ANGL4_MOUSE
ID ANGL4_MOUSE Reviewed; 410 AA.
AC Q9Z1P8; Q78ZJ9; Q9JHX7; Q9JLX7;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Angiopoietin-related protein 4;
DE AltName: Full=425O18-1;
DE AltName: Full=Angiopoietin-like protein 4;
DE AltName: Full=Fasting-induced adipose factor {ECO:0000303|PubMed:10862772};
DE AltName: Full=Hepatic fibrinogen/angiopoietin-related protein {ECO:0000303|PubMed:10698685};
DE Short=HFARP {ECO:0000303|PubMed:10698685};
DE AltName: Full=Secreted protein Bk89;
DE Contains:
DE RecName: Full=ANGPTL4 N-terminal chain;
DE Contains:
DE RecName: Full=ANGPTL4 C-terminal chain;
DE Flags: Precursor;
GN Name=Angptl4; Synonyms=Farp, Fiaf {ECO:0000303|PubMed:10862772}, Ng27;
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=10698685; DOI=10.1042/bj3460603;
RA Kim I., Kim H.-G., Kim H., Kim H.-H., Park S.K., Uhm C.-S., Lee Z.H.,
RA Koh G.Y.;
RT "Hepatic expression, synthesis and secretion of a novel
RT fibrinogen/angiopoietin-related protein that prevents endothelial-cell
RT apoptosis.";
RL Biochem. J. 346:603-610(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=White adipose tissue;
RX PubMed=10862772; DOI=10.1074/jbc.m004029200;
RA Kersten S., Mandard S., Tan N.S., Escher P., Metzger D., Chambon P.,
RA Gonzalez F.J., Desvergne B., Wahli W.;
RT "Characterization of the fasting-induced adipose factor FIAF, a novel
RT peroxisome proliferator-activated receptor target gene.";
RL J. Biol. Chem. 275:28488-28493(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP TRANSGENIC MICE.
RX PubMed=14583458;
RA Ito Y., Oike Y., Yasunaga K., Hamada K., Miyata K., Matsumoto S.,
RA Sugano S., Tanihara H., Masuho Y., Suda T.;
RT "Inhibition of angiogenesis and vascular leakiness by angiopoietin-related
RT protein 4.";
RL Cancer Res. 63:6651-6657(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Adipocyte;
RX PubMed=10866690; DOI=10.1128/mcb.20.14.5343-5349.2000;
RA Yoon J.C., Chickering T.W., Rosen E.D., Dussault B., Qin Y., Soukas A.,
RA Friedman J.M., Holmes W.E., Spiegelman B.M.;
RT "Peroxisome proliferator-activated receptor gamma target gene encoding a
RT novel angiopoietin-related protein associated with adipose
RT differentiation.";
RL Mol. Cell. Biol. 20:5343-5349(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA Nagaraja R.;
RT "Gene content of the 750-kb critical region for mouse embryonic ectoderm
RT lethal tcl-w5.";
RL Mamm. Genome 15:265-276(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15837923; DOI=10.1073/pnas.0408452102;
RA Xu A., Lam M.C., Chan K.W., Wang Y., Zhang J., Hoo R.L., Xu J.Y., Chen B.,
RA Chow W.S., Tso A.W., Lam K.S.;
RT "Angiopoietin-like protein 4 decreases blood glucose and improves glucose
RT tolerance but induces hyperlipidemia and hepatic steatosis in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6086-6091(2005).
RN [10]
RP INDUCTION BY ISCHEMIA.
RX PubMed=17068295; DOI=10.1161/01.res.0000250758.63358.91;
RA Cazes A., Galaup A., Chomel C., Bignon M., Brechot N., Le Jan S., Weber H.,
RA Corvol P., Muller L., Germain S., Monnot C.;
RT "Extracellular matrix-bound angiopoietin-like 4 inhibits endothelial cell
RT adhesion, migration, and sprouting and alters actin cytoskeleton.";
RL Circ. Res. 99:1207-1215(2006).
RN [11]
RP FUNCTION, AND XENOGRAFT MODELS.
