HDBP1_MOUSE
ID HDBP1_MOUSE Reviewed; 228 AA.
AC Q9D1N2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 {ECO:0000303|PubMed:12496272};
DE Short=GPI-HBP1 {ECO:0000303|PubMed:12496272};
DE Short=GPI-anchored HDL-binding protein 1 {ECO:0000303|PubMed:12496272};
DE AltName: Full=High density lipoprotein-binding protein 1 {ECO:0000303|PubMed:12496272};
DE Flags: Precursor;
GN Name=Gpihbp1 {ECO:0000312|MGI:MGI:1915703};
GN Synonyms=Hbp1 {ECO:0000312|EMBL:BAC23061.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC23061.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HDL-BINDING, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND GPI-ANCHOR AT GLY-198.
RC TISSUE=Liver {ECO:0000269|PubMed:12496272};
RX PubMed=12496272; DOI=10.1074/jbc.m211932200;
RA Ioka R.X., Kang M.-J., Kamiyama S., Kim D.-H., Magoori K., Kamataki A.,
RA Ito Y., Takei Y.A., Sasaki M., Suzuki T., Sasano H., Takahashi S.,
RA Sakai J., Fujino T., Yamamoto T.T.;
RT "Expression cloning and characterization of a novel
RT glycosylphosphatidylinositol-anchored high density lipoprotein-binding
RT protein, GPI-HBP1.";
RL J. Biol. Chem. 278:7344-7349(2003).
RN [2] {ECO:0000312|EMBL:BAB22704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22704.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB22704.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH61225.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH LPL, SUBCELLULAR LOCATION, SUBUNIT, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY FASTING.
RX PubMed=17403372; DOI=10.1016/j.cmet.2007.02.002;
RA Beigneux A.P., Davies B.S.J., Gin P., Weinstein M.M., Farber E., Qiao X.,
RA Peale F., Bunting S., Walzem R.L., Wong J.S., Blaner W.S., Ding Z.-M.,
RA Melford K., Wongsiriroj N., Shu X., de Sauvage F., Ryan R.O., Fong L.G.,
RA Bensadoun A., Young S.G.;
RT "Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding
RT protein 1 plays a critical role in the lipolytic processing of
RT chylomicrons.";
RL Cell Metab. 5:279-291(2007).
RN [5] {ECO:0000305}
RP REVIEW.
RX PubMed=17620854; DOI=10.1097/mol.0b013e3281527914;
RA Young S.G., Davies B.S.J., Fong L.G., Gin P., Weinstein M.M., Bensadoun A.,
RA Beigneux A.P.;
RT "GPIHBP1: an endothelial cell molecule important for the lipolytic
RT processing of chylomicrons.";
RL Curr. Opin. Lipidol. 18:389-396(2007).
RN [6]
RP FUNCTION, GLYCOSYLATION AT ASN-76, SUBCELLULAR LOCATION, INTERACTION WITH
RP LPL AND APOA5, AND TISSUE SPECIFICITY.
RX PubMed=18340083; DOI=10.1194/jlr.m700593-jlr200;
RA Beigneux A.P., Gin P., Davies B.S., Weinstein M.M., Bensadoun A.,
RA Ryan R.O., Fong L.G., Young S.G.;
RT "Glycosylation of Asn-76 in mouse GPIHBP1 is critical for its appearance on
RT the cell surface and the binding of chylomicrons and lipoprotein lipase.";
RL J. Lipid Res. 49:1312-1321(2008).
RN [7]
RP MUTAGENESIS OF GLN-114, AND INTERACTION WITH LPL.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LPL, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF 24-GLU--GLU-48.
RX PubMed=20620994; DOI=10.1016/j.cmet.2010.04.016;
RA Davies B.S., Beigneux A.P., Barnes R.H. II, Tu Y., Gin P., Weinstein M.M.,
RA Nobumori C., Nyren R., Goldberg I., Olivecrona G., Bensadoun A.,
RA Young S.G., Fong L.G.;
RT "GPIHBP1 is responsible for the entry of lipoprotein lipase into
RT capillaries.";
RL Cell Metab. 12:42-52(2010).
RN [10]
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH LPL.
RX PubMed=24726386; DOI=10.1016/j.cmet.2014.01.017;
RA Goulbourne C.N., Gin P., Tatar A., Nobumori C., Hoenger A., Jiang H.,
RA Grovenor C.R., Adeyo O., Esko J.D., Goldberg I.J., Reue K., Tontonoz P.,
RA Bensadoun A., Beigneux A.P., Young S.G., Fong L.G.;
RT "The GPIHBP1-LPL complex is responsible for the margination of
RT triglyceride-rich lipoproteins in capillaries.";
RL Cell Metab. 19:849-860(2014).
