HDBP1_HUMAN
ID HDBP1_HUMAN Reviewed; 184 AA.
AC Q8IV16; Q6P3T2; Q86W15;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1;
DE Short=GPI-HBP1;
DE Short=GPI-anchored HDL-binding protein 1;
DE AltName: Full=High density lipoprotein-binding protein 1;
DE Flags: Precursor;
GN Name=GPIHBP1 {ECO:0000312|HGNC:HGNC:24945}; Synonyms=HBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-14.
RA Shan Y.X., Yu L.;
RT "Isolation and characterization of human HBP1 gene.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT CYS-14.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-14.
RC TISSUE=Brain, and PNS;
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 [4]
RP INTERACTION WITH APOA5 AND LPL, AND CHARACTERIZATION OF VARIANT ARG-56.
RX PubMed=17997385; DOI=10.1016/j.bbalip.2007.10.005;
RA Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A.,
RA Fong L.G., Young S.G.;
RT "Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1
RT containing a G56R amino acid substitution.";
RL Biochim. Biophys. Acta 1771:1464-1468(2007).
RN [5]
RP REVIEW.
RX PubMed=21844202; DOI=10.1194/jlr.r018689;
RA Young S.G., Davies B.S., Voss C.V., Gin P., Weinstein M.M., Tontonoz P.,
RA Reue K., Bensadoun A., Fong L.G., Beigneux A.P.;
RT "GPIHBP1, an endothelial cell transporter for lipoprotein lipase.";
RL J. Lipid Res. 52:1869-1884(2011).
RN [6]
RP DOMAIN, INTERACTION WITH LPL, AND MUTAGENESIS OF TRP-109.
RX PubMed=26725083; DOI=10.7554/elife.12095;
RA Mysling S., Kristensen K.K., Larsson M., Beigneux A.P., Gaardsvoll H.,
RA Fong L.G., Bensadouen A., Joergensen T.J., Young S.G., Ploug M.;
RT "The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes
RT lipoprotein lipase activity by preventing unfolding of its catalytic
RT domain.";
RL Elife 5:E12095-E12095(2016).
RN [7]
RP FUNCTION, AND INTERACTION WITH LPL.
RX PubMed=27929370; DOI=10.7554/elife.20958;
RA Mysling S., Kristensen K.K., Larsson M., Kovrov O., Bensadouen A.,
RA Joergensen T.J., Olivecrona G., Young S.G., Ploug M.;
RT "The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase
RT domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1
RT counteracts this unfolding.";
RL Elife 5:0-0(2016).
RN [8]
RP FUNCTION, INTERACTION WITH LPL, AND MUTAGENESIS OF TRP-109.
RX PubMed=27811232; DOI=10.1194/jlr.m072520;
RA Allan C.M., Larsson M., Jung R.S., Ploug M., Bensadoun A., Beigneux A.P.,
RA Fong L.G., Young S.G.;
RT "Mobility of 'HSPG-bound' LPL explains how LPL is able to reach GPIHBP1 on
RT capillaries.";
RL J. Lipid Res. 58:216-225(2017).
RN [9]
RP FUNCTION, INTERACTION WITH LPL, SULFATION AT TYR-38, GLYCOSYLATION AT
RP ASN-78, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF TYR-38.
RX PubMed=29899144; DOI=10.1073/pnas.1806774115;
RA Kristensen K.K., Midtgaard S.R., Mysling S., Kovrov O., Hansen L.B.,
RA Skar-Gislinge N., Beigneux A.P., Kragelund B.B., Olivecrona G., Young S.G.,
RA Joergensen T.J.D., Fong L.G., Ploug M.;
RT "A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine
RT regulates lipoprotein lipase.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E6020-E6029(2018).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 21-151 IN COMPLEX WITH LPL,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-78, AND MUTAGENESIS OF TRP-109.
