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Protein

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1

Gene

Gpihbp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  • chylomicron binding Source: BHF-UCL
  • high-density lipoprotein particle binding Source: MGI
  • lipase binding Source: BHF-UCL
  • lipid binding Source: UniProtKB-KW
  • lipoprotein particle binding Source: UniProtKB
  • protein transmembrane transporter activity Source: BHF-UCL

GO - Biological processi

  • cholesterol homeostasis Source: BHF-UCL
  • intracellular protein transport Source: BHF-UCL
  • lipid transport Source: MGI
  • positive regulation of chylomicron remnant clearance Source: BHF-UCL
  • positive regulation of chylomicron remodeling Source: BHF-UCL
  • positive regulation of lipoprotein lipase activity Source: BHF-UCL
  • protein import Source: BHF-UCL
  • protein localization to cell surface Source: BHF-UCL
  • protein stabilization Source: BHF-UCL
  • response to heparin Source: Ensembl
  • transcytosis Source: BHF-UCL
  • triglyceride homeostasis Source: BHF-UCL

Keywordsi

Biological processTransport
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-163125. Post-translational modification: synthesis of GPI-anchored proteins.
R-MMU-8963889. Assembly of active LPL and LIPC lipase complexes.
R-MMU-8963901. Chylomicron remodeling.
R-MMU-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 11 Publication
Short name:
GPI-HBP1
Short name:
GPI-anchored HDL-binding protein 11 Publication
Alternative name(s):
High density lipoprotein-binding protein 1Imported
Gene namesi
Name:Gpihbp1Imported
Synonyms:Hbp1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1915703. Gpihbp1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: Ensembl
  • anchored component of plasma membrane Source: MGI
  • apical plasma membrane Source: BHF-UCL
  • basolateral plasma membrane Source: BHF-UCL
  • cell surface Source: MGI
  • external side of plasma membrane Source: BHF-UCL
  • high-density lipoprotein particle Source: UniProtKB-KW
  • intracellular Source: GOC

Keywords - Cellular componenti

Cell membrane, HDL, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi88C → A: Reduced number of monomers. 1 Publication1
Mutagenesisi114Q → P: Does not affect expression of the at the cell surface. Cannot bind LPL and chylomicrons. 1 Publication1

Keywords - Diseasei

Hyperlipidemia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000034379823 – 198Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1Add BLAST176
PropeptideiPRO_0000429859199 – 228Removed in mature formCuratedAdd BLAST30

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi63 ↔ 88By similarity
Disulfide bondi66 ↔ 75By similarity
Glycosylationi76N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi81 ↔ 109By similarity
Disulfide bondi113 ↔ 129By similarity
Disulfide bondi130 ↔ 135By similarity
Lipidationi198GPI-anchor amidated glycineCurated1

Post-translational modificationi

Glycosylation of Asn-76 is critical for cell surface localization and the binding of chylomicrons and lipoprotein lipase.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ9D1N2.
PaxDbiQ9D1N2.
PeptideAtlasiQ9D1N2.
PRIDEiQ9D1N2.

PTM databases

PhosphoSitePlusiQ9D1N2.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiENSMUSG00000022579.
CleanExiMM_HBP1.
ExpressionAtlasiQ9D1N2. baseline and differential.
GenevisibleiQ9D1N2. MM.

Interactioni

Subunit structurei

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).By similarity3 Publications

GO - Molecular functioni

  • lipase binding Source: BHF-UCL

Protein-protein interaction databases

IntActiQ9D1N2. 1 interactor.
MINTiMINT-4126642.
STRINGi10090.ENSMUSP00000023243.

Structurei

3D structure databases

ProteinModelPortaliQ9D1N2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 148UPAR/Ly6Sequence analysisAdd BLAST88

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi38 – 42Poly-AspSequence analysis5
Compositional biasi43 – 48Poly-GluSequence analysis6

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J46G. Eukaryota.
ENOG41116TR. LUCA.
GeneTreeiENSGT00390000012601.
HOGENOMiHOG000112872.
InParanoidiQ9D1N2.
OMAiQSTLCNI.
OrthoDBiEOG091G0UW5.
PhylomeDBiQ9D1N2.
TreeFamiTF338440.

Family and domain databases

InterProiView protein in InterPro
IPR018363. CD59_antigen_CS.
IPR016054. LY6_UPA_recep-like.
PfamiView protein in Pfam
PF00021. UPAR_LY6. 1 hit.
PROSITEiView protein in PROSITE
PS00983. LY6_UPAR. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D1N2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALRAVLLI LLLSGQPGSG WAQEDGDADP EPENYNYDDD DDEEEEEETN
60 70 80 90 100
MIPGSRDRAP LQCYFCQVLH SGESCNQTQS CSSSKPFCIT LVSHSGTDKG
110 120 130 140 150
YLTTYSMWCT DTCQPIIKTV GGTQMTQTCC QSTLCNIPPW QNPQVQNPLG
160 170 180 190 200
GRADSPLESG TRHPQGGKFS HPQVVKAAHP QSDGANLPKS GKANQPQGSG
210 220
AGYPSGWTKF GNIALLLSFF TCLWASGA
Length:228
Mass (Da):24,566
Last modified:June 1, 2001 - v1
Checksum:iB2FB456A10865E81
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB095543 mRNA. Translation: BAC23061.1.
AK003305 mRNA. Translation: BAB22704.1.
BC061225 mRNA. Translation: AAH61225.1.
CCDSiCCDS27545.1.
RefSeqiNP_081006.1. NM_026730.1.
UniGeneiMm.46367.

Genome annotation databases

EnsembliENSMUST00000023243; ENSMUSP00000023243; ENSMUSG00000022579.
GeneIDi68453.
UCSCiuc007wgw.1. mouse.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiHDBP1_MOUSE
AccessioniPrimary (citable) accession number: Q9D1N2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: June 1, 2001
Last modified: June 7, 2017
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot