FOSL2_RAT
ID FOSL2_RAT Reviewed; 326 AA.
AC P51145; Q6GXE4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Fos-related antigen 2;
DE Short=FRA-2;
GN Name=Fosl2; Synonyms=Fra-2, Fra2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Pineal gland;
RX PubMed=7592994; DOI=10.1074/jbc.270.45.27319;
RA Baler R.D., Klein D.C.;
RT "Circadian expression of transcription factor Fra-2 in the rat pineal
RT gland.";
RL J. Biol. Chem. 270:27319-27325(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Osteoblast;
RX PubMed=15299028; DOI=10.1074/jbc.m405549200;
RA Chang W., Rewari A., Centrella M., McCarthy T.L.;
RT "Fos-related antigen 2 controls protein kinase A-induced CCAAT/enhancer-
RT binding protein beta expression in osteoblasts.";
RL J. Biol. Chem. 279:42438-42444(2004).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19103603; DOI=10.1074/jbc.m808394200;
RA Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q.,
RA Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F.,
RA Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C.;
RT "Night/day changes in pineal expression of >600 genes: central role of
RT adrenergic/cAMP signaling.";
RL J. Biol. Chem. 284:7606-7622(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Controls osteoclast survival and size (By similarity). As a
CC dimer with JUN, activates LIF transcription (By similarity). Activates
CC CEBPB transcription in PGE2-activated osteoblasts (PubMed:15299028).
CC {ECO:0000250|UniProtKB:P47930, ECO:0000269|PubMed:15299028}.
CC -!- SUBUNIT: Heterodimer (By similarity). Interacts with the BAF
CC multiprotein chromatin-remodeling complex subunits SMARCB1 and SMARCD1
CC (By similarity). Interacts with ARID1A and JUN (By similarity).
CC {ECO:0000250|UniProtKB:P47930}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:15299028}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain cortex. Expressed at night
CC in pineal gland (at protein level). Also expressed in osteoblasts (at
CC protein level). {ECO:0000269|PubMed:15299028,
CC ECO:0000269|PubMed:19103603, ECO:0000269|PubMed:7592994}.
CC -!- INDUCTION: In the pineal gland, exhibits night/day variations with a 4-
CC fold increased expression at night (at protein level). Up-regulation is
CC due to a large degree to the release of norepinephrine from nerve
CC terminals in the pineal gland and cAMP signaling pathway. Nocturnally
CC elevated expression is also observed in the brain cortex. In
CC osteoblasts, up-regulated by PGE2 (at protein level).
CC {ECO:0000269|PubMed:15299028, ECO:0000269|PubMed:19103603,
CC ECO:0000269|PubMed:7592994}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; U18913; AAC52310.1; -; mRNA.
DR EMBL; AY622611; AAT52165.1; -; mRNA.
DR PIR; I55459; I55459.
DR RefSeq; NP_037086.1; NM_012954.1.
DR AlphaFoldDB; P51145; -.
DR SMR; P51145; -.
DR STRING; 10116.ENSRNOP00000064213; -.
DR iPTMnet; P51145; -.
DR PhosphoSitePlus; P51145; -.
DR PaxDb; P51145; -.
DR GeneID; 25446; -.
DR KEGG; rno:25446; -.
DR CTD; 2355; -.
DR RGD; 2628; Fosl2.
DR eggNOG; KOG1414; Eukaryota.
DR InParanoid; P51145; -.
DR OrthoDB; 1221590at2759; -.
DR PRO; PR:P51145; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0001661; P:conditioned taste aversion; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0003334; P:keratinocyte development; ISO:RGD.
DR GO; GO:0009648; P:photoperiodism; IEP:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IMP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IMP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0030431; P:sleep; IEP:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029814; Fra2.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF25; PTHR23351:SF25; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..326
FT /note="Fos-related antigen 2"
FT /id="PRO_0000076485"
FT DOMAIN 124..187
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..128
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 129..136
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 193..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P47930"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CONFLICT 56
FT /note="T -> TT (in Ref. 1; AAC52310)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="A -> R (in Ref. 1; AAC52310)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="A -> T (in Ref. 1; AAC52310)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="P -> S (in Ref. 1; AAC52310)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="L -> V (in Ref. 1; AAC52310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 35255 MW; 07DD44D47D0B790A CRC64;
MYQDYPGNFD TSSRGSSGSP AHAESYSSGG GGQQKFRVDM PGSGSAFIPT INAITTSQDL
QWMVQPTVIT SMSNPYPRSH PYSPLPGLAS VPGHMALPRP GVIKTIGTTV GRRRRDEQLS
PEEEEKRRIR RERNKLAAAK CRNRRRELTE KLQAETEELE EEKSGLQKEI AELQKEKEKL
EFMLVAHGPV CKISPEERRS PPTSGLQSLR GTGSAVGPVV VKQEPPEEDS PSSSAGMDKT
QRSVIKPISI AGGGFYGEEP LHTPIVVTST PAITPGTSNL VFTYPSVLEQ ESPASPSESC
SKAHRRSSSS GDQSSDSLNS PTLLAL
