Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Angiopoietin-1

Gene

Angpt1

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

Functioni

Binds and activates TIE2 receptor by inducing its tyrosine phosphorylation. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Mediates blood vessel maturation/stability. It may play an important role in the heart early development.

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • glomerulus vasculature development Source: UniProtKB
  • negative regulation of apoptotic process Source: RGD
  • organ regeneration Source: RGD
  • ovarian follicle development Source: RGD
  • protein homooligomerization Source: RGD
  • response to estrogen Source: RGD
  • response to hypoxia Source: RGD
  • response to vitamin B3 Source: RGD
  • Tie signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-1
Short name:
ANG-1
Gene namesi
Name:Angpt1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628896. Angpt1.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 497478Angiopoietin-1PRO_0000009112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence analysis
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence analysis
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence analysis
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi285 ↔ 314PROSITE-ProRule annotation
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence analysis
Disulfide bondi438 ↔ 451PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO35460.
PRIDEiO35460.

PTM databases

PhosphoSiteiO35460.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007979.

Structurei

3D structure databases

ProteinModelPortaliO35460.
SMRiO35460. Positions 282-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini276 – 496221Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili81 – 11939Sequence analysisAdd
BLAST
Coiled coili153 – 261109Sequence analysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiO35460.
KOiK05465.
PhylomeDBiO35460.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR028843. Ang-1.
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:SF156. PTHR19143:SF156. 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.

O35460-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVFLSFAFF AAILTHIGCS NQRRSPENGG RRYNRIQHGQ CAYTFILPEH
60 70 80 90 100
DGNCRESATE QYNTNALQRD APHVETDFSS QKLQHLEHVM ENYTQWLQKL
110 120 130 140 150
ENYIVENMKS EMAQIQQNAV QNHTATMLEI GTSLLSQTAE QTRKLTDVET
160 170 180 190 200
QVLNQTSRLE IQLLENSLST YELEKQLLQQ TNEILKIQEK NSLLEHKILE
210 220 230 240 250
MEGKHKEELD TLKEEKENLQ GLVTRQTFII QELEKQLSRA TSNNSVLQKQ
260 270 280 290 300
QLELMDTVHN LVSLCTKEVL LKGGKREEEK PFRDCADVYQ AGFNKSGIYT
310 320 330 340 350
IYFNNMPEPK KVFCNMDVNE GGWTVIQHRE DGSLDFQRGW KEYKMGFGNP
360 370 380 390 400
SGEYWLGNEF IFAITSQRQY MLRIELMDWE GNRAYSQYDR FHIGNQKQNY
410 420 430 440 450
RLYLKGHTGT AGKQSSLILH GADFSTKDAD NDNCMCKCAL MLTGGWWFDA
460 470 480 490
CGPSNLNGMF YTAGQNHGKL NGIKWHYFKG PSYSLRSTTM MIRPLDF
Length:497
Mass (Da):57,461
Last modified:November 8, 2002 - v2
Checksum:i08E66AEBEFD868AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981Q → E in AAC78246 (PubMed:9776732).Curated
Sequence conflicti172 – 1721E → K in AAC78246 (PubMed:9776732).Curated
Sequence conflicti189 – 1891E → K in AAC78246 (PubMed:9776732).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB080023 mRNA. Translation: BAC10290.1.
AF030376 mRNA. Translation: AAC78246.1.
RefSeqiNP_445998.1. NM_053546.1.
UniGeneiRn.161953.

Genome annotation databases

GeneIDi89807.
KEGGirno:89807.
UCSCiRGD:628896. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB080023 mRNA. Translation: BAC10290.1.
AF030376 mRNA. Translation: AAC78246.1.
RefSeqiNP_445998.1. NM_053546.1.
UniGeneiRn.161953.

3D structure databases

ProteinModelPortaliO35460.
SMRiO35460. Positions 282-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007979.

PTM databases

PhosphoSiteiO35460.

Proteomic databases

PaxDbiO35460.
PRIDEiO35460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi89807.
KEGGirno:89807.
UCSCiRGD:628896. rat.

Organism-specific databases

CTDi284.
RGDi628896. Angpt1.

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiO35460.
KOiK05465.
PhylomeDBiO35460.

Miscellaneous databases

NextBioi617664.
PROiO35460.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR028843. Ang-1.
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:SF156. PTHR19143:SF156. 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

  1. "Augmented expression of the tight junction protein occludin in brain endothelial cell line TR-bBB by rat angiopoietin-1 expressed in baculovirus-infected sf plus insect cells."
    Iizasa H., Bae S.H., Asashima T., Kitano T., Matsunaga N., Terasaki T., Kang Y.S., Nakashima E.
    Pharm. Res. 19:1757-1760(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Placenta.
  2. "Regulation of angiopoietin-2 mRNA levels in bovine microvascular endothelial cells by cytokines and hypoxia."
    Mandriota S.J., Pepper M.S.
    Circ. Res. 83:852-859(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-200.
    Strain: Sprague-Dawley.
    Tissue: Placenta.

Entry informationi

Entry nameiANGP1_RAT
AccessioniPrimary (citable) accession number: O35460
Secondary accession number(s): Q8K4Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 8, 2002
Last modified: November 11, 2015
This is version 104 of the entry and version 2 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

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 one 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.