RX PubMed=17130448; DOI=10.1073/pnas.0609025103;
RA Galaup A., Cazes A., Le Jan S., Philippe J., Connault E., Le Coz E.,
RA Mekid H., Mir L.M., Opolon P., Corvol P., Monnot C., Germain S.;
RT "Angiopoietin-like 4 prevents metastasis through inhibition of vascular
RT permeability and tumor cell motility and invasiveness.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18721-18726(2006).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17609370; DOI=10.1073/pnas.0705041104;
RA Desai U., Lee E.C., Chung K., Gao C., Gay J., Key B., Hansen G.,
RA Machajewski D., Platt K.A., Sands A.T., Schneider M., Van Sligtenhorst I.,
RA Suwanichkul A., Vogel P., Wilganowski N., Wingert J., Zambrowicz B.P.,
RA Landes G., Powell D.R.;
RT "Lipid-lowering effects of anti-angiopoietin-like 4 antibody recapitulate
RT the lipid phenotype found in angiopoietin-like 4 knockout mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11766-11771(2007).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=21832056; DOI=10.1074/jbc.m111.220061;
RA Perdiguero E.G., Galaup A., Durand M., Teillon J., Philippe J.,
RA Valenzuela D.M., Murphy A.J., Yancopoulos G.D., Thurston G., Germain S.;
RT "Alteration of developmental and pathological retinal angiogenesis in
RT angptl4-deficient mice.";
RL J. Biol. Chem. 286:36841-36851(2011).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29899519; DOI=10.1038/s41467-018-04611-z;
RA Gusarova V., O'Dushlaine C., Teslovich T.M., Benotti P.N., Mirshahi T.,
RA Gottesman O., Van Hout C.V., Murray M.F., Mahajan A., Nielsen J.B.,
RA Fritsche L., Wulff A.B., Gudbjartsson D.F., Sjoegren M., Emdin C.A.,
RA Scott R.A., Lee W.J., Small A., Kwee L.C., Dwivedi O.P., Prasad R.B.,
RA Bruse S., Lopez A.E., Penn J., Marcketta A., Leader J.B., Still C.D.,
RA Kirchner H.L., Mirshahi U.L., Wardeh A.H., Hartle C.M., Habegger L.,
RA Fetterolf S.N., Tusie-Luna T., Morris A.P., Holm H., Steinthorsdottir V.,
RA Sulem P., Thorsteinsdottir U., Rotter J.I., Chuang L.M., Damrauer S.,
RA Birtwell D., Brummett C.M., Khera A.V., Natarajan P., Orho-Melander M.,
RA Flannick J., Lotta L.A., Willer C.J., Holmen O.L., Ritchie M.D.,
RA Ledbetter D.H., Murphy A.J., Borecki I.B., Reid J.G., Overton J.D.,
RA Hansson O., Groop L., Shah S.H., Kraus W.E., Rader D.J., Chen Y.I.,
RA Hveem K., Wareham N.J., Kathiresan S., Melander O., Stefansson K.,
RA Nordestgaard B.G., Tybjaerg-Hansen A., Abecasis G.R., Altshuler D.,
RA Florez J.C., Boehnke M., McCarthy M.I., Yancopoulos G.D., Carey D.J.,
RA Shuldiner A.R., Baras A., Dewey F.E., Gromada J.;
RT "Genetic inactivation of ANGPTL4 improves glucose homeostasis and is
RT associated with reduced risk of diabetes.";
RL Nat. Commun. 9:2252-2252(2018).
CC -!- FUNCTION: Mediates inactivation of the lipoprotein lipase LPL, and
CC thereby plays a role in the regulation of triglyceride clearance from
CC the blood serum and in lipid metabolism (PubMed:15837923,
CC PubMed:17609370, PubMed:29899519). May also play a role in regulating
CC glucose homeostasis and insulin sensitivity (PubMed:15837923,
CC PubMed:29899519). Inhibits proliferation, migration, and tubule
CC formation of endothelial cells and reduces vascular leakage
CC (PubMed:14583458, PubMed:17130448, PubMed:21832056). Upon heterologous
CC expression, inhibits the adhesion of endothelial cell to the
CC extracellular matrix (ECM), and inhibits the reorganization of the
CC actin cytoskeleton, formation of actin stress fibers and focal
CC adhesions in endothelial cells that have adhered to ANGPTL4-containing
CC ECM (in vitro) (By similarity). Depending on context, may modulate
CC tumor-related angiogenesis (Probable). {ECO:0000250|UniProtKB:Q9BY76,
CC ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:15837923,
CC ECO:0000269|PubMed:17130448, ECO:0000269|PubMed:17609370,
CC ECO:0000269|PubMed:21832056, ECO:0000269|PubMed:29899519,
CC ECO:0000305|PubMed:14583458, ECO:0000305|PubMed:17130448}.
CC -!- FUNCTION: [ANGPTL4 N-terminal chain]: Mediates inactivation of the
CC lipoprotein lipase LPL, and thereby plays an important role in the
CC regulation of triglyceride clearance from the blood serum and in lipid
CC metabolism. Has higher activity in LPL inactivation than the uncleaved
CC protein. {ECO:0000250|UniProtKB:Q9BY76}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked via Cys residues in the N-
CC terminal part of the protein (PubMed:14583458). The homooligomer
CC undergoes proteolytic processing to release the ANGPTL4 C-terminal
CC chain, which circulates as a monomer. The homooligomer unprocessed form
CC is able to interact with the extracellular matrix (By similarity).
