ANGL4_BOVIN
ID ANGL4_BOVIN Reviewed; 410 AA.
AC Q2KJ51;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ma Y., Xu S.-Z., Zhang Y.-H., Gao X., Ren H.-Y., Xin Y.-P., Gao S.-X.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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; DQ355521; ABC84490.1; -; mRNA.
DR EMBL; BC105516; AAI05517.1; -; mRNA.
DR RefSeq; NP_001039508.1; NM_001046043.2.
DR AlphaFoldDB; Q2KJ51; -.
DR SMR; Q2KJ51; -.
DR STRING; 9913.ENSBTAP00000003204; -.
DR PaxDb; Q2KJ51; -.
DR PRIDE; Q2KJ51; -.
DR Ensembl; ENSBTAT00000003204; ENSBTAP00000003204; ENSBTAG00000002473.
DR GeneID; 509963; -.
DR KEGG; bta:509963; -.
DR CTD; 51129; -.
DR VEuPathDB; HostDB:ENSBTAG00000002473; -.
DR VGNC; VGNC:25893; ANGPTL4.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000159478; -.
DR HOGENOM; CLU_038628_2_1_1; -.
DR InParanoid; Q2KJ51; -.
DR OMA; INCAKHL; -.
DR OrthoDB; 357340at2759; -.
DR TreeFam; TF329953; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000002473; Expressed in bone marrow and 104 other tissues.
DR ExpressionAtlas; Q2KJ51; baseline and differential.
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..410
FT /note="Angiopoietin-related protein 4"
FT /id="PRO_0000244421"
FT CHAIN 24..171
FT /note="ANGPTL4 N-terminal chain"
FT /id="PRO_0000446857"
FT CHAIN 172..410
FT /note="ANGPTL4 C-terminal chain"
FT /id="PRO_0000446858"
FT DOMAIN 186..408
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 81..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..155
FT /evidence="ECO:0000255"
FT SITE 171..172
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9BY76"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 195..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 348..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 410 AA; 45553 MW; 932B5F43B268EC19 CRC64;
MRCAPTAGAA LMLCAATAGL LSAQGRPEPP ETPRFASWDE VNVLAHGLLQ LGHGLREHVE
RTRGQLGELE RRLGACGAAC KDPEGSAAPP RAQANLVNPG GGDASPETLR SLKTQLEAQN
SRIQQLFQKV AQQQRHLEKQ QLRIQNLQSQ MDHLAPRHLG HEMAKPARRK RLPKMAQLAG
PAHNISRLHR LPRDCQELFE EGERESGLFQ IQPQGSPPFL VNCKMTSDGG WTVIQRRQDG
SVDFNQPWEA YKDGFGDPQG EFWLGLEKVH HILGDRGSRL AVQLQDWEGN AESLQFPIHL
GGEDTAYSLQ LTPPVASKLG ATTFSPSGLS LPFSTWDQDH DLRGDKNCAR SLSGGWWFGT
CSHSNLNGQY FHSIPRQRQQ RKKGIFWKTW RGRYYPLQAT TILVQPTAAS
