ID A0A2U9CP78_SCOMX Unreviewed; 671 AA.
AC A0A2U9CP78;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Putative retinoic acid receptor alpha-B-like {ECO:0000313|EMBL:AWP18388.1};
GN ORFNames=SMAX5B_005732 {ECO:0000313|EMBL:AWP18388.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP18388.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP18388.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Heterodimer; with an rxr molecule. Binds DNA preferentially as
CC a rar/rxr heterodimer. {ECO:0000256|ARBA:ARBA00011431}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU004334}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000256|ARBA:ARBA00008092}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; CP026261; AWP18388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CP78; -.
DR STRING; 52904.ENSSMAP00000027997; -.
DR Proteomes; UP000246464; Chromosome 19.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:InterPro.
DR CDD; cd06964; NR_DBD_RAR; 1.
DR CDD; cd06937; NR_LBD_RAR; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR047159; NR_DBD_RAR.
DR InterPro; IPR047158; NR_LBD_RAR.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003078; Retinoic_acid_rcpt.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR24085; NUCLEAR HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24085:SF8; RETINOIC ACID RECEPTOR ALPHA; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF00530; SRCR; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01292; RETNOICACIDR.
DR PRINTS; PR00258; SPERACTRCPTR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00202; SR; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004334};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004334};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU004334}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT TRANSMEM 609..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..132
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 155..389
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT DOMAIN 393..493
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 499..590
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DISULFID 462..472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 671 AA; 74095 MW; AA13B6AB376BF49C CRC64;
MEASAATGMR AQLRHSVGSL ARAGCRLSVT IETESTSSGE DLLVPSPPSP PPPPRIYKPC
FVCQDKSSGY HYGVSACEGC KGFFRRSIQK NMVYNCHRDK VCVINKVTRN RCQSCRLQKC
LDVGMSKELV RNDRTKKKKE EKRPGEAEIY VLSADTEQMI ERVRRAHQGT FPSLCQLGKY
TTGNSSEQRV ALDVSLWDKF SELSTKCIIK TVEFAKQMPG FTTLTIADQI TLLKAACLDI
LILRICTRYT PDQDTMTFSD GLTLNRTQMH NAGFGPLTDL VFTFANQLLP LEMDDAETGL
LSAICLLCGD RQDLEEPEKV DVLQEPMLEA LKIYVRRRRP EKPCMFPKIL MKITDLRSIS
VKGAERVITL KMEIPGSMPP LIQEMLENSE GGIRLAEGGV TRCSGRVEIY HKYAWTTVCG
DSWHLNDAMV VCRQLDCGTA VSTTRSAHFG WGPGPIWLNV ACSGYEGVIK DCRHGRFEEH
ACPHREDASV ICSVPLQQPN ISLTSPDGAG LLWSAEAAVV TRGHGFVITC SISKHYPGGV
FSLIFSGSNI TDTEPAVDHS ATFEFPVAGY QHQGNYSCVY KVTLSSRTFT SIETTSISVI
IKSPLLRPLL SSLAPGGLVL LLWVLALICL VHKRRRQAMS PAVAHFAQCP CSPGQHCTLH
ETAACLFQDT L
//