CC {ECO:0000250|UniProtKB:Q9BY76, ECO:0000269|PubMed:14583458}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14583458,
CC ECO:0000269|PubMed:15837923}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:Q9BY76}. Note=The
CC unprocessed form interacts with the extracellular matrix. This may
CC constitute a dynamic reservoir, a regulatory mechanism of the
CC bioavailability of ANGPTL4. {ECO:0000250|UniProtKB:Q9BY76}.
CC -!- TISSUE SPECIFICITY: Detected in liver and kidney (PubMed:10698685,
CC PubMed:17609370). Predominantly expressed in adipose tissue and is
CC strongly up-regulated by fasting in white adipose tissue and liver.
CC {ECO:0000269|PubMed:10698685, ECO:0000269|PubMed:10862772,
CC ECO:0000269|PubMed:17609370}.
CC -!- DEVELOPMENTAL STAGE: Detected in endothelial cells in the capillary
CC plexus, veins and arteries in the retina at 2, 12 and 17 days after
CC birth (PubMed:21832056). Expressed at low levels in most organs and
CC connective tissue at 13.5 dpc. Between 15.5 dpc and 18.5 dpc, strongest
CC expression in brown fat. {ECO:0000269|PubMed:10866690,
CC ECO:0000269|PubMed:21832056}.
CC -!- INDUCTION: Induced in interstitial capillaries in response to hind leg
CC ischemia (PubMed:17068295). Alterations in nutrition and leptin
CC administration are found to modulate the expression in vivo.
CC {ECO:0000269|PubMed:10866690, ECO:0000269|PubMed:17068295}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9BY76}.
CC -!- PTM: [ANGPTL4 N-terminal chain]: Forms disulfide-linked dimers and
CC tetramers. {ECO:0000250|UniProtKB:Q9BY76}.
CC -!- PTM: Cleaved into a smaller N-terminal chain and a larger chain that
CC contains the fibrinogen C-terminal domain; both cleaved and uncleaved
CC forms are detected in the extracellular space. The cleaved form is not
CC present within the cell. {ECO:0000250|UniProtKB:Q9BY76}.
CC -!- DISRUPTION PHENOTYPE: Pups are born at less than the expected Mendelian
CC rate, indicative of significant embryonic lethality. No obvious
CC phenotype after birth; mice are viable and fertile (PubMed:21832056).
CC Mutant mice have reduced circulating triglyceride and cholesterol
CC levels when fed a high-fat diet (PubMed:17609370, PubMed:29899519).
CC Besides, they display 30% lower non-fasted blood glucose levels and
CC improved glucose tolerance when fed a high-fat diet. In contrast,
CC glucose levels and glucose tolerance are not different from wild-type
CC when mice are kept on a normal diet (PubMed:29899519). The retinal
CC vascular network displays subtle alterations, including a somewhat
CC larger diameter of veins and capillaries. Pups display a delay in
CC pericyte spreading on newly formed capillaries in the retina, and
CC defects in the organization of endothelial cell tight junctions. In
CC retinas from 17 day old animals, hypoxia-induced pathological
CC neovascularization is strongly reduced (PubMed:21832056). Some studies
CC observed decreased survival of suckling pups and of adults kept on a
CC high-fat diet due to intestinal pathologies, with lipogranulomatous
CC lesions of the intestines and their draining lymphatics and mesenteric
CC lymph nodes (PubMed:17609370). Other studies observed no such effects
CC (PubMed:29899519). {ECO:0000269|PubMed:17609370,
CC ECO:0000269|PubMed:21832056, ECO:0000269|PubMed:29899519}.
CC -!- MISCELLANEOUS: Upon heterologous expression under the control of the
CC keratinocyte promoter in the skin, inhibits tumor-associated
CC angiogenesis and tumor growth (PubMed:14583458). In xenograft models,
CC it inhibits both intra- and extravasation of tumor cells as well as
CC vascular permeability leading to inhibition of metastases. Expression
CC by tumor cells induces reorganization of the actin cytoskeleton through
CC inhibition of actin stress fiber formation and vinculin localization at
CC focal contacts. It might prevent the metastatic process by inhibiting
CC vascular activity as well as tumor cell motility and invasiveness
CC (PubMed:17130448). {ECO:0000269|PubMed:14583458,
CC ECO:0000269|PubMed:17130448}.
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; AF169313; AAF62869.1; -; mRNA.
DR EMBL; AF278699; AAF86342.1; -; mRNA.
DR EMBL; AB054540; BAB83079.1; -; mRNA.
