ANGP1_HUMAN
ID ANGP1_HUMAN Reviewed; 498 AA.
AC Q15389; Q5HYA0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Angiopoietin-1;
DE Short=ANG-1;
DE Flags: Precursor;
GN Name=ANGPT1; Synonyms=KIAA0003;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal lung;
RX PubMed=8980223; DOI=10.1016/s0092-8674(00)81812-7;
RA Davis S., Aldrich T.H., Jones P.F., Acheson A., Compton D.L., Jain V.,
RA Ryan T.E., Bruno J., Radziejewski C., Maisonpierre P.C., Yancopoulos G.D.;
RT "Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-
RT trap expression cloning.";
RL Cell 87:1161-1169(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Nakatsukasa M., Komai K., Shiozawa S.;
RT "Human angiopoietin-1 mRNA variant form.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Shan Z.X., Yu X.Y., Lin Q.Y., Fu Y.H., Tan H.H., Zheng M., Lin S.G.;
RT "Human angiopoietin-1 mRNA variant forms.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH TEK.
RX PubMed=9204896; DOI=10.1126/science.277.5322.55;
RA Maisonpierre P.C., Suri C., Jones P.F., Bartunkova S., Wiegand S.J.,
RA Radziejewski C., Compton D.L., McClain J., Aldrich T.H., Papadopoulos N.,
RA Daly T.J., Davis S., Sato T.N., Yancopoulos G.D.;
RT "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo
RT angiogenesis.";
RL Science 277:55-60(1997).
RN [11]
RP INTERACTION WITH TEK.
RX PubMed=12427764; DOI=10.1074/jbc.m208550200;
RA Fiedler U., Krissl T., Koidl S., Weiss C., Koblizek T., Deutsch U.,
RA Martiny-Baron G., Marme D., Augustin H.G.;
RT "Angiopoietin-1 and angiopoietin-2 share the same binding domains in the
RT Tie-2 receptor involving the first Ig-like loop and the epidermal growth
RT factor-like repeats.";
RL J. Biol. Chem. 278:1721-1727(2003).
RN [12]
RP FUNCTION IN REGULATION OF ANGIOGENESIS; CELL SURVIVAL; CELL MIGRATION AND
RP ACTIVATION OF AKT1, AND INTERACTION WITH TEK/TIE2.
RX PubMed=15284220; DOI=10.1096/fj.03-1466com;
RA Lee H.J., Cho C.H., Hwang S.J., Choi H.H., Kim K.T., Ahn S.Y., Kim J.H.,
RA Oh J.L., Lee G.M., Koh G.Y.;
RT "Biological characterization of angiopoietin-3 and angiopoietin-4.";
RL FASEB J. 18:1200-1208(2004).
RN [13]
RP FUNCTION IN REGULATION OF ENDOTHELIAL CELL MIGRATION AND CELL SPREADING.
RX PubMed=18425120; DOI=10.1038/ncb1714;
RA Fukuhara S., Sako K., Minami T., Noda K., Kim H.Z., Kodama T., Shibuya M.,
RA Takakura N., Koh G.Y., Mochizuki N.;
RT "Differential function of Tie2 at cell-cell contacts and cell-substratum
RT contacts regulated by angiopoietin-1.";
RL Nat. Cell Biol. 10:513-526(2008).
RN [14]
RP FUNCTION IN REGULATION OF ENDOTHELIAL CELL MIGRATION.
RX PubMed=18425119; DOI=10.1038/ncb1715;
RA Saharinen P., Eklund L., Miettinen J., Wirkkala R., Anisimov A.,
RA Winderlich M., Nottebaum A., Vestweber D., Deutsch U., Koh G.Y.,
RA Olsen B.R., Alitalo K.;
RT "Angiopoietins assemble distinct Tie2 signalling complexes in endothelial
RT cell-cell and cell-matrix contacts.";
RL Nat. Cell Biol. 10:527-537(2008).
RN [15]
RP REVIEW.
