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Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor NER) (Nuclear receptor subfamily 1 group H member 2) (Ubiquitously-expressed nuclear receptor)

 NR1H2_HUMAN             Reviewed;         460 AA.
P55055; A8K490; B4DNM6; E7EWA6; Q12970; Q5I0Y1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
18-JUL-2018, entry version 196.
RecName: Full=Oxysterols receptor LXR-beta;
AltName: Full=Liver X receptor beta;
AltName: Full=Nuclear receptor NER;
AltName: Full=Nuclear receptor subfamily 1 group H member 2;
AltName: Full=Ubiquitously-expressed nuclear receptor;
Name=NR1H2; Synonyms=LXRB, NER, UNR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Osteosarcoma, and Skin;
PubMed=7926814; DOI=10.1016/0378-1119(94)90080-9;
Shinar D.M., Endo N., Rutledge S.J., Vogel R., Rodan G.A., Schmidt A.;
"NER, a new member of the gene family encoding the human steroid
hormone nuclear receptor.";
Gene 147:273-276(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood, Brain, Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-460 (ISOFORM 1).
Song C., Konkontis J.M., Hiipakka R.A., Liao S.;
"Ubiquitous receptor: a novel receptor that modulates gene activation
by retinoic acid and thyroid hormone receptors.";
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, INTERACTION WITH GPS2, SUMOYLATION AT LYS-409 AND LYS-447,
AND MUTAGENESIS OF LYS-409 AND LYS-447.
PubMed=20159957; DOI=10.1101/gad.545110;
Venteclef N., Jakobsson T., Ehrlund A., Damdimopoulos A., Mikkonen L.,
Ellis E., Nilsson L.M., Parini P., Jaenne O.A., Gustafsson J.A.,
Steffensen K.R., Treuter E.;
"GPS2-dependent corepressor/SUMO pathways govern anti-inflammatory
actions of LRH-1 and LXRbeta in the hepatic acute phase response.";
Genes Dev. 24:381-395(2010).
[7]
FUNCTION, AND INTERACTION WITH CCAR2.
PubMed=25661920; DOI=10.1016/j.jsbmb.2015.02.001;
Sakurabashi A., Wada-Hiraike O., Hirano M., Fu H., Isono W.,
Fukuda T., Morita Y., Tanikawa M., Miyamoto Y., Oda K., Kawana K.,
Osuga Y., Fujii T.;
"CCAR2 negatively regulates nuclear receptor LXRalpha by competing
with SIRT1 deacetylase.";
J. Steroid Biochem. Mol. Biol. 149:80-88(2015).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 208-460 IN COMPLEX WITH
SYNTHETIC LIGANDS.
PubMed=12819202; DOI=10.1074/jbc.M304842200;
Farnegardh M., Bonn T., Sun S., Ljunggren J., Ahola H.,
Wilhelmsson A., Gustafsson J.-A., Carlquist M.;
"The three-dimensional structure of the liver X receptor beta reveals
a flexible ligand-binding pocket that can accommodate fundamentally
different ligands.";
J. Biol. Chem. 278:38821-38828(2003).
-!- FUNCTION: Nuclear receptor that exhibits a ligand-dependent
transcriptional activation activity (PubMed:25661920). Binds
preferentially to double-stranded oligonucleotide direct repeats
having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt
spacing (DR-4). Regulates cholesterol uptake through MYLIP-
dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8.
Interplays functionally with RORA for the regulation of genes
involved in liver metabolism (By similarity). Plays an anti-
inflammatory role during the hepatic acute phase response by
acting as a corepressor: inhibits the hepatic acute phase response
by preventing dissociation of the N-Cor corepressor complex
(PubMed:20159957). {ECO:0000250|UniProtKB:Q60644,
ECO:0000269|PubMed:20159957, ECO:0000269|PubMed:25661920}.
-!- SUBUNIT: Forms a heterodimer with RXR. Interacts with CCAR2 (via
N-terminus) in a ligand-independent manner (PubMed:25661920).
Interacts (when sumoylated) with GPS2; interaction with GPS2 onto
hepatic acute phase protein promoters prevents N-Cor corepressor
complex dissociation (PubMed:20159957).
{ECO:0000269|PubMed:12819202, ECO:0000269|PubMed:20159957,
ECO:0000269|PubMed:25661920}.