RX PubMed=30559189; DOI=10.1073/pnas.1817984116;
RA Birrane G., Beigneux A.P., Dwyer B., Strack-Logue B., Kristensen K.K.,
RA Francone O.L., Fong L.G., Mertens H.D.T., Pan C.Q., Ploug M., Young S.G.,
RA Meiyappan M.;
RT "Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma
RT triglyceride hydrolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:1723-1732(2019).
RN [11]
RP VARIANT ARG-56.
RX PubMed=17883852; DOI=10.1186/1476-511x-6-23;
RA Wang J., Hegele R.A.;
RT "Homozygous missense mutation (G56R) in glycosylphosphatidylinositol-
RT anchored high-density lipoprotein-binding protein 1 (GPI-HBP1) in two
RT siblings with fasting chylomicronemia (MIM 144650).";
RL Lipids Health Dis. 6:23-23(2007).
RN [12]
RP VARIANT HLPP1D PRO-115, CHARACTERIZATION OF VARIANT HLPP1D PRO-115,
RP INTERACTION WITH LPL, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19304573; DOI=10.1161/atvbaha.109.186577;
RA Beigneux A.P., Franssen R., Bensadoun A., Gin P., Melford K., Peter J.,
RA Walzem R.L., Weinstein M.M., Davies B.S.J., Kuivenhoven J.A.,
RA Kastelein J.J.P., Fong L.G., Dallinga-Thie G.M., Young S.G.;
RT "Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein
RT lipase.";
RL Arterioscler. Thromb. Vasc. Biol. 29:956-962(2009).
RN [13]
RP VARIANTS HLPP1D SER-65 AND GLY-68, AND CHARACTERIZATION OF VARIANTS HLPP1D
RP SER-65 AND GLY-68.
RX PubMed=20026666; DOI=10.1194/jlr.m002717;
RA Olivecrona G., Ehrenborg E., Semb H., Makoveichuk E., Lindberg A.,
RA Hayden M.R., Gin P., Davies B.S., Weinstein M.M., Fong L.G., Beigneux A.P.,
RA Young S.G., Olivecrona T., Hernell O.;
RT "Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial
RT chylomicronemia.";
RL J. Lipid Res. 51:1535-1545(2010).
RN [14]
RP VARIANTS HLPP1D PHE-89 AND ARG-175, VARIANT CYS-14, CHARACTERIZATION OF
RP VARIANTS HLPP1D PHE-89 AND ARG-175, AND CHARACTERIZATION OF VARIANT CYS-14.
RX PubMed=21816778; DOI=10.1210/jc.2011-1444;
RA Charriere S., Peretti N., Bernard S., Di Filippo M., Sassolas A.,
RA Merlin M., Delay M., Debard C., Lefai E., Lachaux A., Moulin P.,
RA Marcais C.;
RT "GPIHBP1 C89F neomutation and hydrophobic C-terminal domain G175R mutation
RT in two pedigrees with severe hyperchylomicronemia.";
RL J. Clin. Endocrinol. Metab. 96:E1675-E1679(2011).
RN [15]
RP VARIANT HLPP1D TYR-68, AND FUNCTION.
RX PubMed=21314738; DOI=10.1111/j.1365-2796.2011.02361.x;
RA Coca-Prieto I., Kroupa O., Gonzalez-Santos P., Magne J., Olivecrona G.,
RA Ehrenborg E., Valdivielso P.;
RT "Childhood-onset chylomicronaemia with reduced plasma lipoprotein lipase
RT activity and mass: identification of a novel GPIHBP1 mutation.";
RL J. Intern. Med. 270:224-228(2011).
RN [16]
RP VARIANTS HLPP1D TYR-65; ARG-108; PRO-115 AND PHE-144.
RX PubMed=22239554; DOI=10.1111/j.1365-2796.2012.02516.x;
RA Surendran R.P., Visser M.E., Heemelaar S., Wang J., Peter J.,
RA Defesche J.C., Kuivenhoven J.A., Hosseini M., Peterfy M., Kastelein J.J.,
RA Johansen C.T., Hegele R.A., Stroes E.S., Dallinga-Thie G.M.;
RT "Mutations in LPL, APOC2, APOA5, GPIHBP1 and LMF1 in patients with severe
RT hypertriglyceridaemia.";
RL J. Intern. Med. 272:185-196(2012).
RN [17]
RP VARIANT CYS-14, VARIANT HLPP1D ARG-68, CHARACTERIZATION OF VARIANT CYS-14,
RP AND CHARACTERIZATION OF VARIANT HLPP1D ARG-68.
RX PubMed=23831619; DOI=10.5551/jat.18861;
RA Yamamoto H., Onishi M., Miyamoto N., Oki R., Ueda H., Ishigami M.,
RA Hiraoka H., Matsuzawa Y., Kihara S.;
RT "Novel combined GPIHBP1 mutations in a patient with hypertriglyceridemia
RT associated with CAD.";
RL J. Atheroscler. Thromb. 20:777-784(2013).
RN [18]
RP CHARACTERIZATION OF VARIANTS HLPP1D SER-65; TYR-65; ARG-68; GLY-68; TYR-68;
RP PHE-89; ARG-108 AND PRO-115, SUBUNIT, INTERACTION WITH LPL, AND MUTAGENESIS
RP OF TYR-66; LEU-71; THR-91; LEU-92; ILE-93; GLY-101; THR-104; THR-105;
RP HIS-106; SER-107; THR-108; TRP-109; GLN-115 AND VAL-126.
RX PubMed=25387803; DOI=10.1161/circresaha.116.305085;
RA Beigneux A.P., Fong L.G., Bensadoun A., Davies B.S., Oberer M.,
RA Gaardsvoll H., Ploug M., Young S.G.;
RT "GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and
RT thereby prevent lipoprotein lipase binding.";
RL Circ. Res. 116:624-632(2015).
RN [19]
RP VARIANT HLPP1D ARG-83.
RX PubMed=27578123; DOI=10.1016/j.jacl.2016.03.009;
RA Rabacchi C., D'Addato S., Palmisano S., Lucchi T., Bertolini S.,
RA Calandra S., Tarugi P.;
RT "Clinical and genetic features of 3 patients with familial chylomicronemia
RT due to mutations in GPIHBP1 gene.";
RL J. Clin. Lipidol. 10:915-921(2016).
CC -!- FUNCTION: Mediates the transport of lipoprotein lipase LPL from the
CC basolateral to the apical surface of endothelial cells in capillaries
CC (By similarity). Anchors LPL on the surface of endothelial cells in the
CC lumen of blood capillaries (By similarity). Protects LPL against loss
CC of activity, and against ANGPTL4-mediated unfolding (PubMed:27929370,
CC PubMed:29899144). Thereby, plays an important role in lipolytic
CC processing of chylomicrons by LPL, triglyceride metabolism and lipid
CC homeostasis (PubMed:19304573, PubMed:21314738). Binds chylomicrons and
CC phospholipid particles that contain APOA5 (PubMed:17997385,
CC PubMed:19304573). Binds high-density lipoprotein (HDL) and plays a role
CC in the uptake of lipids from HDL (By similarity).
CC {ECO:0000250|UniProtKB:Q9D1N2, ECO:0000269|PubMed:17997385,
CC ECO:0000269|PubMed:19304573, ECO:0000269|PubMed:21314738,
CC ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144}.
CC -!- SUBUNIT: Mostly monomer, but also homodimer and homooligomer
CC (PubMed:25387803). Interacts with lipoprotein lipase (LPL) with 1:1
CC stoichiometry (PubMed:17997385, PubMed:26725083, PubMed:27929370,
CC PubMed:29899144, PubMed:30559189, PubMed:19304573, PubMed:25387803).
CC Interacts with high affinity with high-density lipoprotein (HDL) (By
CC similarity). Interacts with chylomicrons. Interacts with APOA5
CC (PubMed:17997385). {ECO:0000250|UniProtKB:Q9D1N2,
CC ECO:0000269|PubMed:17997385, ECO:0000269|PubMed:19304573,
CC ECO:0000269|PubMed:25387803, ECO:0000269|PubMed:26725083,
CC ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144,
CC ECO:0000269|PubMed:30559189}.