RX PubMed=19234476; DOI=10.1038/nrm2639;
RA Augustin H.G., Koh G.Y., Thurston G., Alitalo K.;
RT "Control of vascular morphogenesis and homeostasis through the
RT angiopoietin-Tie system.";
RL Nat. Rev. Mol. Cell Biol. 10:165-177(2009).
RN [16]
RP REVIEW.
RX PubMed=20054809; DOI=10.14670/hh-25.387;
RA Fukuhara S., Sako K., Noda K., Zhang J., Minami M., Mochizuki N.;
RT "Angiopoietin-1/Tie2 receptor signaling in vascular quiescence and
RT angiogenesis.";
RL Histol. Histopathol. 25:387-396(2010).
RN [17]
RP REVIEW.
RX PubMed=20651738; DOI=10.1038/nrc2894;
RA Huang H., Bhat A., Woodnutt G., Lappe R.;
RT "Targeting the ANGPT-TIE2 pathway in malignancy.";
RL Nat. Rev. Cancer 10:575-585(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP VARIANTS HAE5 SER-119; CYS-225 AND GLN-494, INVOLVEMENT IN HAE5, SUBUNIT,
RP INTERACTION WITH TEK, AND CHARACTERIZATION OF VARIANTS HAE5 SER-119;
RP CYS-225 AND GLN-494.
RX PubMed=28601681; DOI=10.1016/j.jaci.2017.05.020;
RA Bafunno V., Firinu D., D'Apolito M., Cordisco G., Loffredo S., Leccese A.,
RA Bova M., Barca M.P., Santacroce R., Cicardi M., Del Giacco S.,
RA Margaglione M.;
RT "Mutation of the angiopoietin-1 gene (ANGPT1) associates with a new type of
RT hereditary angioedema.";
RL J. Allergy Clin. Immunol. 141:1009-1017(2018).
RN [20]
RP VARIANT HAE5 SER-119, FUNCTION, INTERACTION WITH TEK, AND CHARACTERIZATION
RP OF VARIANT HAE5 SER-119.
RX PubMed=30689269; DOI=10.1111/cea.13349;
RA d'Apolito M., Santacroce R., Colia A.L., Cordisco G., Maffione A.B.,
RA Margaglione M.;
RT "Angiopoietin-1 haploinsufficiency affects the endothelial barrier and
RT causes hereditary angioedema.";
RL Clin. Exp. Allergy 49:626-635(2019).
CC -!- FUNCTION: Binds and activates TEK/TIE2 receptor by inducing its
CC dimerization and tyrosine phosphorylation. Plays an important role in
CC the regulation of angiogenesis, endothelial cell survival,
CC proliferation, migration, adhesion and cell spreading, reorganization
CC of the actin cytoskeleton, but also maintenance of vascular quiescence.
CC Required for normal angiogenesis and heart development during
CC embryogenesis. After birth, activates or inhibits angiogenesis,
CC depending on the context. Inhibits angiogenesis and promotes vascular
CC stability in quiescent vessels, where endothelial cells have tight
CC contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-
CC cell contacts, forming complexes with TEK molecules from adjoining
CC cells, and this leads to preferential activation of
CC phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In
CC migrating endothelial cells that lack cell-cell adhesions, ANGT1
CC recruits TEK to contacts with the extracellular matrix, leading to the
CC formation of focal adhesion complexes, activation of PTK2/FAK and of
CC the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the
CC stimulation of sprouting angiogenesis. Mediates blood vessel
CC maturation/stability. Implicated in endothelial developmental processes
CC later and distinct from that of VEGF. Appears to play a crucial role in
CC mediating reciprocal interactions between the endothelium and
CC surrounding matrix and mesenchyme. {ECO:0000269|PubMed:15284220,
CC ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120,
CC ECO:0000269|PubMed:30689269, ECO:0000269|PubMed:9204896}.
