位置:首页 > 蛋白库 > RARB_CHICK
RARB_CHICK
ID   RARB_CHICK              Reviewed;         455 AA.
AC   P22448; P27537; Q90598; Q91354;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Retinoic acid receptor beta;
DE            Short=RAR-beta;
DE   AltName: Full=Nuclear receptor subfamily 1 group B member 2;
GN   Name=RARB; Synonyms=NR1B2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
RX   PubMed=1849630; DOI=10.1093/nar/19.2.395;
RA   Padanilam B.J., McLeod L.B., Suzuki H., Solursh M.;
RT   "Nucleotide sequence of an isoform of chicken retinoic acid binding
RT   protein-beta varying in its A domain.";
RL   Nucleic Acids Res. 19:395-395(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
RX   PubMed=1647216; DOI=10.1016/0167-4781(91)90024-g;
RA   Nohno T., Muto K., Noji S., Saito T., Taniguchi S.;
RT   "Isoforms of retinoic acid receptor beta expressed in the chicken embryo.";
RL   Biochim. Biophys. Acta 1089:273-275(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2), AND DEVELOPMENTAL STAGE.
RC   STRAIN=White leghorn;
RX   PubMed=1848357; DOI=10.1038/350083a0;
RA   Noji S., Nohno T., Koyama E., Muto K., Ohyama K., Aoki Y., Tamura K.,
RA   Ohsugi K., Ide H., Taniguchi S., Saito T.;
RT   "Retinoic acid induces polarizing activity but is unlikely to be a
RT   morphogen in the chick limb bud.";
RL   Nature 350:83-86(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
RX   PubMed=1849811; DOI=10.1242/dev.111.1.245;
RA   Smith S.M., Eichele G.;
RT   "Temporal and regional differences in the expression pattern of distinct
RT   retinoic acid receptor-beta transcripts in the chick embryo.";
RL   Development 111:245-252(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-59 (ISOFORM BETA-1), FUNCTION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=7703521; DOI=10.1002/aja.1002020106;
RA   Smith S.M., Kirstein I.J., Wang Z.S., Fallon J.F., Kelley J.,
RA   Bradshaw-Rouse J.;
RT   "Differential expression of retinoic acid receptor-beta isoforms during
RT   chick limb ontogeny.";
RL   Dev. Dyn. 202:54-66(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-455 (ISOFORM BETA-2), INDUCTION, FUNCTION,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=1652423; DOI=10.1242/dev.111.4.1007;
RA   Rowe A., Richman J.M., Brickell P.M.;
RT   "Retinoic acid treatment alters the distribution of retinoic acid receptor-
RT   beta transcripts in the embryonic chick face.";
RL   Development 111:1007-1016(1991).
CC   -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC       heterodimers to their target response elements in response to their
CC       ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC       in various biological processes. The RAR/RXR heterodimers bind to the
CC       retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3'
CC       sites known as DR1-DR5 (By similarity). Required for limb and
CC       craniofacial development. {ECO:0000250, ECO:0000269|PubMed:1652423,
CC       ECO:0000269|PubMed:7703521}.
CC   -!- SUBUNIT: Heterodimer; with a RXR molecule. Binds DNA preferentially as
CC       a RAR/RXR heterodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta-1;
CC         IsoId=P22448-1; Sequence=Displayed;
CC       Name=Beta-2;
CC         IsoId=P22448-2; Sequence=VSP_003641;
CC   -!- DEVELOPMENTAL STAGE: In the developing embryo, expressed in the limb
CC       bud mesenchyme, in cranofacial mesenchyme, and in hindbrain
CC       neuroectoderm. At stages 20, 24 and 28 of embryonic development,
CC       expressed ununiformly in facial primordia. Present in lateral nasal
CC       processes, at edges and corners of frontonasal mass and in the anterior
CC       part of the maxillary primordia. Expressed in mesenchyme at all stages
CC       of facial development. In the developing limb, isoform Beta-1 is
CC       expressed limb bud mesenchyme and ectoderm, then become restricted
CC       within perichondrial regions and loose connective tissue of the limb,
CC       while isoform Beta-2, expressed in subsets of similar tissues, in the
CC       proximal limb mesenchyme and in the initial mesenchymal condensate.
CC       later abundantly expressed in cells lateral to the digit cartilage.
CC       {ECO:0000269|PubMed:1652423, ECO:0000269|PubMed:1848357,
CC       ECO:0000269|PubMed:7703521}.