CC -!- INTERACTION:
CC Q8IV16; P06858: LPL; NbExp=7; IntAct=EBI-9080234, EBI-715909;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q9D1N2}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q9D1N2}. Cell membrane
CC {ECO:0000269|PubMed:19304573}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q9D1N2}.
CC -!- DOMAIN: The N-terminal acidic region is intrinsically disordered
CC (PubMed:26725083). This region contributes to LPL binding, stabilizes
CC LPL and protects LPL against loss of activity (PubMed:26725083,
CC PubMed:27929370). {ECO:0000269|PubMed:26725083,
CC ECO:0000269|PubMed:27929370}.
CC -!- PTM: Glycosylation of Asn-78 is critical for cell surface localization.
CC {ECO:0000250|UniProtKB:Q9D1N2}.
CC -!- PTM: Sulfation of a Tyr in the N-terminal acidic region increases the
CC affinity for LPL. {ECO:0000269|PubMed:29899144}.
CC -!- POLYMORPHISM: The missense variant Arg-56 may be associated with severe
CC hypertriglyceridemia and chylomicronemia.
CC -!- DISEASE: Hyperlipoproteinemia 1D (HLPP1D) [MIM:615947]: An autosomal
CC recessive disorder characterized by hyperlipoproteinemia, decreased
CC plasma LPL levels in some patients, high plasma triglyceride levels,
CC and refractory fasting chylomicronemia. {ECO:0000269|PubMed:19304573,
CC ECO:0000269|PubMed:20026666, ECO:0000269|PubMed:21314738,
CC ECO:0000269|PubMed:21816778, ECO:0000269|PubMed:22239554,
CC ECO:0000269|PubMed:23831619, ECO:0000269|PubMed:25387803,
CC ECO:0000269|PubMed:27578123}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AY245915; AAO86519.1; -; mRNA.
DR EMBL; CH471162; EAW82276.1; -; Genomic_DNA.
DR EMBL; BC035810; AAH35810.2; -; mRNA.
DR EMBL; BC063857; AAH63857.1; -; mRNA.
DR CCDS; CCDS34954.1; -.
DR RefSeq; NP_001288701.1; NM_001301772.1.
DR RefSeq; NP_835466.2; NM_178172.5.
DR PDB; 6E7K; X-ray; 2.80 A; C/D=21-151.
DR PDB; 6OAU; X-ray; 2.48 A; C/D=21-151.
DR PDB; 6OAZ; X-ray; 3.04 A; E/F/G/H=21-151.
DR PDB; 6OB0; X-ray; 2.81 A; E/F/G/H=21-151.
DR PDBsum; 6E7K; -.
DR PDBsum; 6OAU; -.
DR PDBsum; 6OAZ; -.
DR PDBsum; 6OB0; -.
DR AlphaFoldDB; Q8IV16; -.
DR SASBDB; Q8IV16; -.
DR BioGRID; 130712; 141.
DR ComplexPortal; CPX-6091; LPL-GPIHBP1 triglyceride-rich lipoprotein processing complex.
DR IntAct; Q8IV16; 2.
DR STRING; 9606.ENSP00000480053; -.
DR GlyGen; Q8IV16; 1 site.
DR iPTMnet; Q8IV16; -.
DR PhosphoSitePlus; Q8IV16; -.
DR BioMuta; GPIHBP1; -.
DR DMDM; 74728020; -.
DR MassIVE; Q8IV16; -.
DR PaxDb; Q8IV16; -.
DR PeptideAtlas; Q8IV16; -.
DR PRIDE; Q8IV16; -.
DR Antibodypedia; 75628; 198 antibodies from 18 providers.
DR DNASU; 338328; -.
DR Ensembl; ENST00000622500.2; ENSP00000480053.1; ENSG00000277494.2.