CC -!- SUBUNIT: Homooligomer (PubMed:28601681). Interacts with TEK/TIE2
CC (PubMed:28601681, PubMed:30689269). {ECO:0000269|PubMed:12427764,
CC ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:28601681,
CC ECO:0000269|PubMed:30689269, ECO:0000269|PubMed:9204896}.
CC -!- INTERACTION:
CC Q15389; Q15389: ANGPT1; NbExp=3; IntAct=EBI-2922365, EBI-2922365;
CC Q15389; Q02763: TEK; NbExp=2; IntAct=EBI-2922365, EBI-2257090;
CC Q15389-2; Q13387: MAPK8IP2; NbExp=3; IntAct=EBI-10692491, EBI-722813;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15389-1; Sequence=Displayed;
CC Name=2; Synonyms=Gly-269 del;
CC IsoId=Q15389-2; Sequence=VSP_046324;
CC -!- PTM: Glycosylated.
CC -!- DISEASE: Angioedema, hereditary, 5 (HAE5) [MIM:619361]: A form of
CC angioedema, a disorder characterized by episodic local swelling
CC involving subcutaneous or submucous tissue of the upper respiratory and
CC gastrointestinal tracts, face, extremities, and genitalia. HAE5 is an
CC autosomal dominant form characterized by onset of episodic swelling of
CC the face, lips, hands, and abdomen in the second decade of life.
CC {ECO:0000269|PubMed:28601681, ECO:0000269|PubMed:30689269}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: It may have a potential therapeutic utility since it can
CC be used for specifically targeting tumor vasculature or for promoting
CC angiogenic processes in certain organs such as an ischemic heart.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02793.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Angiopoietin entry;
CC URL="https://en.wikipedia.org/wiki/Angiopoietin";
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DR EMBL; U83508; AAB50557.1; -; mRNA.
DR EMBL; AB084454; BAB91325.1; -; mRNA.
DR EMBL; AY121504; AAM81745.1; -; mRNA.
DR EMBL; AY124380; AAM92271.1; -; mRNA.
DR EMBL; D13628; BAA02793.2; ALT_INIT; mRNA.
DR EMBL; BX648814; CAI45984.1; -; mRNA.
DR EMBL; AC091010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91909.1; -; Genomic_DNA.
DR EMBL; BC152411; AAI52412.1; -; mRNA.
DR EMBL; BC152419; AAI52420.1; -; mRNA.
DR CCDS; CCDS56551.1; -. [Q15389-2]
DR CCDS; CCDS6306.1; -. [Q15389-1]
DR RefSeq; NP_001137.2; NM_001146.4. [Q15389-1]
DR RefSeq; NP_001186788.1; NM_001199859.2. [Q15389-2]
DR RefSeq; NP_001300980.1; NM_001314051.1.
DR PDB; 4EPU; X-ray; 2.10 A; A/B=282-497.
DR PDB; 4JYO; X-ray; 2.50 A; X=280-498.
DR PDB; 4K0V; X-ray; 4.51 A; B=280-498.
DR PDBsum; 4EPU; -.
DR PDBsum; 4JYO; -.
DR PDBsum; 4K0V; -.
DR AlphaFoldDB; Q15389; -.
DR SMR; Q15389; -.
DR BioGRID; 106781; 7.
DR IntAct; Q15389; 3.
DR MINT; Q15389; -.
DR STRING; 9606.ENSP00000428340; -.
DR ChEMBL; CHEMBL3217395; -.
DR GlyGen; Q15389; 5 sites.
DR iPTMnet; Q15389; -.
DR PhosphoSitePlus; Q15389; -.
DR BioMuta; ANGPT1; -.
DR DMDM; 12229574; -.
DR EPD; Q15389; -.
DR jPOST; Q15389; -.
DR MassIVE; Q15389; -.
DR PaxDb; Q15389; -.
DR PeptideAtlas; Q15389; -.
DR PRIDE; Q15389; -.
DR ProteomicsDB; 60559; -. [Q15389-1]
DR ABCD; Q15389; 3 sequenced antibodies.
DR Antibodypedia; 4501; 694 antibodies from 40 providers.
