APOBR_MOUSE
ID APOBR_MOUSE Reviewed; 942 AA.
AC Q8VBT6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Apolipoprotein B receptor {ECO:0000305};
DE AltName: Full=Apolipoprotein B-100 receptor;
DE Short=Apolipoprotein B48 receptor;
DE Short=apoB-48R;
GN Name=Apobr {ECO:0000312|MGI:MGI:2176230}; Synonyms=Apob48r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=129; TISSUE=Macrophage;
RX PubMed=12177162;
RA Brown M.L., Yui K., Smith J.D., LeBoeuf R.C., Weng W., Umeda P.K., Li R.,
RA Song R., Gianturco S.H., Bradley W.A.;
RT "The murine macrophage apoB-48 receptor gene (Apob-48r): homology to the
RT human receptor.";
RL J. Lipid Res. 43:1181-1191(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INDUCTION.
RX PubMed=17192460; DOI=10.2337/db06-1076;
RA Lumeng C.N., Deyoung S.M., Bodzin J.L., Saltiel A.R.;
RT "Increased inflammatory properties of adipose tissue macrophages recruited
RT during diet-induced obesity.";
RL Diabetes 56:16-23(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; SER-484 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Macrophage receptor that binds to the apolipoprotein B48
CC (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a
CC like domain of APOB in hypertriglyceridemic very low density
CC lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the
CC context of the macrophage. May provide essential lipids to
CC reticuloendothelial cells. Could also be involved in foam cell
CC formation with elevated TRL and remnant lipoprotein (RLP). Mediates the
CC rapid high-affinity uptake of chylomicrons (CM), HTG-VLDL, and
CC trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages.
CC {ECO:0000269|PubMed:12177162}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Binds monocyte-macrophage membrane. Thought
CC to be anchored in the membrane through an interaction with an integral
CC membrane protein (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, lung and skeletal
CC muscle, and weakly in brain, heart, kidney, and testis.
CC {ECO:0000269|PubMed:12177162}.
CC -!- DEVELOPMENTAL STAGE: Finds at the highest levels in 7 dpc, then
CC progressively lower at 11 dpc and 15 dpc, and finally very diminished
CC at the 17 dpc. {ECO:0000269|PubMed:12177162}.
CC -!- INDUCTION: Increased in high-fat diet ATM (adipose tissue macrophages).
CC {ECO:0000269|PubMed:17192460}.
CC -!- PTM: There are 2 forms in macrophages, the membrane-binding proteins
CC 200 kDa (MBP 200) and 235 kDa (MBP 235), that can be reduced into a
CC single active ligand-binding species with intermediate mobility (MBP
CC 200R). {ECO:0000250}.
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DR EMBL; AF141335; AAL54862.1; -; mRNA.
DR EMBL; AF141336; AAL54863.1; -; Genomic_DNA.
DR EMBL; BC030718; AAH30718.1; -; mRNA.
DR CCDS; CCDS21834.1; -.
DR RefSeq; NP_612183.1; NM_138310.1.
DR AlphaFoldDB; Q8VBT6; -.
DR BioGRID; 228601; 1.
DR STRING; 10090.ENSMUSP00000042028; -.
DR iPTMnet; Q8VBT6; -.
DR PhosphoSitePlus; Q8VBT6; -.
DR SwissPalm; Q8VBT6; -.
DR CPTAC; non-CPTAC-3448; -.
DR EPD; Q8VBT6; -.
DR jPOST; Q8VBT6; -.
DR MaxQB; Q8VBT6; -.
DR PaxDb; Q8VBT6; -.
DR PeptideAtlas; Q8VBT6; -.
DR PRIDE; Q8VBT6; -.
DR ProteomicsDB; 296337; -.
DR Antibodypedia; 26469; 237 antibodies from 22 providers.
DR DNASU; 171504; -.
DR Ensembl; ENSMUST00000039522; ENSMUSP00000042028; ENSMUSG00000042759.
DR GeneID; 171504; -.
DR KEGG; mmu:171504; -.