-!- INTERACTION:
O95477:ABCA1; NbExp=2; IntAct=EBI-745354, EBI-784112;
Q92828:CORO2A; NbExp=4; IntAct=EBI-745354, EBI-2835660;
Q99750:MDFI; NbExp=3; IntAct=EBI-745354, EBI-724076;
O75376:NCOR1; NbExp=6; IntAct=EBI-745354, EBI-347233;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P55055-1; Sequence=Displayed;
Name=2;
IsoId=P55055-2; Sequence=VSP_053789;
Note=No experimental confirmation.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Sumoylated by SUMO2 at Lys-409 and Lys-447 during the hepatic
acute phase response, leading to promote interaction with GPS2 and
prevent N-Cor corepressor complex dissociation.
{ECO:0000269|PubMed:20159957}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
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EMBL; U07132; AAA61783.1; -; mRNA.
EMBL; AK290855; BAF83544.1; -; mRNA.
EMBL; AK297978; BAG60288.1; -; mRNA.
EMBL; AC008655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007790; AAH07790.1; -; mRNA.
EMBL; BC033500; AAH33500.1; -; mRNA.
EMBL; BC047750; AAH47750.1; -; mRNA.
EMBL; BC074500; AAH74500.1; -; mRNA.
EMBL; U14534; AAA58594.1; -; mRNA.
PIR; JC4014; JC4014.
RefSeq; NP_001243576.1; NM_001256647.1.
RefSeq; NP_009052.3; NM_007121.5.
UniGene; Hs.432976; -.
PDB; 1P8D; X-ray; 2.80 A; A/B=213-460.
PDB; 1PQ6; X-ray; 2.40 A; A/B/C/D=212-460.
PDB; 1PQ9; X-ray; 2.10 A; A/B/C/D=212-460.
PDB; 1PQC; X-ray; 2.80 A; A/B/C/D=212-460.
PDB; 1UPV; X-ray; 2.10 A; A=208-460.
PDB; 1UPW; X-ray; 2.40 A; A=208-460.
PDB; 3KFC; X-ray; 2.40 A; A/B/C/D=212-460.
PDB; 3L0E; X-ray; 2.30 A; A=212-460.
PDB; 4DK7; X-ray; 2.45 A; A/C=218-460.
PDB; 4DK8; X-ray; 2.75 A; A/C=218-460.
PDB; 4NQA; X-ray; 3.10 A; B/I=72-460.
PDB; 4RAK; X-ray; 2.04 A; A/B=213-460.
PDB; 5HJP; X-ray; 2.60 A; B/D=216-460.
PDB; 5I4V; X-ray; 2.61 A; A/E=210-460.
PDB; 5JY3; X-ray; 2.40 A; A/B/C/D=213-460.
PDB; 5KYA; X-ray; 2.60 A; A/E=210-460.
PDB; 5KYJ; X-ray; 2.80 A; A/E=210-460.
PDBsum; 1P8D; -.
PDBsum; 1PQ6; -.
PDBsum; 1PQ9; -.
PDBsum; 1PQC; -.
PDBsum; 1UPV; -.
PDBsum; 1UPW; -.
PDBsum; 3KFC; -.
PDBsum; 3L0E; -.
PDBsum; 4DK7; -.
PDBsum; 4DK8; -.
PDBsum; 4NQA; -.
PDBsum; 4RAK; -.
PDBsum; 5HJP; -.
PDBsum; 5I4V; -.
PDBsum; 5JY3; -.
PDBsum; 5KYA; -.
PDBsum; 5KYJ; -.
ProteinModelPortal; P55055; -.
SMR; P55055; -.
BioGrid; 113222; 58.
ComplexPortal; CPX-652; RXRbeta-LXRbeta nuclear hormone receptor complex.
ComplexPortal; CPX-678; RXRalpha-LXRbeta nuclear hormone receptor complex.
DIP; DIP-53004N; -.
IntAct; P55055; 38.
MINT; P55055; -.
STRING; 9606.ENSP00000253727; -.
BindingDB; P55055; -.
ChEMBL; CHEMBL4093; -.
DrugBank; DB03848; Benzenesulfonyl.
GuidetoPHARMACOLOGY; 601; -.
SwissLipids; SLP:000001551; -.