RN [12]
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF CYS-88.
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 [13]
RP FUNCTION, INTERACTION WITH LPL, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Mediates the transport of lipoprotein lipase LPL from the
CC basolateral to the apical surface of endothelial cells in capillaries
CC (PubMed:20620994). Anchors LPL on the surface of endothelial cells in
CC the lumen of blood capillaries (PubMed:20620994, PubMed:24726386,
CC PubMed:27811232). Thereby, plays an important role in lipolytic
CC processing of chylomicrons by LPL, triglyceride metabolism and lipid
CC homeostasis (PubMed:17403372). Binds chylomicrons and phospholipid
CC particles that contain APOA5 (PubMed:18340083). Binds high-density
CC lipoprotein (HDL) and plays a role in the uptake of lipids from HDL
CC (PubMed:12496272). {ECO:0000269|PubMed:12496272,
CC ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083,
CC ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386,
CC ECO:0000269|PubMed:27811232}.
CC -!- SUBUNIT: Mostly monomer, but also homodimer and homooligomer
CC (PubMed:25387803). Interacts with lipoprotein lipase (LPL)
CC (PubMed:17403372, PubMed:18340083, PubMed:19304573, PubMed:20620994,
CC PubMed:25387803, PubMed:24726386, PubMed:27811232). Interacts with high
CC affinity with high-density lipoprotein (HDL) (PubMed:12496272).
CC Interacts with chylomicrons (PubMed:17403372). Interacts with APOA5
CC (PubMed:18340083). {ECO:0000269|PubMed:12496272,
CC ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083,
CC ECO:0000269|PubMed:19304573, ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:25387803,
CC ECO:0000269|PubMed:27811232}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:25387803}. Basolateral cell membrane
CC {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:25387803}. Cell membrane
CC {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083,
CC ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}; Lipid-
CC anchor, GPI-anchor {ECO:0000269|PubMed:17403372,
CC ECO:0000269|PubMed:18340083, ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:25387803}.
CC -!- TISSUE SPECIFICITY: Detected in fat tissue (PubMed:18340083,
CC PubMed:17403372). Detected on the luminal surface of capillary
CC endothelial cells in heart, skeletal muscle and brown adipose tissue
CC (at protein level) (PubMed:17403372, PubMed:20620994). Detected in
CC heart and brown adipose tissue (PubMed:12496272, PubMed:17403372).
CC Expressed at lower levels in lung and liver (PubMed:12496272).
CC {ECO:0000269|PubMed:12496272, ECO:0000269|PubMed:17403372,
CC ECO:0000269|PubMed:18340083, ECO:0000269|PubMed:20620994}.
CC -!- INDUCTION: Induced by fasting. {ECO:0000269|PubMed:17403372}.
CC -!- DOMAIN: The N-terminal acidic region is intrinsically disordered (By
CC similarity). This region contributes to LPL binding (PubMed:20620994).
CC It stabilizes LPL and protects LPL against loss of activity (By
CC similarity). {ECO:0000250|UniProtKB:Q8IV16,
CC ECO:0000269|PubMed:20620994}.
CC -!- PTM: Glycosylation of Asn-76 is critical for cell surface localization.
CC {ECO:0000269|PubMed:18340083}.
CC -!- PTM: Sulfation of a Tyr in the N-terminal acidic region increases the
CC affinity for LPL. {ECO:0000250|UniProtKB:Q8IV16}.
CC -!- DISRUPTION PHENOTYPE: Adult mice display chylomicronemia when kept on a
CC normal chow diet, with milky-looking blood plasma due to marked
CC accumulation of chylomicrons in the plasma. Their plasma triglyceride
CC levels are generally above 1000 mg/dl and can be as high as 5000 mg/dl.
CC Mice display decreased plasma levels of lipoprotein lipase LPL
CC (PubMed:17403372). Contrary to wild-type, LPL is not recruited to the
CC apical surface of endothelial cell that faces the lumen of capillaries,
CC but is mislocalized to the interstitial spaces surrounding myocytes and
CC adipocytes (PubMed:20620994, PubMed:24726386, PubMed:27811232).
CC {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994,
CC ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}.
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DR EMBL; AB095543; BAC23061.1; -; mRNA.
DR EMBL; AK003305; BAB22704.1; -; mRNA.
DR EMBL; BC061225; AAH61225.1; -; mRNA.
DR CCDS; CCDS27545.1; -.
DR RefSeq; NP_081006.1; NM_026730.1.
