ANGL3_MOUSE
ID ANGL3_MOUSE Reviewed; 455 AA.
AC Q9R182;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Angiopoietin-related protein 3;
DE AltName: Full=Angiopoietin-like protein 3;
DE Contains:
DE RecName: Full=ANGPTL3(17-224);
DE Flags: Precursor;
GN Name=Angptl3;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10644446; DOI=10.1006/geno.1999.6041;
RA Conklin D., Gilbertson D., Taft D.W., Maurer M.F., Whitmore T.E.,
RA Smith D.L., Walker K.M., Chen L.H., Wattler S., Nehls M., Lewis K.B.;
RT "Identification of a mammalian angiopoietin-related protein expressed
RT specifically in liver.";
RL Genomics 62:477-482(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
RP FUNCTION.
RX PubMed=11877390; DOI=10.1074/jbc.m109768200;
RA Camenisch G., Pisabarro M.T., Sherman D., Kowalski J., Nagel M., Hass P.,
RA Xie M.H., Gurney A., Bodary S., Liang X.H., Clark K., Beresini M.,
RA Ferrara N., Gerber H.P.;
RT "ANGPTL3 stimulates endothelial cell adhesion and migration via integrin
RT alpha vbeta 3 and induces blood vessel formation in vivo.";
RL J. Biol. Chem. 277:17281-17290(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11788823; DOI=10.1038/ng814;
RA Koishi R., Ando Y., Ono M., Shimamura M., Yasumo H., Fujiwara T.,
RA Horikoshi H., Furukawa H.;
RT "Angptl3 regulates lipid metabolism in mice.";
RL Nat. Genet. 30:151-157(2002).
RN [5]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=12909640; DOI=10.1074/jbc.m302861200;
RA Ono M., Shimizugawa T., Shimamura M., Yoshida K., Noji-Sakikawa C.,
RA Ando Y., Koishi R., Furukawa H.;
RT "Protein region important for regulation of lipid metabolism in
RT angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo.";
RL J. Biol. Chem. 278:41804-41809(2003).
RN [6]
RP FUNCTION.
RX PubMed=12671033; DOI=10.1194/jlr.m300031-jlr200;
RA Ando Y., Shimizugawa T., Takeshita S., Ono M., Shimamura M., Koishi R.,
RA Furukawa H.;
RT "A decreased expression of angiopoietin-like 3 is protective against
RT atherosclerosis in apoE-deficient mice.";
RL J. Lipid Res. 44:1216-1223(2003).
RN [7]
RP INDUCTION.
RX PubMed=15336575; DOI=10.1016/j.bbrc.2004.08.024;
RA Shimamura M., Matsuda M., Ando Y., Koishi R., Yasumo H., Furukawa H.,
RA Shimomura I.;
RT "Leptin and insulin down-regulate angiopoietin-like protein 3, a plasma
RT triglyceride-increasing factor.";
RL Biochem. Biophys. Res. Commun. 322:1080-1085(2004).
RN [8]
RP INDUCTION.
RX PubMed=15863837; DOI=10.1194/jlr.m500005-jlr200;
RA Ge H., Cha J.Y., Gopal H., Harp C., Yu X., Repa J.J., Li C.;
RT "Differential regulation and properties of angiopoietin-like proteins 3 and
RT 4.";
RL J. Lipid Res. 46:1484-1490(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16081640; DOI=10.1210/en.2005-0476;
RA Koester A., Chao Y.B., Mosior M., Ford A., Gonzalez-DeWhitt P.A.,
RA Hale J.E., Li D., Qiu Y., Fraser C.C., Yang D.D., Heuer J.G.,
RA Jaskunas S.R., Eacho P.;
RT "Transgenic angiopoietin-like (angptl)4 overexpression and targeted
RT disruption of angptl4 and angptl3: regulation of triglyceride metabolism.";
RL Endocrinology 146:4943-4950(2005).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=16508209; DOI=10.1538/expanim.55.27;
RA Fujimoto K., Koishi R., Shimizugawa T., Ando Y.;
RT "Angptl3-null mice show low plasma lipid concentrations by enhanced
RT lipoprotein lipase activity.";
RL Exp. Anim. 55:27-34(2006).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=17110602; DOI=10.1161/01.atv.0000252827.51626.89;
RA Shimamura M., Matsuda M., Yasumo H., Okazaki M., Fujimoto K., Kono K.,
RA Shimizugawa T., Ando Y., Koishi R., Kohama T., Sakai N., Kotani K.,
RA Komuro R., Ishida T., Hirata K., Yamashita S., Furukawa H., Shimomura I.;
RT "Angiopoietin-like protein3 regulates plasma HDL cholesterol through
RT suppression of endothelial lipase.";
RL Arterioscler. Thromb. Vasc. Biol. 27:366-372(2007).