MoonDB; P55055; Predicted.
iPTMnet; P55055; -.
PhosphoSitePlus; P55055; -.
BioMuta; NR1H2; -.
DMDM; 296439251; -.
EPD; P55055; -.
MaxQB; P55055; -.
PaxDb; P55055; -.
PeptideAtlas; P55055; -.
PRIDE; P55055; -.
ProteomicsDB; 56767; -.
DNASU; 7376; -.
Ensembl; ENST00000253727; ENSP00000253727; ENSG00000131408. [P55055-1]
Ensembl; ENST00000411902; ENSP00000396151; ENSG00000131408. [P55055-2]
Ensembl; ENST00000593926; ENSP00000471194; ENSG00000131408. [P55055-1]
GeneID; 7376; -.
KEGG; hsa:7376; -.
UCSC; uc002psa.6; human. [P55055-1]
CTD; 7376; -.
DisGeNET; 7376; -.
EuPathDB; HostDB:ENSG00000131408.13; -.
GeneCards; NR1H2; -.
HGNC; HGNC:7965; NR1H2.
HPA; HPA056838; -.
HPA; HPA070212; -.
MIM; 600380; gene.
neXtProt; NX_P55055; -.
OpenTargets; ENSG00000131408; -.
PharmGKB; PA31750; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOGENOM; HOG000220845; -.
HOVERGEN; HBG108655; -.
InParanoid; P55055; -.
KO; K08535; -.
OMA; RRYACRG; -.
OrthoDB; EOG091G0I4P; -.
PhylomeDB; P55055; -.
TreeFam; TF352167; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
SignaLink; P55055; -.
SIGNOR; P55055; -.
ChiTaRS; NR1H2; human.
EvolutionaryTrace; P55055; -.
GeneWiki; Liver_X_receptor_beta; -.
GenomeRNAi; 7376; -.
PRO; PR:P55055; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000131408; -.
CleanEx; HS_NR1H2; -.
ExpressionAtlas; P55055; baseline and differential.
Genevisible; P55055; HS.
GO; GO:0005737; C:cytoplasm; IDA:HGNC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0034191; F:apolipoprotein A-I receptor binding; IPI:BHF-UCL.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0004879; F:nuclear receptor activity; TAS:ProtInc.
GO; GO:0046965; F:retinoid X receptor binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0044255; P:cellular lipid metabolic process; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
GO; GO:0010887; P:negative regulation of cholesterol storage; IMP:BHF-UCL.
GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; NAS:BHF-UCL.
GO; GO:0032369; P:negative regulation of lipid transport; IMP:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:0048550; P:negative regulation of pinocytosis; IMP:BHF-UCL.
GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:BHF-UCL.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
GO; GO:0090108; P:positive regulation of high-density lipoprotein particle assembly; IEA:Ensembl.
GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IMP:BHF-UCL.
GO; GO:0090187; P:positive regulation of pancreatic juice secretion; IEA:Ensembl.
GO; GO:0090340; P:positive regulation of secretion of lysosomal enzymes; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:BHF-UCL.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR023257; Liver_X_rcpt.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR02034; LIVERXRECPTR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Polymorphism;
Receptor; Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 460 Oxysterols receptor LXR-beta.
/FTId=PRO_0000053532.
DOMAIN 222 460 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 84 161 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 87 107 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 125 149 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 85 Transactivation AF-1; required for
ligand-independent transactivation
function. {ECO:0000269|PubMed:25661920}.
REGION 219 460 Transactivation AF-2; required for
ligand-dependent transactivation
function; mediates interaction with
CCAR2. {ECO:0000269|PubMed:25661920}.
COMPBIAS 190 195 Poly-Ser.
CROSSLNK 409 409 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000269|PubMed:20159957}.
CROSSLNK 447 447 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000269|PubMed:20159957}.
VAR_SEQ 61 158 VIPDPEEEPERKRKKGPAPKMLGHELCRVCGDKASGFHYNV
LSCEGCKGFFRRSVVRGGARRYACRGGGTCQMDAFMRRKCQ
QCRLRKCKEAGMREQC -> G (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053789.
VARIANT 2 2 S -> F (in dbSNP:rs41379547).
/FTId=VAR_050579.
