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Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPI-HBP1) (GPI-anchored HDL-binding protein 1) (High density lipoprotein-binding protein 1)

 HDBP1_MOUSE             Reviewed;         228 AA.
Q9D1N2;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 {ECO:0000303|PubMed:16141072};
Short=GPI-HBP1;
Short=GPI-anchored HDL-binding protein 1 {ECO:0000303|PubMed:16141072};
AltName: Full=High density lipoprotein-binding protein 1 {ECO:0000312|EMBL:BAC23061.1};
Flags: Precursor;
Name=Gpihbp1 {ECO:0000312|MGI:MGI:1915703};
Synonyms=Hbp1 {ECO:0000312|EMBL:BAC23061.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:BAC23061.1}
NUCLEOTIDE SEQUENCE [MRNA], HDL-BINDING, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND GPI-ANCHOR AT GLY-198.
TISSUE=Liver {ECO:0000269|PubMed:12496272};
PubMed=12496272; DOI=10.1074/jbc.M211932200;
Ioka R.X., Kang M.-J., Kamiyama S., Kim D.-H., Magoori K.,
Kamataki A., Ito Y., Takei Y.A., Sasaki M., Suzuki T., Sasano H.,
Takahashi S., Sakai J., Fujino T., Yamamoto T.T.;
"Expression cloning and characterization of a novel
glycosylphosphatidylinositol-anchored high density lipoprotein-binding
protein, GPI-HBP1.";
J. Biol. Chem. 278:7344-7349(2003).
[2] {ECO:0000312|EMBL:BAB22704.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22704.1};
TISSUE=Embryo {ECO:0000312|EMBL:BAB22704.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000312|EMBL:AAH61225.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4] {ECO:0000305}
FUNCTION, INTERACTION WITH LPL, SUBUNIT, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=17403372; DOI=10.1016/j.cmet.2007.02.002;
Beigneux A.P., Davies B.S.J., Gin P., Weinstein M.M., Farber E.,
Qiao X., Peale F., Bunting S., Walzem R.L., Wong J.S., Blaner W.S.,
Ding Z.-M., Melford K., Wongsiriroj N., Shu X., de Sauvage F.,
Ryan R.O., Fong L.G., Bensadoun A., Young S.G.;
"Glycosylphosphatidylinositol-anchored high-density lipoprotein-
binding protein 1 plays a critical role in the lipolytic processing of
chylomicrons.";
Cell Metab. 5:279-291(2007).
[5] {ECO:0000305}
FUNCTION.
PubMed=17620854; DOI=10.1097/MOL.0b013e3281527914;
Young S.G., Davies B.S.J., Fong L.G., Gin P., Weinstein M.M.,
Bensadoun A., Beigneux A.P.;
"GPIHBP1: an endothelial cell molecule important for the lipolytic
processing of chylomicrons.";
Curr. Opin. Lipidol. 18:389-396(2007).
[6]
GLYCOSYLATION AT ASN-76.
PubMed=18340083; DOI=10.1194/jlr.M700593-JLR200;
Beigneux A.P., Gin P., Davies B.S., Weinstein M.M., Bensadoun A.,
Ryan R.O., Fong L.G., Young S.G.;
"Glycosylation of Asn-76 in mouse GPIHBP1 is critical for its
appearance on the cell surface and the binding of chylomicrons and
lipoprotein lipase.";
J. Lipid Res. 49:1312-1321(2008).
[7]
MUTAGENESIS OF GLN-114.
PubMed=19304573; DOI=10.1161/ATVBAHA.109.186577;
Beigneux A.P., Franssen R., Bensadoun A., Gin P., Melford K.,
Peter J., Walzem R.L., Weinstein M.M., Davies B.S.J.,
Kuivenhoven J.A., Kastelein J.J.P., Fong L.G., Dallinga-Thie G.M.,
Young S.G.;
"Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind
lipoprotein lipase.";
Arterioscler. Thromb. Vasc. Biol. 29:956-962(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=20620994; DOI=10.1016/j.cmet.2010.04.016;
Davies B.S., Beigneux A.P., Barnes R.H. II, Tu Y., Gin P.,
Weinstein M.M., Nobumori C., Nyren R., Goldberg I., Olivecrona G.,
Bensadoun A., Young S.G., Fong L.G.;
"GPIHBP1 is responsible for the entry of lipoprotein lipase into
capillaries.";
Cell Metab. 12:42-52(2010).