DR EMBL; AF123261; AAF42969.1; -; mRNA.
DR EMBL; AK014564; BAB29431.1; -; mRNA.
DR EMBL; AK132761; BAE21342.1; -; mRNA.
DR EMBL; AF528162; AAO17378.1; -; Genomic_DNA.
DR EMBL; AF110520; AAC97965.1; -; Genomic_DNA.
DR EMBL; BC006611; AAH06611.1; -; mRNA.
DR EMBL; BC021343; AAH21343.1; -; mRNA.
DR EMBL; BC025797; AAH25797.1; -; mRNA.
DR CCDS; CCDS28629.1; -.
DR RefSeq; NP_065606.2; NM_020581.2.
DR AlphaFoldDB; Q9Z1P8; -.
DR SMR; Q9Z1P8; -.
DR BioGRID; 208345; 3.
DR DIP; DIP-61311N; -.
DR IntAct; Q9Z1P8; 1.
DR STRING; 10090.ENSMUSP00000002360; -.
DR GlyGen; Q9Z1P8; 3 sites.
DR PhosphoSitePlus; Q9Z1P8; -.
DR MaxQB; Q9Z1P8; -.
DR PaxDb; Q9Z1P8; -.
DR PRIDE; Q9Z1P8; -.
DR ProteomicsDB; 296356; -.
DR Antibodypedia; 1649; 524 antibodies from 38 providers.
DR DNASU; 57875; -.
DR Ensembl; ENSMUST00000002360; ENSMUSP00000002360; ENSMUSG00000002289.
DR GeneID; 57875; -.
DR KEGG; mmu:57875; -.
DR UCSC; uc008bzp.2; mouse.
DR CTD; 51129; -.
DR MGI; MGI:1888999; Angptl4.
DR VEuPathDB; HostDB:ENSMUSG00000002289; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000159478; -.
DR HOGENOM; CLU_038628_2_1_1; -.
DR InParanoid; Q9Z1P8; -.
DR OMA; INCAKHL; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; Q9Z1P8; -.
DR TreeFam; TF329953; -.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR BioGRID-ORCS; 57875; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Angptl4; mouse.
DR PRO; PR:Q9Z1P8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1P8; protein.
DR Bgee; ENSMUSG00000002289; Expressed in brown adipose tissue and 180 other tissues.
DR ExpressionAtlas; Q9Z1P8; baseline and differential.
DR Genevisible; Q9Z1P8; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0009267; P:cellular response to starvation; NAS:UniProtKB.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IDA:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:MGI.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IDA:UniProtKB.
DR GO; GO:0045834; P:positive regulation of lipid metabolic process; NAS:UniProtKB.
DR GO; GO:0043335; P:protein unfolding; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR028793; ANGPTL4.
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 InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF256; PTHR19143:SF256; 2.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Coiled coil; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..410
FT /note="Angiopoietin-related protein 4"
FT /id="PRO_0000009125"
FT CHAIN 24..167
FT /note="ANGPTL4 N-terminal chain"
FT /id="PRO_0000446861"
FT CHAIN 168..410
FT /note="ANGPTL4 C-terminal chain"
FT /id="PRO_0000446862"
FT DOMAIN 183..405
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 79..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..152
FT /evidence="ECO:0000255"
FT SITE 168..169
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9BY76"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 192..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 345..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 168..170
FT /note="RLP -> KLS (in Ref. 4; AAF42969)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="P -> S (in Ref. 4; AAF42969)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="P -> A (in Ref. 4; AAF42969)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="N -> D (in Ref. 2; AAF86342 and 4; AAF42969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 45538 MW; BCEE2259921D6D81 CRC64;
MRCAPTAGAA LVLCAATAGL LSAQGRPAQP EPPRFASWDE MNLLAHGLLQ LGHGLREHVE
RTRGQLGALE RRMAACGNAC QGPKGKDAPF KDSEDRVPEG QTPETLQSLQ TQLKAQNSKI
QQLFQKVAQQ QRYLSKQNLR IQNLQSQIDL LAPTHLDNGV DKTSRGKRLP KMTQLIGLTP
NATHLHRPPR DCQELFQEGE RHSGLFQIQP LGSPPFLVNC EMTSDGGWTV IQRRLNGSVD
FNQSWEAYKD GFGDPQGEFW LGLEKMHSIT GNRGSQLAVQ LQDWDGNAKL LQFPIHLGGE
DTAYSLQLTE PTANELGATN VSPNGLSLPF STWDQDHDLR GDLNCAKSLS GGWWFGTCSH
SNLNGQYFHS IPRQRQERKK GIFWKTWKGR YYPLQATTLL IQPMEATAAS