DR GeneID; 338328; -.
DR KEGG; hsa:338328; -.
DR MANE-Select; ENST00000622500.2; ENSP00000480053.1; NM_178172.6; NP_835466.2.
DR UCSC; uc033cbs.1; human.
DR CTD; 338328; -.
DR DisGeNET; 338328; -.
DR GeneCards; GPIHBP1; -.
DR HGNC; HGNC:24945; GPIHBP1.
DR HPA; ENSG00000277494; Tissue enhanced (adipose tissue, brain, breast).
DR MalaCards; GPIHBP1; -.
DR MIM; 612757; gene.
DR MIM; 615947; phenotype.
DR neXtProt; NX_Q8IV16; -.
DR OpenTargets; ENSG00000277494; -.
DR Orphanet; 535458; Familial GPIHBP1 deficiency.
DR PharmGKB; PA162390135; -.
DR VEuPathDB; HostDB:ENSG00000277494; -.
DR eggNOG; ENOG502SVBD; Eukaryota.
DR GeneTree; ENSGT00940000153378; -.
DR HOGENOM; CLU_102231_0_0_1; -.
DR InParanoid; Q8IV16; -.
DR OrthoDB; 1415737at2759; -.
DR PhylomeDB; Q8IV16; -.
DR TreeFam; TF338440; -.
DR PathwayCommons; Q8IV16; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-HSA-8963901; Chylomicron remodeling.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; Q8IV16; -.
DR BioGRID-ORCS; 338328; 10 hits in 1062 CRISPR screens.
DR ChiTaRS; GPIHBP1; human.
DR GenomeRNAi; 338328; -.
DR Pharos; Q8IV16; Tbio.
DR PRO; PR:Q8IV16; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8IV16; protein.
DR Bgee; ENSG00000277494; Expressed in apex of heart and 130 other tissues.
DR Genevisible; Q8IV16; HS.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031225; C:anchored component of membrane; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; ISS:BHF-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:BHF-UCL.
DR GO; GO:1902494; C:catalytic complex; IPI:ComplexPortal.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0035478; F:chylomicron binding; IDA:BHF-UCL.
DR GO; GO:0035473; F:lipase binding; IPI:BHF-UCL.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:ARUK-UCL.
DR GO; GO:0071813; F:lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0140318; F:protein transporter activity; ISS:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0006886; P:intracellular protein transport; ISS:BHF-UCL.
DR GO; GO:0090321; P:positive regulation of chylomicron remnant clearance; ISS:BHF-UCL.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:ARUK-UCL.
DR GO; GO:0017038; P:protein import; ISS:BHF-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:ARUK-UCL.
DR GO; GO:0071503; P:response to heparin; IMP:BHF-UCL.
DR GO; GO:0045056; P:transcytosis; ISS:BHF-UCL.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:ComplexPortal.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
DR CDD; cd00117; LU; 1.
