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Database: UniProt
Entry: A0A3Q3AZK6_KRYMA
LinkDB: A0A3Q3AZK6_KRYMA
Original site: A0A3Q3AZK6_KRYMA 
ID   A0A3Q3AZK6_KRYMA        Unreviewed;       425 AA.
AC   A0A3Q3AZK6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Retinoic acid receptor RXR {ECO:0000256|RuleBase:RU369010};
DE   AltName: Full=Nuclear receptor subfamily 2 group B member {ECO:0000256|RuleBase:RU369010};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000022030.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000022030.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC       factor. Forms homo- or heterodimers with retinoic acid receptors (rars)
CC       and binds to target response elements in response to their ligands,
CC       all-trans or 9-cis retinoic acid, to regulate gene expression in
CC       various biological processes. {ECO:0000256|RuleBase:RU369010}.
CC   -!- SUBUNIT: Homodimer. Heterodimer; with a rar molecule.
CC       {ECO:0000256|RuleBase:RU369010}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU004334}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC       {ECO:0000256|RuleBase:RU369010}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC       subfamily. {ECO:0000256|ARBA:ARBA00006421}.
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DR   RefSeq; XP_017282010.1; XM_017426521.1.
DR   RefSeq; XP_017282011.1; XM_017426522.1.
DR   RefSeq; XP_017282012.1; XM_017426523.1.
DR   RefSeq; XP_017282013.1; XM_017426524.1.
DR   AlphaFoldDB; A0A3Q3AZK6; -.
DR   Ensembl; ENSKMAT00000022315.1; ENSKMAP00000022030.1; ENSKMAG00000016360.1.
DR   GeneID; 108241994; -.
DR   KEGG; kmr:108241994; -.
DR   CTD; 30486; -.
DR   GeneTree; ENSGT00940000159208; -.
DR   OMA; VNPIKWK; -.
DR   OrthoDB; 5400963at2759; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06956; NR_DBD_RXR; 1.
DR   CDD; cd06943; NR_LBD_RXR_like; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR021780; Nuc_recep-AF1.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24083; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24083:SF90; RETINOIC ACID RECEPTOR RXR-BETA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF11825; Nuc_recep-AF1; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00545; RETINOIDXR.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
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:UP000264800};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004334};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU004334};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT   DOMAIN          86..161
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          180..421
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51843"
FT   REGION          50..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  47230 MW;  AE2E1E6C5E11650B CRC64;
     MSTQQNSSAS NSPRSILGSP FSVISPTLNS PVVSPSLAFG PISSSQISSS APVSGMHSVS
     SSEDIKPPFG LRPLQSPSPG VMTSQKRLCV ICGDRSSGKH YGVYSCEGCK GFFKRTVRKD
     LSYTCRDNKE CLVDKRQRNR CQYCRYQKCL AMGMKREAVQ EERQRNRERE GELEFSVGVN
     DEMPVEKILE AETAVDMRTE LHSDGGSAGN SPHDAVSNIC QTADKQLFAL VEWAKRIPHF
     SELPLDDQVI LLRAGWNELL IASFSHRSIP LKDGALLASE LQRDGAHMAG VGAIFDRENV
     QSAEVGAIFE RVLTELVNKM RDMQMDKTEL GCLRAIVLFN PDAKGLSSTT EVELLREKVY
     ASLEAYCKQK YPEQQGRFAK LLLRLPALRS IGLKCLEHLF FFKLIGDTPI DTFLMEMLEA
     PHQLS
//
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