RN [12]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=17681148; DOI=10.1016/j.cmet.2007.07.009;
RA Jin W., Wang X., Millar J.S., Quertermous T., Rothblat G.H., Glick J.M.,
RA Rader D.J.;
RT "Hepatic proprotein convertases modulate HDL metabolism.";
RL Cell Metab. 6:129-136(2007).
RN [13]
RP FUNCTION.
RX PubMed=20633534; DOI=10.1016/j.bbrc.2010.07.027;
RA Gao X., Xu H., Liu H., Rao J., Li Y., Zha X.;
RT "Angiopoietin-like protein 3 regulates the motility and permeability of
RT podocytes by altering nephrin expression in vitro.";
RL Biochem. Biophys. Res. Commun. 399:31-36(2010).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ARG-221.
RX PubMed=20581395; DOI=10.1074/jbc.m110.144279;
RA Liu J., Afroza H., Rader D.J., Jin W.;
RT "Angiopoietin-like protein 3 inhibits lipoprotein lipase activity through
RT enhancing its cleavage by proprotein convertases.";
RL J. Biol. Chem. 285:27561-27570(2010).
RN [15]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=20424482; DOI=10.1159/000313829;
RA Jia R., Hong X., Li S., Haichun Y., Chuanming H.;
RT "Expression of angiopoietin-like 3 associated with puromycin-induced
RT podocyte damage.";
RL Nephron Exp. Nephrol. 115:E38-E45(2010).
RN [16]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20959605; DOI=10.1182/blood-2010-06-291716;
RA Zheng J., Huynh H., Umikawa M., Silvany R., Zhang C.C.;
RT "Angiopoietin-like protein 3 supports the activity of hematopoietic stem
RT cells in the bone marrow niche.";
RL Blood 117:470-479(2011).
RN [17]
RP FUNCTION.
RX PubMed=24294595; DOI=10.1155/2013/135608;
RA Lin Y., Rao J., Zha X.L., Xu H.;
RT "Angiopoietin-like 3 induces podocyte F-actin rearrangement through
RT integrin alpha(V)beta(3)/FAK/PI3K pathway-mediated Rac1 activation.";
RL Biomed. Res. Int. 2013:135608-135608(2013).
RN [18]
RP PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF ARG-221 AND ARG-224, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23918928; DOI=10.1074/jbc.m113.501304;
RA Essalmani R., Susan-Resiga D., Chamberland A., Asselin M.C., Canuel M.,
RA Constam D., Creemers J.W., Day R., Gauthier D., Prat A., Seidah N.G.;
RT "Furin is the primary in vivo convertase of angiopoietin-like 3 and
RT endothelial lipase in hepatocytes.";
RL J. Biol. Chem. 288:26410-26418(2013).
RN [19]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25338813; DOI=10.2337/db14-0647;
RA Kim H.K., Shin M.S., Youn B.S., Kang G.M., Gil S.Y., Lee C.H., Choi J.H.,
RA Lim H.S., Yoo H.J., Kim M.S.;
RT "Regulation of energy balance by the hypothalamic lipoprotein lipase
RT regulator Angptl3.";
RL Diabetes 64:1142-1153(2015).
RN [20]
RP FUNCTION.
RX PubMed=25954050; DOI=10.1194/jlr.m054882;
RA Wang Y., Gusarova V., Banfi S., Gromada J., Cohen J.C., Hobbs H.H.;
RT "Inactivation of ANGPTL3 reduces hepatic VLDL-triglyceride secretion.";
RL J. Lipid Res. 56:1296-1307(2015).