DR DisProt; DP01327; -.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR Pfam; PF00021; UPAR_LY6; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disease variant; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipid-binding; Lipoprotein; Membrane; Reference proteome;
KW Signal; Sulfation; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..151
FT /note="Glycosylphosphatidylinositol-anchored high density
FT lipoprotein-binding protein 1"
FT /id="PRO_0000318208"
FT PROPEP 152..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000429858"
FT DOMAIN 63..148
FT /note="UPAR/Ly6"
FT REGION 21..35
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:26725083"
FT REGION 27..50
FT /note="Important for LPL transport to the lumenal surface
FT of endothelial cells"
FT /evidence="ECO:0000250|UniProtKB:Q9D1N2"
FT REGION 103..109
FT /note="Important for interaction with LPL"
FT /evidence="ECO:0000269|PubMed:26725083,
FT ECO:0000269|PubMed:30559189"
FT COMPBIAS 24..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:29899144"
FT LIPID 151
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1N2"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29899144,
FT ECO:0000269|PubMed:30559189, ECO:0007744|PDB:6E7K"
FT DISULFID 65..89
FT /evidence="ECO:0000269|PubMed:30559189,
FT ECO:0007744|PDB:6E7K"
FT DISULFID 68..77
FT /evidence="ECO:0000269|PubMed:30559189,
FT ECO:0007744|PDB:6E7K"
FT DISULFID 83..110
FT /evidence="ECO:0000269|PubMed:30559189,
FT ECO:0007744|PDB:6E7K"
FT DISULFID 114..130
FT /evidence="ECO:0000269|PubMed:30559189,
FT ECO:0007744|PDB:6E7K"
FT DISULFID 131..136
FT /evidence="ECO:0000269|PubMed:30559189,
FT ECO:0007744|PDB:6E7K"
FT VARIANT 14
FT /note="F -> C (it may act as a disease modifier preserving
FT from severe HLPP1D when associated with R-68 or F-89;
FT results in increased GPIHBP1 expression at the cell
FT surface; does not affect interaction with LPL when
FT associated in cis with R-68 in one individual;
FT dbSNP:rs11538389)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:21816778, ECO:0000269|PubMed:23831619,
FT ECO:0000269|Ref.1, ECO:0000269|Ref.2"
FT /id="VAR_044503"
FT VARIANT 56
FT /note="G -> R (no discernible effect on interaction with
FT LPL, chylomicrons or APOA5; dbSNP:rs587777636)"
FT /evidence="ECO:0000269|PubMed:17883852,
FT ECO:0000269|PubMed:17997385"
FT /id="VAR_044504"
FT VARIANT 65
FT /note="C -> S (in HLPP1D; does not affect protein
FT expression at the cell surface; does not interact with LPL;
FT promotes formation of dimers and oligomers severely
FT reducing number of monomers; dbSNP:rs587777638)"
FT /evidence="ECO:0000269|PubMed:20026666,
FT ECO:0000269|PubMed:25387803"
FT /id="VAR_071881"
FT VARIANT 65
FT /note="C -> Y (in HLPP1D; does not interact with LPL;
FT promotes formation of dimers and oligomers severely
FT reducing number of monomers; dbSNP:rs587777638)"
FT /evidence="ECO:0000269|PubMed:22239554,
FT ECO:0000269|PubMed:25387803"
FT /id="VAR_077634"
FT VARIANT 68
FT /note="C -> G (in HLPP1D; does not affect protein
FT expression at the cell surface; does not interact with LPL;
FT promotes formation of dimers and oligomers reducing number
FT of monomers; dbSNP:rs587777639)"
FT /evidence="ECO:0000269|PubMed:20026666,
FT ECO:0000269|PubMed:25387803"
FT /id="VAR_071882"
FT VARIANT 68
FT /note="C -> R (in HLPP1D; unknown pathological
FT significance; results in decreased GPIHBP1 expression;
FT promotes formation of dimers and oligomers severely
FT reducing number of monomers; does not affect interaction
FT with LPL when associated in cis with F-14 in one
FT individual; dbSNP:rs587777639)"
FT /evidence="ECO:0000269|PubMed:23831619,
FT ECO:0000269|PubMed:25387803"
FT /id="VAR_077635"
FT VARIANT 68
FT /note="C -> Y (in HLPP1D; does not interact with LPL;
FT promotes formation of dimers and oligomers severely
FT reducing number of monomers)"
FT /evidence="ECO:0000269|PubMed:21314738,
FT ECO:0000269|PubMed:25387803"
FT /id="VAR_077636"
FT VARIANT 83
FT /note="C -> R (in HLPP1D)"
FT /evidence="ECO:0000269|PubMed:27578123"
FT /id="VAR_077637"
FT VARIANT 89
FT /note="C -> F (in HLPP1D; drastically affects interaction
FT with LPL; promotes formation of dimers and oligomers