MUTAGEN 409 409 K->R: Impaired ability to act as an anti-
inflammatory role during the hepatic
acute phase response; when associated
with R-447.
{ECO:0000269|PubMed:20159957}.
MUTAGEN 447 447 K->R: Impaired ability to act as an anti-
inflammatory role during the hepatic
acute phase response; when associated
with R-409.
{ECO:0000269|PubMed:20159957}.
CONFLICT 175 175 Q -> QQ (in Ref. 1; AAA61783, 2;
BAF83544/BAG60288, 4; AAH07790/AAH33500/
AAH47750/AAH74500 and 5; AAA58594).
{ECO:0000305}.
CONFLICT 244 244 D -> G (in Ref. 2; BAG60288).
{ECO:0000305}.
STRAND 88 90 {ECO:0000244|PDB:4NQA}.
STRAND 99 103 {ECO:0000244|PDB:4NQA}.
HELIX 105 116 {ECO:0000244|PDB:4NQA}.
HELIX 137 139 {ECO:0000244|PDB:4NQA}.
HELIX 142 151 {ECO:0000244|PDB:4NQA}.
HELIX 162 165 {ECO:0000244|PDB:4NQA}.
TURN 167 169 {ECO:0000244|PDB:4NQA}.
HELIX 170 173 {ECO:0000244|PDB:4NQA}.
TURN 176 178 {ECO:0000244|PDB:4NQA}.
STRAND 183 185 {ECO:0000244|PDB:4NQA}.
STRAND 212 214 {ECO:0000244|PDB:4NQA}.
HELIX 221 241 {ECO:0000244|PDB:4RAK}.
HELIX 242 244 {ECO:0000244|PDB:4RAK}.
TURN 245 247 {ECO:0000244|PDB:4RAK}.
HELIX 260 286 {ECO:0000244|PDB:4RAK}.
HELIX 291 293 {ECO:0000244|PDB:4RAK}.
HELIX 296 317 {ECO:0000244|PDB:4RAK}.
STRAND 318 320 {ECO:0000244|PDB:4NQA}.
TURN 321 324 {ECO:0000244|PDB:4RAK}.
STRAND 325 328 {ECO:0000244|PDB:4RAK}.
TURN 329 331 {ECO:0000244|PDB:4RAK}.
STRAND 332 334 {ECO:0000244|PDB:4RAK}.
HELIX 336 340 {ECO:0000244|PDB:4RAK}.
TURN 341 343 {ECO:0000244|PDB:4RAK}.
HELIX 349 360 {ECO:0000244|PDB:4RAK}.
TURN 361 363 {ECO:0000244|PDB:4RAK}.
HELIX 366 377 {ECO:0000244|PDB:4RAK}.
HELIX 388 409 {ECO:0000244|PDB:4RAK}.
TURN 411 413 {ECO:0000244|PDB:4RAK}.
HELIX 416 434 {ECO:0000244|PDB:4RAK}.
STRAND 444 446 {ECO:0000244|PDB:4RAK}.
HELIX 450 455 {ECO:0000244|PDB:4RAK}.
SEQUENCE 460 AA; 50974 MW; 9465A6FFB7FCFD2F CRC64;
MSSPTTSSLD TPLPGNGPPQ PGAPSSSPTV KEEGPEPWPG GPDPDVPGTD EASSACSTDW
VIPDPEEEPE RKRKKGPAPK MLGHELCRVC GDKASGFHYN VLSCEGCKGF FRRSVVRGGA
RRYACRGGGT CQMDAFMRRK CQQCRLRKCK EAGMREQCVL SEEQIRKKKI RKQQQESQSQ
SQSPVGPQGS SSSASGPGAS PGGSEAGSQG SGEGEGVQLT AAQELMIQQL VAAQLQCNKR
SFSDQPKVTP WPLGADPQSR DARQQRFAHF TELAIISVQE IVDFAKQVPG FLQLGREDQI
ALLKASTIEI MLLETARRYN HETECITFLK DFTYSKDDFH RAGLQVEFIN PIFEFSRAMR
RLGLDDAEYA LLIAINIFSA DRPNVQEPGR VEALQQPYVE ALLSYTRIKR PQDQLRFPRM
LMKLVSLRTL SSVHSEQVFA LRLQDKKLPP LLSEIWDVHE


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