DR UCSC; uc009jsb.1; mouse.
DR CTD; 55911; -.
DR MGI; MGI:2176230; Apobr.
DR VEuPathDB; HostDB:ENSMUSG00000042759; -.
DR eggNOG; ENOG502SSHE; Eukaryota.
DR GeneTree; ENSGT00530000065031; -.
DR HOGENOM; CLU_006101_0_0_1; -.
DR InParanoid; Q8VBT6; -.
DR OMA; RVWVLEE; -.
DR OrthoDB; 248102at2759; -.
DR PhylomeDB; Q8VBT6; -.
DR TreeFam; TF337147; -.
DR Reactome; R-MMU-8964046; VLDL clearance.
DR BioGRID-ORCS; 171504; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Apobr; mouse.
DR PRO; PR:Q8VBT6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VBT6; protein.
DR Bgee; ENSMUSG00000042759; Expressed in granulocyte and 74 other tissues.
DR ExpressionAtlas; Q8VBT6; baseline and differential.
DR Genevisible; Q8VBT6; MM.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006641; P:triglyceride metabolic process; IDA:MGI.
DR InterPro; IPR026158; ApolipoprotB_rcpt.
DR PANTHER; PTHR15964; PTHR15964; 2.
PE 1: Evidence at protein level;
KW Atherosclerosis; Cell membrane; Cholesterol metabolism; Chylomicron; LDL;
KW Lipid metabolism; Lipid transport; Lipoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Steroid metabolism; Sterol metabolism;
KW Transport; VLDL.
FT CHAIN 1..942
FT /note="Apolipoprotein B receptor"
FT /id="PRO_0000327264"
FT REGION 66..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
SQ SEQUENCE 942 AA; 102705 MW; D88B379D1928C6AF CRC64;
MDFLRLRLPG LHQALRGALD SFSAFVSYLV GDTVPTVERQ TQAAEELGEV TEGKVVGEEA
QEVLEGLRSG QSEGVEAPEE TRRCQEGSLA GEQTWGWRAD SSARPQAERQ DTGSWKAAED
ARGQEPSVPL KPEAEPGTHR DRSSNTAQEI WEHGEEEASS GEPLRTCEQK EEEEEVVRAA
ESGMAEGVES QPTWHSEPGG NAGTEGQHVT EDSKEIDWVA KDMVAEIEWF GAKGIDKEEE
RMVPMRDGER ARAQGTQCPG AESEDQAMLS REAWTVSDRE GADSLGVQGT EYGSDPGDNF
PGTTGRVWVL EEADKGDQQD EVDEKREAEV RFPIQTLEAE RTGEMTEGHI AEEEAMGEQE
TEGSFEDEER QDLAIRDNGV SLEEEVRAEE SSREKRNSWA TEPTLVLDTE AKDEPDWEDS
PEVSTEELFV GERSEAAQMT PEVLRVKVTE GQDPELVRHS QALTKQLEEG QKGQEETSGA
PDLSPERVLS LKEYPGPVGF AGPELEAWGN WSRGVDRRNS QEVKADAEAG KEQTATEQAV
EIRAEGGQEA QQPEVFGSGG EEALTSVALN PELEGSQGAE AGTEESVEES KPTENEAAEE
EAVVPWEADG TCRKRRLEEV TLSLQDSEDT ETSYLAEEII VGIRAVDTEE GPKWEAGLAP
ETELGKAWCS EGRGEAGRGT ELEETTEKQS GQEVGLVGSA EKVSGYDIQE IDGTEEGEQA
EMETSVMAED IRGTDGVTLG SQAERAEGSI TPMETEGLLR DQMLLEEEAG GGQSREQKVH
NSEGEIQTLD DSSDQEGQQT HQIPTVAVPG PLESAEATAG APGDVHSNWN EALLPGSRLD
VSVPRSRVLL SRSSSRRRSR PSFHRISVPE PQCDPPSPQP QAERPVPEQS SLQLEETPEL
SATKPEGTPV PARRKMLGRG FGFAHPGMMQ ELQARLSQPK PQ
