Angiopoietin-related protein 4 precursor

Contribute

Send feedback

Read comments (?) or add your own

Q6TMA8 (ANGL4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Angiopoietin-related protein 4

Alternative name(s):
Angiopoietin-like protein 4
Hepatic fibrinogen/angiopoietin-related protein
Short name=HFARP

Gene names

Name:

Angptl4

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.1
Subcellular location	Secreted. Secreted › extracellular space › extracellular 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.
Post-translational modification	N-glycosylated By similarity.
Sequence similarities	Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Cellular component	Extracellular matrix Secreted
Domain	Coiled coil Signal
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of lipoprotein lipase activity Traceable author statement Ref.1. Source: RGD protein homooligomerization Inferred from direct assay Ref.1. Source: RGD regulation of lipid metabolic process Traceable author statement PubMed 15863837. Source: RGD response to hypoxia Inferred from expression pattern PubMed 17033689. Source: RGD triglyceride homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	enzyme inhibitor activity Traceable author statement PubMed 15863837. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

Potential

Chain

24 – 405

382

Angiopoietin-related protein 4

PRO_0000009126

Regions

Domain

178 – 400

223

Fibrinogen C-terminal

Coiled coil

54 – 146

Potential

Amino acid modifications

Glycosylation

176

N-linked (GlcNAc...) Potential

Glycosylation

231

N-linked (GlcNAc...) Potential

Glycosylation

237

N-linked (GlcNAc...) Potential

Disulfide bond

187 ↔ 215

By similarity

Disulfide bond

340 ↔ 353

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6TMA8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3C54185DE5989E46
Show »

FASTA

405

44,951

        10         20         30         40         50         60 
MRCAPTAGAA LVLCAATAGL LSAQGRPAQP EPPRFASWDE MNLLAHGLLQ LGHGLREHVE 

        70         80         90        100        110        120 
RTRGQLGALE RRMAACGNAC QGPKGTDPKD RVPEGQAPET LQSLQTQLKA QNSKIQQLFQ 

       130        140        150        160        170        180 
KVAQQQRYLS KQNLRIQNLQ SQIDLLTPTH LDNGVDKTSR GKRLPKMAQL IGLTPNATRL 

       190        200        210        220        230        240 
HRPPRDCQEL FQEGERHSGL FQIQPLGSPP FLVNCEMTSD GGWTVIQRRL NGSVDFNQSW 

       250        260        270        280        290        300 
EAYKDGFGDP QGEFWLGLEK MHSITGDRGS QLAVQLQDWD GNAKLLQFPI HLGGEDTAYS 

       310        320        330        340        350        360 
LQLTEPTANE LGATNVSPNG LSLPFSTWDQ DHDLRGDLNC AKSLSGGWWF GTCSHSNLNG 

       370        380        390        400 
QYFHSIPRQR QQRKKGIFWK TWKGRYYPLQ ATTLLIQPME ATAAS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(2004) [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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY393999 mRNA. Translation: AAQ93383.1. BC078944 mRNA. Translation: AAH78944.1.
IPI	IPI00191550.
RefSeq	NP_954546.1. NM_199115.2.
UniGene	Rn.119611.
3D structure databases
ProteinModelPortal	Q6TMA8.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000010031.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010031; ENSRNOP00000010031; ENSRNOG00000007545.
GeneID	362850.
KEGG	rno:362850.
UCSC	RGD:735058. rat.
Organism-specific databases
CTD	51129.
RGD	735058. Angptl4.
Phylogenomic databases
eggNOG	NOG281759.
GeneTree	ENSGT00700000104197.
HOGENOM	HOG000015386.
HOVERGEN	HBG001644.
InParanoid	Q6TMA8.
KO	K08767.
OMA	VDFNRPW.
OrthoDB	EOG4Q58Q8.
Gene expression databases
Genevestigator	Q6TMA8.
GermOnline	ENSRNOG00000007545. Rattus norvegicus.
Family and domain databases
Gene3D	3.90.215.10. 1 hit. 4.10.530.10. 1 hit.
InterPro	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]
Pfam	PF00147. Fibrinogen_C. 1 hit. [Graphical view]
SMART	SM00186. FBG. 1 hit. [Graphical view]
SUPFAM	SSF56496. Fibrinogen_a/b/g_C. 1 hit.
PROSITE	PS00514. FIBRINOGEN_C_1. 1 hit. PS51406. FIBRINOGEN_C_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	681522.

Entry information

Entry name

ANGL4_RAT

Accession

Primary (citable) accession number: Q6TMA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents