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Q6TMA8

- ANGL4_RAT

UniProt

Q6TMA8 - ANGL4_RAT

Protein

Angiopoietin-related protein 4

Gene

Angptl4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Enzyme and pathway databases

    ReactomeiREACT_196408. PPARA activates gene expression.

    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: 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. extracellular space Source: InterPro
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    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.
    GeneTreeiENSGT00750000117415.
    HOGENOMiHOG000015386.
    HOVERGENiHBG001644.
    InParanoidiQ6TMA8.
    KOiK08767.
    OMAiVDFNRPW.
    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

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    MRCAPTAGAA LVLCAATAGL LSAQGRPAQP EPPRFASWDE MNLLAHGLLQ    50
    LGHGLREHVE RTRGQLGALE RRMAACGNAC QGPKGTDPKD RVPEGQAPET 100
    LQSLQTQLKA QNSKIQQLFQ KVAQQQRYLS KQNLRIQNLQ SQIDLLTPTH 150
    LDNGVDKTSR GKRLPKMAQL IGLTPNATRL HRPPRDCQEL FQEGERHSGL 200
    FQIQPLGSPP FLVNCEMTSD GGWTVIQRRL NGSVDFNQSW EAYKDGFGDP 250
    QGEFWLGLEK MHSITGDRGS QLAVQLQDWD GNAKLLQFPI HLGGEDTAYS 300
    LQLTEPTANE LGATNVSPNG LSLPFSTWDQ DHDLRGDLNC AKSLSGGWWF 350
    GTCSHSNLNG QYFHSIPRQR QQRKKGIFWK TWKGRYYPLQ ATTLLIQPME 400
    ATAAS 405
    Length:405
    Mass (Da):44,951
    Last modified:July 5, 2004 - v1
    Checksum:i3C54185DE5989E46
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY393999 mRNA. Translation: AAQ93383.1 .
    BC078944 mRNA. Translation: AAH78944.1 .
    RefSeqi NP_954546.1. NM_199115.2.
    UniGenei Rn.119611.

    3D structure databases

    ProteinModelPortali Q6TMA8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000010031.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000010031 ; ENSRNOP00000010031 ; ENSRNOG00000007545 .
    GeneIDi 362850.
    KEGGi rno:362850.
    UCSCi RGD:735058. rat.

    Organism-specific databases

    CTDi 51129.
    RGDi 735058. Angptl4.

    Phylogenomic databases

    eggNOGi NOG281759.
    GeneTreei ENSGT00750000117415.
    HOGENOMi HOG000015386.
    HOVERGENi HBG001644.
    InParanoidi Q6TMA8.
    KOi K08767.
    OMAi VDFNRPW.
    OrthoDBi EOG7X9G60.
    PhylomeDBi Q6TMA8.
    TreeFami TF329953.

    Enzyme and pathway databases

    Reactomei REACT_196408. PPARA activates gene expression.

    Miscellaneous databases

    NextBioi 681522.
    PROi Q6TMA8.

    Gene expression databases

    Genevestigatori Q6TMA8.

    Family and domain databases

    Gene3Di 3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProi IPR028793. 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 ]
    PANTHERi PTHR19143:SF16. PTHR19143:SF16. 1 hit.
    Pfami PF00147. Fibrinogen_C. 1 hit.
    [Graphical view ]
    SMARTi SM00186. FBG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56496. SSF56496. 1 hit.
    PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiANGL4_RAT
    AccessioniPrimary (citable) accession number: Q6TMA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 84 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