CC   -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:1652423}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X56674; CAA39997.1; -; mRNA.
DR   EMBL; X57341; CAA40617.1; -; mRNA.
DR   EMBL; X57340; CAA40616.1; -; mRNA.
DR   EMBL; X57339; CAA40615.1; -; mRNA.
DR   EMBL; S75943; AAB33959.1; -; mRNA.
DR   EMBL; X59473; CAA42077.1; -; mRNA.
DR   EMBL; S63196; AAB19628.1; -; mRNA.
DR   PIR; A43786; A43786.
DR   PIR; I51272; I51272.
DR   PIR; S13512; S13512.
DR   RefSeq; NP_990657.1; NM_205326.1. [P22448-1]
DR   RefSeq; XP_015136799.1; XM_015281313.1. [P22448-1]
DR   RefSeq; XP_015136800.1; XM_015281314.1. [P22448-1]
DR   RefSeq; XP_015136802.1; XM_015281316.1. [P22448-2]
DR   AlphaFoldDB; P22448; -.
DR   SMR; P22448; -.
DR   STRING; 9031.ENSGALP00000036953; -.
DR   PaxDb; P22448; -.
DR   Ensembl; ENSGALT00000037748; ENSGALP00000036953; ENSGALG00000011298. [P22448-1]
DR   Ensembl; ENSGALT00000049834; ENSGALP00000052356; ENSGALG00000011298. [P22448-1]
DR   GeneID; 396266; -.
DR   KEGG; gga:396266; -.
DR   CTD; 5915; -.
DR   VEuPathDB; HostDB:geneid_396266; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000156196; -.
DR   HOGENOM; CLU_007368_18_2_1; -.
DR   InParanoid; P22448; -.
DR   OMA; PFHATRN; -.
DR   OrthoDB; 1165737at2759; -.
DR   PhylomeDB; P22448; -.
DR   TreeFam; TF328382; -.
DR   Reactome; R-GGA-383280; Nuclear Receptor transcription pathway.
DR   PRO; PR:P22448; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000011298; Expressed in spermatid and 12 other tissues.
DR   ExpressionAtlas; P22448; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071729; P:beak morphogenesis; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0070660; P:inner ear receptor cell differentiation involved in inner ear sensory epithelium regeneration; NAS:AgBase.
DR   GO; GO:0035108; P:limb morphogenesis; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; 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; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR003078; Retinoic_acid_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01292; RETNOICACIDR.
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   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..455
FT                   /note="Retinoic acid receptor beta"
FT                   /id="PRO_0000053469"
FT   DOMAIN          183..417
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        88..153
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         88..108
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         124..148
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..87
FT                   /note="Modulating"
FT                   /evidence="ECO:0000250"
FT   REGION          44..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..182
FT                   /note="Hinge"
FT                   /evidence="ECO:0000250"
FT   REGION          416..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..60
FT                   /note="MTTSSRTCPVPAVNGHMTHYPAAPYPLLFPPVIGGLSLPSLHGLQSHPPTSG
FT                   CSTPSPAT -> MFDCMDVLAVSPAQMLDFYTASPSSCMLQEKALKACFSGLAQTEWQH
FT                   RHSAQS (in isoform Beta-2)"
FT                   /evidence="ECO:0000303|PubMed:1647216,
FT                   ECO:0000303|PubMed:1652423, ECO:0000303|PubMed:1848357,
FT                   ECO:0000303|PubMed:1849811"
FT                   /id="VSP_003641"
FT   CONFLICT        30
FT                   /note="P -> A (in Ref. 1; CAA39997)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="S -> T (in Ref. 4; CAA42077)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="E -> D (in Ref. 6; AAB19628)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   455 AA;  50708 MW;  819F6083ECA50610 CRC64;
     MTTSSRTCPV PAVNGHMTHY PAAPYPLLFP PVIGGLSLPS LHGLQSHPPT SGCSTPSPAT
     VETQSTSSEE LVPSPPSPLP PPRVYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM
     VYTCHRDKNC VINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKEPT KQESTENYEM
     TAELDDLTEK IRKAHQETFP SLCQLGKYTT NSSADHRVRL DLGLWDKFSE LATKCIIKIV
     EFAKRLPGFT SLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
     GFGPLTDLVF TFANQLLPLE MDDTETGLLS AICLICGDRQ DLEEPMKVDK LQEPLLEALK
     IYIRKRRPNK PHMFPKILMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGH
     EPLTPTSNGN TAEHSPSISP SSVDNSSVSQ SPMVQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024