[10]
REVIEW.
PubMed=21844202; DOI=10.1194/jlr.R018689;
Young S.G., Davies B.S., Voss C.V., Gin P., Weinstein M.M.,
Tontonoz P., Reue K., Bensadoun A., Fong L.G., Beigneux A.P.;
"GPIHBP1, an endothelial cell transporter for lipoprotein lipase.";
J. Lipid Res. 52:1869-1884(2011).
[11]
SUBUNIT, AND MUTAGENESIS OF CYS-88.
PubMed=25387803; DOI=10.1161/CIRCRESAHA.116.305085;
Beigneux A.P., Fong L.G., Bensadoun A., Davies B.S., Oberer M.,
Gaardsvoll H., Ploug M., Young S.G.;
"GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and
thereby prevent lipoprotein lipase binding.";
Circ. Res. 116:624-632(2015).
-!- FUNCTION: Plays a key role in the lipolytic processing of
chylomicrons. Required for the transport of lipoprotein lipase LPL
into the capillary lumen and across endothelial cells.
{ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:17620854,
ECO:0000269|PubMed:20620994}.
-!- SUBUNIT: Mostly monomer, but also homodimer and homooligomer
(PubMed:25387803). Interacts with high affinity with high-density
lipoprotein (HDL) (PubMed:12496272). Only monomer interacts with
lipoprotein lipase (LPL) (PubMed:25387803, PubMed:17403372).
Interacts with chylomicrons and APOA5 (By similarity).
{ECO:0000250|UniProtKB:Q8IV16, ECO:0000269|PubMed:12496272,
ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:25387803}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:20620994}. Basolateral cell membrane
{ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:20620994}. Cell membrane
{ECO:0000269|PubMed:20620994}; Peripheral membrane protein
{ECO:0000269|PubMed:20620994}; Extracellular side
{ECO:0000269|PubMed:20620994}.
-!- TISSUE SPECIFICITY: Highly expressed on the luminal surface of
capillary endothelium in heart, adipose tissue and skeletal
muscle. Not detected in capillaries of the brain. Expressed at
lower levels in lung and liver. {ECO:0000269|PubMed:12496272,
ECO:0000269|PubMed:17403372}.
-!- PTM: Glycosylation of Asn-76 is critical for cell surface
localization and the binding of chylomicrons and lipoprotein
lipase. {ECO:0000269|PubMed:18340083}.
-!- DISRUPTION PHENOTYPE: Mice manifest chylomicronemia, exhibiting a
marked accumulation of chylomicrons in the plasma resulting in a
milky plasma and plasma triglyceride levels as high as 5000 mg/dl.
In Gpihbp1-deficient mice, LPL is mislocalized to the interstitial
spaces surrounding myocytes and adipocytes.
{ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994}.
-----------------------------------------------------------------------
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EMBL; AB095543; BAC23061.1; -; mRNA.
EMBL; AK003305; BAB22704.1; -; mRNA.
EMBL; BC061225; AAH61225.1; -; mRNA.
CCDS; CCDS27545.1; -.
RefSeq; NP_081006.1; NM_026730.1.
UniGene; Mm.46367; -.
ProteinModelPortal; Q9D1N2; -.
IntAct; Q9D1N2; 1.
MINT; MINT-4126642; -.
STRING; 10090.ENSMUSP00000023243; -.
iPTMnet; Q9D1N2; -.
PhosphoSitePlus; Q9D1N2; -.
MaxQB; Q9D1N2; -.
PaxDb; Q9D1N2; -.
PeptideAtlas; Q9D1N2; -.
PRIDE; Q9D1N2; -.
Ensembl; ENSMUST00000023243; ENSMUSP00000023243; ENSMUSG00000022579.
