24086; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..808
FT /note="Nuclear hormone receptor FTZ-F1 beta"
FT /id="PRO_0000053740"
FT DOMAIN 580..808
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 373..448
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 376..396
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 412..436
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 696..701
FT /note="TCIERM -> VSLCEL (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8479913"
FT /id="VSP_003718"
FT VAR_SEQ 702..808
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8479913"
FT /id="VSP_003719"
FT CONFLICT 185
FT /note="E -> G (in Ref. 1; AAA28543 and 2; AAA28462/
FT AAA28463/AAA28464)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="V -> L (in Ref. 1; AAA28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="G -> F (in Ref. 2; AAA28462/AAA28463/AAA28464)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="P -> Q (in Ref. 2; AAA28462/AAA28464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 87314 MW; 02390BC2D4B35A48 CRC64;
MPNMSSIKAE QQSGPLGGSS GYQVPVNMCT TTVANTTTTL GSSAGGATGS RHNVSVTNIK
CELDELPSPN GNMVPVIANY VHGSLRIPLS GHSNHRESDS EEELASIENL KVRRRTAADK
NGPRPMSWEG ELSDTEVNGG EELMEMEPTI KSEVVPAVAP PQPVCALQPI KTELENIAGE
MQIQEKCYPQ SNTQHHAATK LKVAPTQSDP INLKFEPPLG DNSPLLAARS KSSSGGHLPL
PTNPSPDSAI HSVYTHSSPS QSPLTSRHAP YTPSLSRNNS DASHSSCYSY SSEFSPTHSP
IQARHAPPAG TLYGNHHGIY RQMKVEASST VPSSGQEAQN LSMDSASSNL DTVGLGSSHP
ASPAGISRQQ LINSPCPICG DKISGFHYGI FSCESCKGFF KRTVQNRKNY VCVRGGPCQV
SISTRKKCPA CRFEKCLQKG MKLEAIREDR TRGGRSTYQC SYTLPNSMLS PLLSPDQAAA
AAAAAAVASQ QQPHQRLHQL NGFGGVPIPC STSLPASPSL AGTSVKSEEM AETGKQSLRT
GSVPPLLQEI MDVEHLWQYT DAELARINQP LSAFASGSSS SSSSSGTSSG AHAQLTNPLL
ASAGLSSNGE NANPDLIAHL CNVADHRLYK IVKWCKSLPL FKNISIDDQI CLLINSWCEL
LLFSCCFRSI DTPGEIKMSQ GRKITLSQAK SNGLQTCIER MLNLTDHLRR LRVDRYEYVA
MKVIVLLQSD TTELQEAVKV RECQEKALQS LQAYTLAHYP DTPSKFGELL LRIPDLQRTC
QLGKEMLTIK TRDGADFNLL MELLRGEH
