Gpihbp1
entrez
68453
canonical
uniprot
Q9D1N2
canonical
ensembl
ENSMUSG00000022579
resolver
ensp
ENSMUSP00000023243
resolver
ensp
ENSMUSP00000139511
resolver
ensp
ENSMUSP00000139792
resolver
enst
ENSMUST00000023243
resolver
enst
ENSMUST00000189874
resolver
enst
ENSMUST00000189944
resolver
genesymbol
Gpihbp1
resolver
genesymbol_syn
Hbp1
resolver
uniprot
A0A087WNV7
resolver
uniprot
A0A087WPI6
resolver
uniprot_entry
A0A087WNV7_MOUSE
resolver
uniprot_entry
A0A087WPI6_MOUSE
resolver
uniprot_entry
HDBP1_MOUSE
resolver
amino_acid_sequence
MKALRAVLLILLLSGQPGSGWAQEDGDADPEPENYNYDDDDDEEEEEETNMIPGSRDRAPLQCYFCQVLHSGESCNQTQSCSSSKPFCITLVSHSGTDKGYLTTYSMWCTDTCQPIIKTVGGTQMTQTCCQSTLCNIPPWQNPQVQNPLGGRADSPLESGTRHPQGGKFSHPQVVKAAHPQSDGANLPKSGKANQPQGSGAGYPSGWTKFGNIALLLSFFTCLWASGA
uniprot
proteins
function
FUNCTION: Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries (PubMed:20620994). Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries (PubMed:20620994, PubMed:24726386, PubMed:27811232). Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis (PubMed:17403372). Binds chylomicrons and phospholipid particles that contain APOA5 (PubMed:18340083). Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL (PubMed:12496272). {ECO:0000269|PubMed:12496272, ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}.
uniprot
proteins
mass_dalton
24566
uniprot
proteins
mutagenesis
MUTAGEN 24..48; /note="EDGDADPEPENYNYDDDDDEEEEEE->AAGAAAPAPANYNYAAAAAAAAAAA: Nearly abolishes LPL transport to the lumenal surface of endothelial cells."; /evidence="ECO:0000269|PubMed:20620994"; MUTAGEN 88; /note="C->A: Reduced number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 114; /note="Q->P: Loss of interaction with LPL."; /evidence="ECO:0000269|PubMed:19304573
uniprot
proteins
post_translational_modification
PTM: Glycosylation of Asn-76 is critical for cell surface localization. {ECO:0000269|PubMed:18340083}.; PTM: Sulfation of a Tyr in the N-terminal acidic region increases the affinity for LPL. {ECO:0000250|UniProtKB:Q8IV16}.
uniprot
proteins
pubmed
12496272
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17403372
uniprot
proteins
pubmed
17620854
uniprot
proteins
pubmed
18340083
uniprot
proteins
pubmed
19304573
uniprot
proteins
pubmed
20620994
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21844202
uniprot
proteins
pubmed
24726386
uniprot
proteins
pubmed
25387803
uniprot
proteins
pubmed
27811232
uniprot
proteins
sequence_length
228
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}. Basolateral cell membrane {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}. Cell membrane {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}.
uniprot
proteins