RN [21]
RP FUNCTION, INTERACTION WITH ITGB3, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25710887; DOI=10.1038/pr.2015.38;
RA Liu J., Gao X., Zhai Y., Shen Q., Sun L., Feng C., Rao J., Liu H., Zha X.,
RA Guo M., Ma D., Zhang Z., Li R., Xu H.;
RT "A novel role of angiopoietin-like-3 associated with podocyte injury.";
RL Pediatr. Res. 77:732-739(2015).
RN [22]
RP FUNCTION.
RX PubMed=26305978; DOI=10.1073/pnas.1515374112;
RA Wang Y., McNutt M.C., Banfi S., Levin M.G., Holland W.L., Gusarova V.,
RA Gromada J., Cohen J.C., Hobbs H.H.;
RT "Hepatic ANGPTL3 regulates adipose tissue energy homeostasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11630-11635(2015).
CC -!- FUNCTION: Acts in part as a hepatokine that is involved in regulation
CC of lipid and glucose metabolism (PubMed:11788823, PubMed:12671033).
CC Proposed to play a role in the trafficking of energy substrates to
CC either storage or oxidative tissues in response to food intake
CC (PubMed:26305978). Has a stimulatory effect on plasma triglycerides
CC (TG), which is achieved by suppressing plasma TG clearance via
CC inhibition of LPL activity; the function seems to be specific for the
CC feeding conditions. The inhibition of LPL activity appears to be an
CC indirect mechanism involving recruitment of proprotein convertases
CC PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from
CC the cell surface; the function does not require ANGPTL3 proteolytic
CC cleavage but seems to be mediated by the N-terminal domain, and is not
CC inhibited by GPIHBP1 (PubMed:12909640, PubMed:16081640,
CC PubMed:20581395). Can inhibit endothelial lipase, causing increased
CC plasma levels of high density lipoprotein (HDL) cholesterol and
CC phospholipids; the cleaved N-terminal domain is more efficient than the
CC uncleaved proprotein (PubMed:17681148). Can bind to adipocytes to
CC activate lipolysis, releasing free fatty acids and glycerol (By
CC similarity). Suppresses LPL specifically in oxidative tissues which is
CC required to route very low density lipoprotein (VLDL)-TG to white
CC adipose tissue (WAT) for storage in response to food; the function may
CC involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4
CC expression in WAT (PubMed:26305978). Contributes to lower plasma levels
CC of low density lipoprotein (LDL)-cholesterol by a mechanism that is
CC independent of the canonical pathway implicating APOE and LDLR
CC (PubMed:25954050). May stimulate hypothalamic LPL activity
CC (PubMed:25338813). {ECO:0000250|UniProtKB:Q9Y5C1,
CC ECO:0000269|PubMed:11788823, ECO:0000269|PubMed:12671033,
CC ECO:0000269|PubMed:16081640, ECO:0000269|PubMed:17681148,
CC ECO:0000269|PubMed:20581395, ECO:0000269|PubMed:25338813,
CC ECO:0000269|PubMed:25954050, ECO:0000269|PubMed:26305978}.
CC -!- FUNCTION: Involved in angiogenesis (PubMed:11877390). Binds to
CC endothelial cells via integrin alpha-V/beta-3 (ITGAV:ITGB3), activates
CC FAK, MAPK and Akt signaling pathways and induces cell adhesion and cell
CC migration (By similarity). May increase the motility of podocytes.
CC Secreted from podocytes, may modulate properties of glomerular
CC endothelial cells involving integrin alpha-V/beta-3 and Akt signaling
CC (By similarity). May induce actin filament rearrangements in podocytes
CC implicating integrin alpha-V/beta-3 and Rac1 activation
CC (PubMed:20633534, PubMed:24294595, PubMed:25710887). Binds to
CC hematopoietic stem cells (HSC) and is involved in the regulation of HSC
CC activity probably implicating down-regulation of IKZF1/IKAROS
CC (PubMed:20959605). {ECO:0000250|UniProtKB:Q9Y5C1,
CC ECO:0000269|PubMed:11877390, ECO:0000269|PubMed:20633534,
CC ECO:0000269|PubMed:20959605, ECO:0000269|PubMed:24294595,
CC ECO:0000269|PubMed:25710887}.
CC -!- SUBUNIT: Interacts with ANGPTL8 (By similarity). Interacts with ITGB3.
CC {ECO:0000250|UniProtKB:Q9Y5C1, ECO:0000269|PubMed:25710887}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23918928}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:25710887}.
CC Note=Colocalized with HSPG2 and activated ITGB3 on podocytes.
CC {ECO:0000269|PubMed:20424482, ECO:0000269|PubMed:25710887}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver, weakly expressed
CC in kidney and lung. Expressed in podocytes (at protein level).
CC Expressed in hypothalamic neurons (at protein level). Expressed in bone
CC marrow sinusoidal endothelial cells (at protein level).
CC {ECO:0000269|PubMed:10644446, ECO:0000269|PubMed:20959605,
CC ECO:0000269|PubMed:25338813, ECO:0000269|PubMed:25710887}.
CC -!- INDUCTION: Down-regulated by insulin and leptin. Not regulated by
CC nutritional status (fed/fasting) Up-regulated in podocytes by
CC puromycin. Up-regulated after feeding in the hypothalamus.
CC {ECO:0000269|PubMed:15336575, ECO:0000269|PubMed:15863837,
CC ECO:0000269|PubMed:20424482, ECO:0000269|PubMed:25338813}.
CC -!- DOMAIN: The fibrinogen C-terminal domain is sufficient to mediate
CC endothelial cell adhesion. {ECO:0000250|UniProtKB:Q9Y5C1}.
CC -!- PTM: In part proteolytically cleaved by proprotein convertases;
CC proposed to be involved in activation. In primary hepatocytes is
CC intracellularily predominantly processed by FURIN and extracellularily
CC by FURIN and PCSK6/PACE4. In 18.5 dpc embryos 75% of protein is found
CC to be processed compared to 25 % in adults.
CC {ECO:0000269|PubMed:17681148, ECO:0000269|PubMed:23918928}.
CC -!- DISRUPTION PHENOTYPE: Low plasma levels of triglyceride, HDL
CC cholesterol and HDL phospholipids, and non-esterified fatty acids
CC (NEFA). Animals fed on high-fat, high-calorie (HFC) diet show reduced
CC epididymal adipose tissue weight with no difference in adipocyte size.
CC Hypotriglyceridemia with elevated postheparin plasma LPL activity is
CC specifically observed in the fed state. Mice deficient in both Angptl3
CC and Angptl4 show an additive effect on plasma triglycerides and did not
CC survive past 2 months of age. {ECO:0000269|PubMed:11788823,
CC ECO:0000269|PubMed:15336575, ECO:0000269|PubMed:16081640,
CC ECO:0000269|PubMed:17110602}.
CC -!- MISCELLANEOUS: Was suggested to inhibit LPL through a direct mechanism;
CC however, the necessary concentrations to achieve the in vitro
CC inhibition are at least 30-fold higher than ANGPTL3 plasma
CC concentrations. {ECO:0000305|PubMed:20581395}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF162224; AAD45920.1; -; mRNA.
DR EMBL; BC019491; AAH19491.1; -; mRNA.
DR CCDS; CCDS38817.1; -.
DR RefSeq; NP_038941.1; NM_013913.4.
DR AlphaFoldDB; Q9R182; -.
DR SMR; Q9R182; -.
DR STRING; 10090.ENSMUSP00000030280; -.
DR GlyGen; Q9R182; 5 sites.
DR iPTMnet; Q9R182; -.
DR PhosphoSitePlus; Q9R182; -.
DR CPTAC; non-CPTAC-4016; -.
DR MaxQB; Q9R182; -.
DR PaxDb; Q9R182; -.
DR PRIDE; Q9R182; -.
DR ProteomicsDB; 296291; -.
DR ABCD; Q9R182; 1 sequenced antibody.
DR Antibodypedia; 19489; 492 antibodies from 39 providers.
DR DNASU; 30924; -.
