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Protein

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1

Gene

GPIHBP1

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

GO - Molecular functioni

  1. chylomicron binding Source: BHF-UCL
  2. high-density lipoprotein particle binding Source: Ensembl
  3. lipase binding Source: BHF-UCL
  4. lipid binding Source: UniProtKB-KW
  5. lipoprotein particle binding Source: UniProtKB
  6. protein transmembrane transporter activity Source: BHF-UCL

GO - Biological processi

  1. cholesterol homeostasis Source: BHF-UCL
  2. intracellular protein transport Source: BHF-UCL
  3. lipid transport Source: Ensembl
  4. positive regulation of chylomicron remnant clearance Source: BHF-UCL
  5. positive regulation of lipoprotein lipase activity Source: BHF-UCL
  6. protein import Source: BHF-UCL
  7. protein localization to cell surface Source: BHF-UCL
  8. protein stabilization Source: BHF-UCL
  9. response to heparin Source: BHF-UCL
  10. transcytosis Source: BHF-UCL
  11. triglyceride homeostasis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Short name:
GPI-HBP1
Short name:
GPI-anchored HDL-binding protein 1
Alternative name(s):
High density lipoprotein-binding protein 1
Gene namesi
Name:GPIHBP1
Synonyms:HBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:24945. GPIHBP1.

Subcellular locationi

  1. Apical cell membrane By similarity; Lipid-anchorGPI-anchor By similarity
  2. Basolateral cell membrane By similarity; Lipid-anchorGPI-anchor By similarity
  3. Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: BHF-UCL
  2. apical plasma membrane Source: BHF-UCL
  3. basolateral plasma membrane Source: BHF-UCL
  4. external side of plasma membrane Source: BHF-UCL
  5. high-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, HDL, Membrane

Pathology & Biotechi

Involvement in diseasei

Hyperlipoproteinemia 1D (HLPP1D)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive disorder characterized by hyperlipoproteinemia, decreased plasma LPL levels in some patients, high plasma triglyceride levels, and refractory fasting chylomicronemia.

See also OMIM:615947
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651C → S in HLPP1D; does not affect protein expression at the cell surface; cannot bind LPL. 1 Publication
VAR_071881
Natural varianti68 – 681C → G in HLPP1D; does not affect protein expression at the cell surface; cannot bind LPL. 1 Publication
VAR_071882
Natural varianti89 – 891C → F in HLPP1D; drastically affects LPL-binding. 1 Publication
VAR_071883
Natural varianti115 – 1151Q → P in HLPP1D; a patient with chylomicronemia; does not affect protein expression at the cell surface; cannot bind LPL or chylomicrons. 1 Publication
VAR_058086
Natural varianti175 – 1751G → R in HLPP1D; affects protein expression at the cell surface; reduced LPL binding. 1 Publication
VAR_071884

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615947. phenotype.
Orphaneti411. Hyperlipoproteinemia type 1.
70470. Hyperlipoproteinemia type 5.
PharmGKBiPA162390135.

Polymorphism and mutation databases

BioMutaiGPIHBP1.
DMDMi74728020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 151131Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1PRO_0000318208Add
BLAST
Propeptidei152 – 18433Removed in mature formCuratedPRO_0000429858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 89By similarity
Disulfide bondi68 ↔ 77By similarity
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi83 ↔ 110By similarity
Disulfide bondi114 ↔ 130By similarity
Disulfide bondi131 ↔ 136By similarity
Lipidationi151 – 1511GPI-anchor amidated glycineCurated

Post-translational modificationi

Glycosylation of Asn-78 is critical for cell surface localization and the binding of chylomicrons and lipoprotein lipase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiQ8IV16.

Expressioni

Gene expression databases

BgeeiQ8IV16.
CleanExiHS_GPIHBP1.
HS_HBP1.
GenevestigatoriQ8IV16.

Organism-specific databases

HPAiHPA066302.

Interactioni

Subunit structurei

Binds with high affinity to high-density lipoprotein (HDL) (By similarity). Binds to lipoprotein lipase (LPL), chylomicrons and APOA5.By similarity

Protein-protein interaction databases

IntActiQ8IV16. 1 interaction.
STRINGi9606.ENSP00000329266.

Structurei

3D structure databases

ProteinModelPortaliQ8IV16.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 14886UPAR/Ly6Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi25 – 317Poly-Glu
Compositional biasi40 – 5011Poly-GluAdd
BLAST

Sequence similaritiesi

Contains 1 UPAR/Ly6 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42849.
HOGENOMiHOG000112872.
InParanoidiQ8IV16.
OMAiIAHGNTE.
OrthoDBiEOG7M6D9C.
PhylomeDBiQ8IV16.
TreeFamiTF338440.

Family and domain databases

InterProiIPR016054. LY6_UPA_recep-like.
IPR001526. LY6_UPAR.
[Graphical view]
PfamiPF00021. UPAR_LY6. 1 hit.
[Graphical view]
SMARTiSM00134. LU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8IV16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALGAVLLA LLLCGRPGRG QTQQEEEEED EDHGPDDYDE EDEDEVEEEE
60 70 80 90 100
TNRLPGGRSR VLLRCYTCKS LPRDERCNLT QNCSHGQTCT TLIAHGNTES
110 120 130 140 150
GLLTTHSTWC TDSCQPITKT VEGTQVTMTC CQSSLCNVPP WQSSRVQDPT
160 170 180
GKGAGGPRGS SETVGAALLL NLLAGLGAMG ARRP
Length:184
Mass (Da):19,806
Last modified:December 7, 2004 - v2
Checksum:i89FF61B08A008C70
GO

