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Protein

Angiopoietin-related protein 4

Gene

Angptl4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein with hypoxia-induced expression in endothelial cells. May act as a regulator of angiogenesis and modulate tumorigenesis. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. May exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation (By similarity).By similarity

GO - Molecular functioni

  1. enzyme inhibitor activity Source: RGD

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. negative regulation of catalytic activity Source: RGD
  4. negative regulation of endothelial cell apoptotic process Source: Ensembl
  5. negative regulation of lipoprotein lipase activity Source: RGD
  6. protein homooligomerization Source: RGD
  7. protein oligomerization Source: RGD
  8. regulation of lipid metabolic process Source: RGD
  9. response to hypoxia Source: RGD
  10. triglyceride homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-related protein 4
Alternative name(s):
Angiopoietin-like protein 4
Hepatic fibrinogen/angiopoietin-related protein
Short name:
HFARP
Gene namesi
Name:Angptl4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi735058. Angptl4.

Subcellular locationi

Secreted. Secretedextracellular spaceextracellular matrix
Note: The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (By similarity).By similarity

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 405382Angiopoietin-related protein 4PRO_0000009126Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi187 ↔ 215PROSITE-ProRule annotation
Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi340 ↔ 353PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Gene expression databases

GenevestigatoriQ6TMA8.

Interactioni

Subunit structurei

Homooligomer. The homooligomer undergoes proteolytic processing to release its carboxyl fibrinogen-like domain, which circulates as a monomer. The homooligomer unprocessed form is able to interact with the extracellular matrix (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010031.

Structurei

3D structure databases

ProteinModelPortaliQ6TMA8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 400223Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili54 – 14693Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG281759.
GeneTreeiENSGT00770000120463.
HOGENOMiHOG000015386.
HOVERGENiHBG001644.
InParanoidiQ6TMA8.
KOiK08767.
OMAiLPKMAQL.
OrthoDBiEOG7X9G60.
PhylomeDBiQ6TMA8.
TreeFamiTF329953.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR028793. ANGPTL4.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PANTHERiPTHR19143:SF16. PTHR19143:SF16. 1 hit.
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6TMA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCAPTAGAA LVLCAATAGL LSAQGRPAQP EPPRFASWDE MNLLAHGLLQ
60 70 80 90 100
LGHGLREHVE RTRGQLGALE RRMAACGNAC QGPKGTDPKD RVPEGQAPET
110 120 130 140 150
LQSLQTQLKA QNSKIQQLFQ KVAQQQRYLS KQNLRIQNLQ SQIDLLTPTH
160 170 180 190 200
LDNGVDKTSR GKRLPKMAQL IGLTPNATRL HRPPRDCQEL FQEGERHSGL
210 220 230 240 250
FQIQPLGSPP FLVNCEMTSD GGWTVIQRRL NGSVDFNQSW EAYKDGFGDP
260 270 280 290 300
QGEFWLGLEK MHSITGDRGS QLAVQLQDWD GNAKLLQFPI HLGGEDTAYS
310 320 330 340 350
LQLTEPTANE LGATNVSPNG LSLPFSTWDQ DHDLRGDLNC AKSLSGGWWF
360 370 380 390 400
GTCSHSNLNG QYFHSIPRQR QQRKKGIFWK TWKGRYYPLQ ATTLLIQPME

ATAAS
Length:405
Mass (Da):44,951
Last modified:July 4, 2004 - v1
Checksum:i3C54185DE5989E46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY393999 mRNA. Translation: AAQ93383.1.
BC078944 mRNA. Translation: AAH78944.1.
RefSeqiNP_954546.1. NM_199115.2.
UniGeneiRn.119611.

Genome annotation databases

EnsembliENSRNOT00000010031; ENSRNOP00000010031; ENSRNOG00000007545.
GeneIDi362850.
KEGGirno:362850.
UCSCiRGD:735058. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY393999 mRNA. Translation: AAQ93383.1.
BC078944 mRNA. Translation: AAH78944.1.
RefSeqiNP_954546.1. NM_199115.2.
UniGeneiRn.119611.

3D structure databases

ProteinModelPortaliQ6TMA8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010031; ENSRNOP00000010031; ENSRNOG00000007545.
GeneIDi362850.
KEGGirno:362850.
UCSCiRGD:735058. rat.

Organism-specific databases

CTDi51129.
RGDi735058. Angptl4.

Phylogenomic databases

eggNOGiNOG281759.
GeneTreeiENSGT00770000120463.
HOGENOMiHOG000015386.
HOVERGENiHBG001644.
InParanoidiQ6TMA8.
KOiK08767.
OMAiLPKMAQL.
OrthoDBiEOG7X9G60.
PhylomeDBiQ6TMA8.
TreeFamiTF329953.

Miscellaneous databases

NextBioi681522.
PROiQ6TMA8.

Gene expression databases

GenevestigatoriQ6TMA8.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR028793. ANGPTL4.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PANTHERiPTHR19143:SF16. PTHR19143:SF16. 1 hit.
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Oligomerization and regulated proteolytic processing of angiopoietin-like protein 4."
    Ge H., Yang G., Huang L., Motola D.L., Pourbahrami T., Li C.
    J. Biol. Chem. 279:2038-2045(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    Strain: Wistar.
    Tissue: Adipose tissue.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiANGL4_RAT
AccessioniPrimary (citable) accession number: Q6TMA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2005
Last sequence update: July 4, 2004
Last modified: March 31, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.