DR AlphaFoldDB; Q9D1N2; -.
DR SMR; Q9D1N2; -.
DR STRING; 10090.ENSMUSP00000023243; -.
DR GlyGen; Q9D1N2; 1 site.
DR iPTMnet; Q9D1N2; -.
DR PhosphoSitePlus; Q9D1N2; -.
DR MaxQB; Q9D1N2; -.
DR PaxDb; Q9D1N2; -.
DR PeptideAtlas; Q9D1N2; -.
DR PRIDE; Q9D1N2; -.
DR ProteomicsDB; 269685; -.
DR Antibodypedia; 75628; 198 antibodies from 18 providers.
DR DNASU; 68453; -.
DR Ensembl; ENSMUST00000023243; ENSMUSP00000023243; ENSMUSG00000022579.
DR GeneID; 68453; -.
DR KEGG; mmu:68453; -.
DR UCSC; uc007wgw.1; mouse.
DR CTD; 338328; -.
DR MGI; MGI:1915703; Gpihbp1.
DR VEuPathDB; HostDB:ENSMUSG00000022579; -.
DR eggNOG; ENOG502SVBD; Eukaryota.
DR GeneTree; ENSGT00940000153378; -.
DR HOGENOM; CLU_102231_0_0_1; -.
DR InParanoid; Q9D1N2; -.
DR OMA; TVEGTQM; -.
DR OrthoDB; 1415737at2759; -.
DR PhylomeDB; Q9D1N2; -.
DR TreeFam; TF338440; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-MMU-8963901; Chylomicron remodeling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 68453; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gpihbp1; mouse.
DR PRO; PR:Q9D1N2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D1N2; protein.
DR Bgee; ENSMUSG00000022579; Expressed in right lung and 121 other tissues.
DR ExpressionAtlas; Q9D1N2; baseline and differential.
DR Genevisible; Q9D1N2; MM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISO:MGI.
DR GO; GO:0031225; C:anchored component of membrane; IBA:GO_Central.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0035478; F:chylomicron binding; IMP:BHF-UCL.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0071813; F:lipoprotein particle binding; IMP:UniProtKB.
DR GO; GO:0140318; F:protein transporter activity; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IDA:BHF-UCL.
DR GO; GO:0006869; P:lipid transport; IDA:MGI.
DR GO; GO:0090321; P:positive regulation of chylomicron remnant clearance; IMP:BHF-UCL.
DR GO; GO:0090319; P:positive regulation of chylomicron remodeling; IC:BHF-UCL.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
DR GO; GO:0017038; P:protein import; IDA:BHF-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0071503; P:response to heparin; ISO:MGI.
DR GO; GO:0045056; P:transcytosis; IDA:BHF-UCL.
DR GO; GO:0019433; P:triglyceride catabolic process; ISO:MGI.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
DR CDD; cd00117; LU; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR018363; CD59_antigen_CS.
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.
DR PROSITE; PS00983; LY6_UPAR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hyperlipidemia;
KW Lipid-binding; Lipoprotein; Membrane; Reference proteome; Signal;
KW Sulfation; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..198
FT /note="Glycosylphosphatidylinositol-anchored high density
FT lipoprotein-binding protein 1"
FT /id="PRO_0000343798"
FT PROPEP 199..228
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000429859"
FT DOMAIN 61..148
FT /note="UPAR/Ly6"
FT /evidence="ECO:0000255"
FT REGION 21..32
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT REGION 24..48
FT /note="Important for LPL transport to the lumenal surface
FT of endothelial cells"
FT /evidence="ECO:0000269|PubMed:20620994"
FT REGION 102..108
FT /note="Important for interaction with LPL"
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT REGION 145..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT LIPID 198
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000305|PubMed:12496272"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18340083"
FT DISULFID 63..88
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT DISULFID 66..75
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT DISULFID 81..109
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT DISULFID 113..129
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT DISULFID 130..135
FT /evidence="ECO:0000250|UniProtKB:Q8IV16"
FT MUTAGEN 24..48
FT /note="EDGDADPEPENYNYDDDDDEEEEEE->AAGAAAPAPANYNYAAAAAAAAAAA
FT : Nearly abolishes LPL transport to the lumenal surface of
FT endothelial cells."
FT /evidence="ECO:0000269|PubMed:20620994"
FT MUTAGEN 88
FT /note="C->A: Reduced number of monomers."
FT /evidence="ECO:0000269|PubMed:25387803"
FT MUTAGEN 114
FT /note="Q->P: Loss of interaction with LPL."
FT /evidence="ECO:0000269|PubMed:19304573"
SQ 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