FT reducing number of monomers; dbSNP:rs587777640)"
FT /evidence="ECO:0000269|PubMed:21816778,
FT ECO:0000269|PubMed:25387803"
FT /id="VAR_071883"
FT VARIANT 108
FT /note="T -> R (in HLPP1D; does not interact with LPL;
FT promotes formation of dimers and oligomers reducing number
FT of monomers)"
FT /evidence="ECO:0000269|PubMed:22239554,
FT ECO:0000269|PubMed:25387803"
FT /id="VAR_077638"
FT VARIANT 115
FT /note="Q -> P (in HLPP1D; a patient with chylomicronemia;
FT no effect on protein expression at the cell surface; loss
FT of interaction with LPL; loss of interaction with
FT chylomicrons; promotes formation of dimers and oligomers
FT reducing number of monomers; dbSNP:rs587777637)"
FT /evidence="ECO:0000269|PubMed:19304573,
FT ECO:0000269|PubMed:22239554, ECO:0000269|PubMed:25387803"
FT /id="VAR_058086"
FT VARIANT 144
FT /note="S -> F (in HLPP1D; dbSNP:rs78367243)"
FT /evidence="ECO:0000269|PubMed:22239554"
FT /id="VAR_077639"
FT VARIANT 175
FT /note="G -> R (in HLPP1D; affects protein expression at the
FT cell surface; reduces interaction with LPL;
FT dbSNP:rs145844329)"
FT /evidence="ECO:0000269|PubMed:21816778"
FT /id="VAR_071884"
FT MUTAGEN 38
FT /note="Y->F: Loss of sulfotyrosine formation."
FT /evidence="ECO:0000269|PubMed:29899144"
FT MUTAGEN 66
FT /note="Y->A: Promotes formation of dimers and oligomers
FT reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 71
FT /note="L->A: Promotes formation of dimers and oligomers
FT reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 91
FT /note="T->A: Promotes formation of dimers and oligomers
FT reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 92
FT /note="L->A: Only slightly increased formation of dimers
FT and oligomers. No effect on number of monomers. Loss of LPL
FT interaction."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 93
FT /note="I->A: Promotes formation of dimers and oligomers
FT reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 101
FT /note="G->S: Promotes formation of dimers and oligomers
FT reducing number of monomers. Retained some interaction with
FT LPL."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 104
FT /note="T->A: Promotes formation of dimers and oligomers
FT reducing number of monomers. Retained some interaction with
FT LPL."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 105
FT /note="T->A: Promotes formation of dimers and oligomers
FT reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 106
FT /note="H->L: Promotes formation of dimers and oligomers
FT severely reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 107
FT /note="S->A: Promotes formation of dimers and oligomers
FT reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 108
FT /note="T->A: Retained some interaction with LPL. No effect
FT on number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 109
FT /note="W->C,P,T: Promotes formation of dimers and oligomers
FT reducing number of monomers. Loss of LPL interaction."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 109
FT /note="W->S,Y,H,A,F: Loss of interaction with LPL. Only
FT slightly increased formation of dimers and oligomers. No
FT effect on number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803,
FT ECO:0000269|PubMed:26725083, ECO:0000269|PubMed:27811232,
FT ECO:0000269|PubMed:30559189"
FT MUTAGEN 115
FT /note="Q->K: No effect on number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 126
FT /note="V->A: Promotes formation of dimers and oligomers
FT reducing number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6OAU"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:6OAU"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6OAU"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:6OAU"
FT STRAND 101..113
FT /evidence="ECO:0007829|PDB:6OAU"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:6OAU"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:6OAU"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6OAU"
SQ SEQUENCE 184 AA; 19850 MW; 8F22D5A4D9886D31 CRC64;
MKALGAVLLA LLLFGRPGRG QTQQEEEEED EDHGPDDYDE EDEDEVEEEE TNRLPGGRSR
VLLRCYTCKS LPRDERCNLT QNCSHGQTCT TLIAHGNTES GLLTTHSTWC TDSCQPITKT
VEGTQVTMTC CQSSLCNVPP WQSSRVQDPT GKGAGGPRGS SETVGAALLL NLLAGLGAMG
ARRP