Polymorphismi

The missense variant Arg-56 may be associated with severe hypertriglyceridemia and chylomicronemia.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141C → F Polymorphism; may potentiate the LPL-binding defect of F-89 and likely to contribute to the severe phenotype of this mutation. 2 Publications
Corresponds to variant rs11538389 [ dbSNP | Ensembl ].
VAR_044503
Natural varianti56 – 561G → R Polymorphism; no discernible effect on the binding of LPL, chylomicrons or APOA5. 2 Publications
VAR_044504
Natural varianti65 – 651C → S in HLPP1D; does not affect protein expression at the cell surface; cannot bind LPL. 1 Publication
VAR_071881
Natural varianti68 – 681C → G in HLPP1D; does not affect protein expression at the cell surface; cannot bind LPL. 1 Publication
VAR_071882
Natural varianti89 – 891C → F in HLPP1D; drastically affects LPL-binding. 1 Publication
VAR_071883
Natural varianti115 – 1151Q → P in HLPP1D; a patient with chylomicronemia; does not affect protein expression at the cell surface; cannot bind LPL or chylomicrons. 1 Publication
VAR_058086
Natural varianti175 – 1751G → R in HLPP1D; affects protein expression at the cell surface; reduced LPL binding. 1 Publication
VAR_071884

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY245915 mRNA. Translation: AAO86519.1.
CH471162 Genomic DNA. Translation: EAW82276.1.
BC035810 mRNA. Translation: AAH35810.2.
BC063857 mRNA. Translation: AAH63857.1.
CCDSiCCDS34954.1.
RefSeqiNP_001288701.1. NM_001301772.1.
NP_835466.2. NM_178172.5.
UniGeneiHs.426410.

Genome annotation databases

EnsembliENST00000622500; ENSP00000480053; ENSG00000277494.
GeneIDi338328.
KEGGihsa:338328.
UCSCiuc003yxu.2. human.

Polymorphism and mutation databases

BioMutaiGPIHBP1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY245915 mRNA. Translation: AAO86519.1.
CH471162 Genomic DNA. Translation: EAW82276.1.
BC035810 mRNA. Translation: AAH35810.2.
BC063857 mRNA. Translation: AAH63857.1.
CCDSiCCDS34954.1.
RefSeqiNP_001288701.1. NM_001301772.1.
NP_835466.2. NM_178172.5.
UniGeneiHs.426410.

3D structure databases

ProteinModelPortaliQ8IV16.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8IV16. 1 interaction.
STRINGi9606.ENSP00000329266.

Polymorphism and mutation databases

BioMutaiGPIHBP1.
DMDMi74728020.

Proteomic databases

PRIDEiQ8IV16.

Protocols and materials databases

DNASUi338328.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000622500; ENSP00000480053; ENSG00000277494.
GeneIDi338328.
KEGGihsa:338328.
UCSCiuc003yxu.2. human.

Organism-specific databases

CTDi338328.
GeneCardsiGC08P144295.
HGNCiHGNC:24945. GPIHBP1.
HPAiHPA066302.
MIMi612757. gene.
615947. phenotype.
neXtProtiNX_Q8IV16.
Orphaneti411. Hyperlipoproteinemia type 1.
70470. Hyperlipoproteinemia type 5.
PharmGKBiPA162390135.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42849.
HOGENOMiHOG000112872.
InParanoidiQ8IV16.
OMAiIAHGNTE.
OrthoDBiEOG7M6D9C.
PhylomeDBiQ8IV16.
TreeFamiTF338440.

Miscellaneous databases

GenomeRNAii338328.
NextBioi96941.
PROiQ8IV16.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IV16.
CleanExiHS_GPIHBP1.
HS_HBP1.
GenevestigatoriQ8IV16.

Family and domain databases

InterProiIPR016054. LY6_UPA_recep-like.
IPR001526. LY6_UPAR.
[Graphical view]
PfamiPF00021. UPAR_LY6. 1 hit.
[Graphical view]
SMARTiSM00134. LU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of human HBP1 gene."
    Shan Y.X., Yu L.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-14.
    Tissue: Brain and PNS.
  4. "Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution."
    Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A., Fong L.G., Young S.G.
    Biochim. Biophys. Acta 1771:1464-1468(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APOA5 AND LPL, CHARACTERIZATION OF VARIANT ARG-56.
  5. Cited for: REVIEW.
  6. "Homozygous missense mutation (G56R) in glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPI-HBP1) in two siblings with fasting chylomicronemia (MIM 144650)."
    Wang J., Hegele R.A.
    Lipids Health Dis. 6:23-23(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-56.
  7. Cited for: VARIANT HLPP1D PRO-115, CHARACTERIZATION OF VARIANT HLPP1D PRO-115.
  8. Cited for: VARIANTS HLPP1D SER-65 AND GLY-68, CHARACTERIZATION OF VARIANTS HLPP1D SER-65 AND GLY-68.
  9. "GPIHBP1 C89F neomutation and hydrophobic C-terminal domain G175R mutation in two pedigrees with severe hyperchylomicronemia."
    Charriere S., Peretti N., Bernard S., Di Filippo M., Sassolas A., Merlin M., Delay M., Debard C., Lefai E., Lachaux A., Moulin P., Marcais C.
    J. Clin. Endocrinol. Metab. 96:E1675-E1679(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HLPP1D PHE-89 AND ARG-175, VARIANT PHE-14, CHARACTERIZATION OF VARIANTS HLPP1D PHE-89 AND ARG-175, CHARACTERIZATION OF VARIANT PHE-14.

Entry informationi

Entry nameiHDBP1_HUMAN
AccessioniPrimary (citable) accession number: Q8IV16
Secondary accession number(s): Q6P3T2, Q86W15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 7, 2004
Last modified: April 29, 2015
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.