ANGL4_PIG
ID ANGL4_PIG Reviewed; 412 AA.
AC Q2TNK5; Q1H5H6; Q7YS01;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Angiopoietin-related protein 4;
DE AltName: Full=Angiopoietin-like protein 4;
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=PGAR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Feng S., Yang Z.;
RT "Molecular cloning, expression pattern and chromosomal mapping of pig
RT ANGPTLs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adipose tissue;
RA Ren Z., Xiong Y.;
RT "Isolation and cloning pig angiopoietin-related protein gene.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 214-400.
RC TISSUE=White adipose tissue;
RA Ledoux S., Lord E., Palin M.-F., Murphy B.D.;
RT "Cloning of porcine PGAR from white adipose tissue.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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. May also play a role in
CC regulating glucose homeostasis and insulin sensitivity. Inhibits
CC proliferation, migration, and tubule formation of endothelial cells and
CC reduces vascular leakage (By similarity). Upon heterologous expression,
CC inhibits the adhesion of endothelial cell to the extracellular matrix
CC (ECM), and inhibits the reorganization of the actin cytoskeleton,
CC formation of actin stress fibers and focal adhesions in endothelial
CC cells that have adhered to ANGPTL4-containing ECM (in vitro) (By
CC similarity). Depending on context, may modulate tumor-related
CC angiogenesis (By similarity). {ECO:0000250|UniProtKB:Q9BY76,
CC ECO:0000250|UniProtKB:Q9Z1P8}.
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 (By similarity). 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:0000250|UniProtKB:Q9Z1P8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Z1P8}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:Q9BY76}. Note=The unprocessed form interacts
CC with the extracellular matrix. This may constitute a dynamic reservoir,
CC a regulatory mechanism of the bioavailability of ANGPTL4.
CC {ECO:0000250|UniProtKB:Q9BY76}.
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}.
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DR EMBL; AY751522; AAU93495.1; -; mRNA.
DR EMBL; AY974561; AAY43330.1; -; mRNA.
DR EMBL; AY307772; AAP74568.1; -; mRNA.
DR RefSeq; NP_001033733.1; NM_001038644.1.
DR AlphaFoldDB; Q2TNK5; -.
DR SMR; Q2TNK5; -.
DR STRING; 9823.ENSSSCP00000014452; -.
DR PaxDb; Q2TNK5; -.
DR PRIDE; Q2TNK5; -.
DR Ensembl; ENSSSCT00000014853; ENSSSCP00000014452; ENSSSCG00000013599.
DR Ensembl; ENSSSCT00005074066; ENSSSCP00005046449; ENSSSCG00005045799.
DR Ensembl; ENSSSCT00015103302; ENSSSCP00015043021; ENSSSCG00015076406.
DR Ensembl; ENSSSCT00025023650; ENSSSCP00025009921; ENSSSCG00025017424.
DR Ensembl; ENSSSCT00030024980; ENSSSCP00030011175; ENSSSCG00030018072.
DR Ensembl; ENSSSCT00035098512; ENSSSCP00035041623; ENSSSCG00035072751.
DR Ensembl; ENSSSCT00040003351; ENSSSCP00040001007; ENSSSCG00040002681.
DR Ensembl; ENSSSCT00045051597; ENSSSCP00045035890; ENSSSCG00045030125.
DR Ensembl; ENSSSCT00050052424; ENSSSCP00050022008; ENSSSCG00050038868.
DR Ensembl; ENSSSCT00055013699; ENSSSCP00055010785; ENSSSCG00055006995.
DR Ensembl; ENSSSCT00060031039; ENSSSCP00060013320; ENSSSCG00060022855.
DR Ensembl; ENSSSCT00065055752; ENSSSCP00065024233; ENSSSCG00065040760.
DR Ensembl; ENSSSCT00070050589; ENSSSCP00070042762; ENSSSCG00070025302.
DR GeneID; 397628; -.
DR KEGG; ssc:397628; -.
DR CTD; 51129; -.
DR VGNC; VGNC:85306; ANGPTL4.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000159478; -.
DR HOGENOM; CLU_038628_2_1_1; -.
DR InParanoid; Q2TNK5; -.
DR OMA; INCAKHL; -.
DR OrthoDB; 357340at2759; -.
DR TreeFam; TF329953; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000013599; Expressed in granulosa cell and 36 other tissues.
DR Genevisible; Q2TNK5; SS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IEA:Ensembl.
DR GO; GO:0043335; P:protein unfolding; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
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 2: Evidence at transcript 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..412
FT /note="Angiopoietin-related protein 4"
FT /id="PRO_0000278838"
FT CHAIN 24..170
FT /note="ANGPTL4 N-terminal chain"
FT /id="PRO_0000446863"
FT CHAIN 171..412
FT /note="ANGPTL4 C-terminal chain"
FT /id="PRO_0000446864"
FT DOMAIN 185..407
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 106..153
FT /evidence="ECO:0000255"
FT SITE 170..171
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9BY76"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 194..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 347..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 49
FT /note="L -> P (in Ref. 2; AAY43330)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="L -> P (in Ref. 1; AAU93495)"
FT /evidence="ECO:0000305"
FT CONFLICT 390..400
FT /note="RGRYYPLQATT -> QESNSIPPCAG (in Ref. 3; AAP74568)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="A -> V (in Ref. 1; AAU93495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 45534 MW; 0CF5443D641E3A41 CRC64;
MRSAPTARAA LVLCAATAGL LSAQGSPEPP EAPRFASWDE VNVLAHGLLQ LGRGLREHVE
RTRGQLGALE RRLSACGAAC KDPEGSAVPP LTAGNLVPSQ SDAAPETLHS LQTQLKAQNS
KIQQLFQKVA QQQRHLEKQH LRIQNLQGQL DHLAPMHLGH GVAKAARRKR LPKMTQPAGP
AHNISRLHRL PRDCQELFEE GERQSGLFQI QPQGSPPFLV NCKMTSDGGW TVIQRRQDGS
VDFNQPWEAY KDGFGDPKGE FWLGLEKVHR IMGDRGSRLA VQLQDWEGNA ESLQFPVHLG
GEDTAYSLQL TAPVASKLGA TIDTPSGLSL PFSTWDQDHD LRGDKNCAKI LSGGWWFGTC
SHSNLNGQYF HSIPRQREQR KKGIFWKTWR GRYYPLQATT MLIQPTVAEA AS