DR Ensembl; ENSMUST00000030280; ENSMUSP00000030280; ENSMUSG00000028553.
DR GeneID; 30924; -.
DR KEGG; mmu:30924; -.
DR UCSC; uc008tur.1; mouse.
DR CTD; 27329; -.
DR MGI; MGI:1353627; Angptl3.
DR VEuPathDB; HostDB:ENSMUSG00000028553; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000156746; -.
DR HOGENOM; CLU_038628_2_0_1; -.
DR InParanoid; Q9R182; -.
DR OMA; DWKEEKH; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; Q9R182; -.
DR TreeFam; TF329953; -.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR BioGRID-ORCS; 30924; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q9R182; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9R182; protein.
DR Bgee; ENSMUSG00000028553; Expressed in left lobe of liver and 62 other tissues.
DR ExpressionAtlas; Q9R182; baseline and differential.
DR Genevisible; Q9R182; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; ISS:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0004859; F:phospholipase inhibitor activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0055090; P:acylglycerol homeostasis; IMP:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0006071; P:glycerol metabolic process; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
DR GO; GO:0019915; P:lipid storage; ISO:MGI.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; ISO:MGI.
DR GO; GO:0010519; P:negative regulation of phospholipase activity; IMP:BHF-UCL.
DR GO; GO:0009395; P:phospholipid catabolic process; ISO:MGI.
DR GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; ISO:MGI.
DR GO; GO:0045834; P:positive regulation of lipid metabolic process; NAS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
DR GO; GO:0006641; P:triglyceride metabolic process; NAS:UniProtKB.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell adhesion; Cell projection; Coiled coil; Disulfide bond;
KW Glycoprotein; Heparin-binding; Lipid metabolism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..455
FT /note="Angiopoietin-related protein 3"
FT /id="PRO_0000009123"
FT CHAIN 17..224
FT /note="ANGPTL3(17-224)"
FT /evidence="ECO:0000305|PubMed:12909640,
FT ECO:0000305|PubMed:23918928"
FT /id="PRO_0000435905"
FT DOMAIN 237..455
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 17..207
FT /note="Sufficient to inhibit LIPG/EL phospholipase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5C1"
FT REGION 17..165
FT /note="Sufficient to inhibit LPL lipase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5C1,
FT ECO:0000269|PubMed:20581395"
FT REGION 32..56
FT /note="Required for inhibition of LPL lipase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5C1"
FT REGION 202..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..206
FT /evidence="ECO:0000255"
FT COMPBIAS 208..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5C1"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 394..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT MUTAGEN 221
FT /note="R->A: Abolishes proteolytical cleavage."
FT /evidence="ECO:0000269|PubMed:20581395,
FT ECO:0000269|PubMed:23918928"
FT MUTAGEN 224
FT /note="R->A: Abolishes proteolytical cleavage."
FT /evidence="ECO:0000269|PubMed:23918928"
SQ SEQUENCE 455 AA; 52543 MW; 31609D3700D3F33D CRC64;
MHTIKLFLFV VPLVIASRVD PDLSSFDSAP SEPKSRFAML DDVKILANGL LQLGHGLKDF
VHKTKGQIND IFQKLNIFDQ SFYDLSLRTN EIKEEEKELR RTTSTLQVKN EEVKNMSVEL
NSKLESLLEE KTALQHKVRA LEEQLTNLIL SPAGAQEHPE VTSLKSFVEQ QDNSIRELLQ
SVEEQYKQLS QQHMQIKEIE KQLRKTGIQE PSENSLSSKS RAPRTTPPLQ LNETENTEQD
DLPADCSAVY NRGEHTSGVY TIKPRNSQGF NVYCDTQSGS PWTLIQHRKD GSQDFNETWE
NYEKGFGRLD GEFWLGLEKI YAIVQQSNYI LRLELQDWKD SKHYVEYSFH LGSHETNYTL
HVAEIAGNIP GALPEHTDLM FSTWNHRAKG QLYCPESYSG GWWWNDICGE NNLNGKYNKP
RTKSRPERRR GIYWRPQSRK LYAIKSSKMM LQPTT