GeneID; 68453; -.
UCSC; uc007wgw.1; mouse.
CTD; 338328; -.
MGI; MGI:1915703; Gpihbp1.
eggNOG; ENOG410J46G; Eukaryota.
eggNOG; ENOG41116TR; LUCA.
GeneTree; ENSGT00390000012601; -.
HOGENOM; HOG000112872; -.
InParanoid; Q9D1N2; -.
OMA; QSTLCNI; -.
OrthoDB; EOG091G0UW5; -.
PhylomeDB; Q9D1N2; -.
TreeFam; TF338440; -.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
Reactome; R-MMU-8963901; Chylomicron remodeling.
Reactome; R-MMU-975634; Retinoid metabolism and transport.
PRO; PR:Q9D1N2; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022579; -.
CleanEx; MM_HBP1; -.
ExpressionAtlas; Q9D1N2; baseline and differential.
Genevisible; Q9D1N2; MM.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IEA:Ensembl.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0035478; F:chylomicron binding; IMP:BHF-UCL.
GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:MGI.
GO; GO:0035473; F:lipase binding; IPI:BHF-UCL.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0071813; F:lipoprotein particle binding; IMP:UniProtKB.
GO; GO:0008320; F:protein transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0006886; P:intracellular protein transport; IDA:BHF-UCL.
GO; GO:0006869; P:lipid transport; IDA:MGI.
GO; GO:0090321; P:positive regulation of chylomicron remnant clearance; IMP:BHF-UCL.
GO; GO:0090319; P:positive regulation of chylomicron remodeling; IC:BHF-UCL.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
GO; GO:0017038; P:protein import; IDA:BHF-UCL.
GO; GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0071503; P:response to heparin; IEA:Ensembl.
GO; GO:0045056; P:transcytosis; IDA:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
InterPro; IPR018363; CD59_antigen_CS.
InterPro; IPR016054; LY6_UPA_recep-like.
Pfam; PF00021; UPAR_LY6; 1.
PROSITE; PS00983; LY6_UPAR; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; HDL; Hyperlipidemia; Lipid-binding; Lipoprotein; Membrane;
Reference proteome; Signal; Transport.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 198 Glycosylphosphatidylinositol-anchored
high density lipoprotein-binding protein
1.
/FTId=PRO_0000343798.
PROPEP 199 228 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000429859.
DOMAIN 61 148 UPAR/Ly6. {ECO:0000255}.
COMPBIAS 38 42 Poly-Asp. {ECO:0000255}.
COMPBIAS 43 48 Poly-Glu. {ECO:0000255}.
LIPID 198 198 GPI-anchor amidated glycine.
{ECO:0000305|PubMed:12496272}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18340083}.
DISULFID 63 88 {ECO:0000250|UniProtKB:Q16553}.
DISULFID 66 75 {ECO:0000250|UniProtKB:Q16553}.
DISULFID 81 109 {ECO:0000250|UniProtKB:Q16553}.
DISULFID 113 129 {ECO:0000250|UniProtKB:Q16553}.
DISULFID 130 135 {ECO:0000250|UniProtKB:Q16553}.
MUTAGEN 88 88 C->A: Reduced number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 114 114 Q->P: Does not affect expression of the
at the cell surface. Cannot bind LPL and
chylomicrons.
{ECO:0000269|PubMed:19304573}.
SEQUENCE 228 AA; 24566 MW; B2FB456A10865E81 CRC64;
MKALRAVLLI LLLSGQPGSG WAQEDGDADP EPENYNYDDD DDEEEEEETN MIPGSRDRAP
LQCYFCQVLH SGESCNQTQS CSSSKPFCIT LVSHSGTDKG YLTTYSMWCT DTCQPIIKTV
GGTQMTQTCC QSTLCNIPPW QNPQVQNPLG GRADSPLESG TRHPQGGKFS HPQVVKAAHP
QSDGANLPKS GKANQPQGSG AGYPSGWTKF GNIALLLSFF TCLWASGA


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