DR DNASU; 284; -.
DR Ensembl; ENST00000297450.7; ENSP00000297450.3; ENSG00000154188.10. [Q15389-2]
DR Ensembl; ENST00000517746.6; ENSP00000428340.1; ENSG00000154188.10. [Q15389-1]
DR GeneID; 284; -.
DR KEGG; hsa:284; -.
DR MANE-Select; ENST00000517746.6; ENSP00000428340.1; NM_001146.5; NP_001137.2.
DR UCSC; uc003ymn.4; human. [Q15389-1]
DR CTD; 284; -.
DR DisGeNET; 284; -.
DR GeneCards; ANGPT1; -.
DR HGNC; HGNC:484; ANGPT1.
DR HPA; ENSG00000154188; Tissue enhanced (seminal).
DR MalaCards; ANGPT1; -.
DR MIM; 601667; gene.
DR MIM; 619361; phenotype.
DR neXtProt; NX_Q15389; -.
DR OpenTargets; ENSG00000154188; -.
DR Orphanet; 599418; Hereditary angioedema with normal C1Inh not related to F12 or PLG variant.
DR PharmGKB; PA24791; -.
DR VEuPathDB; HostDB:ENSG00000154188; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158117; -.
DR HOGENOM; CLU_038628_3_1_1; -.
DR InParanoid; Q15389; -.
DR OMA; QAFSQYD; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; Q15389; -.
DR TreeFam; TF336658; -.
DR PathwayCommons; Q15389; -.
DR Reactome; R-HSA-210993; Tie2 Signaling.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR SignaLink; Q15389; -.
DR SIGNOR; Q15389; -.
DR BioGRID-ORCS; 284; 8 hits in 1043 CRISPR screens.
DR ChiTaRS; ANGPT1; human.
DR GeneWiki; Angiopoietin_1; -.
DR GenomeRNAi; 284; -.
DR Pharos; Q15389; Tbio.
DR PRO; PR:Q15389; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15389; protein.
DR Bgee; ENSG00000154188; Expressed in lower lobe of lung and 171 other tissues.
DR ExpressionAtlas; Q15389; baseline and differential.
DR Genevisible; Q15389; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0072012; P:glomerulus vasculature development; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0030210; P:heparin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:UniProtKB.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IMP:ARUK-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:2000446; P:regulation of macrophage migration inhibitory factor signaling pathway; IEA:Ensembl.
DR GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IDA:UniProtKB.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0002040; P:sprouting angiogenesis; IDA:UniProtKB.
DR GO; GO:0048014; P:Tie signaling pathway; IDA:UniProtKB.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR028843; Ang-1.
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:SF156; PTHR19143:SF156; 1.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Coiled coil;
KW Developmental protein; Differentiation; Disease variant; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..498
FT /note="Angiopoietin-1"
FT /id="PRO_0000009110"
FT DOMAIN 277..497
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 81..119
FT /evidence="ECO:0000255"
FT COILED 153..261
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 439..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8980223, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_046324"
FT VARIANT 119
FT /note="A -> S (in HAE5; decreased oligomerization;
FT decreased interaction with TEK; fails to form proper cell-
FT cell adhesions in an in vitro model of endothelial cell
FT barrier)"
FT /evidence="ECO:0000269|PubMed:28601681,
FT ECO:0000269|PubMed:30689269"
FT /id="VAR_085814"
FT VARIANT 225
FT /note="R -> C (in HAE5; unknown pathological significance;
FT does not affect oligomerization; does not affect
FT interaction with TEK)"
FT /evidence="ECO:0000269|PubMed:28601681"
FT /id="VAR_085815"
FT VARIANT 247
FT /note="L -> P (in dbSNP:rs73701083)"
FT /id="VAR_069165"
FT VARIANT 494
FT /note="R -> Q (in HAE5; unknown pathological significance;
FT does not affect oligomerization; does not affect
FT interaction with TEK)"
FT /evidence="ECO:0000269|PubMed:28601681"
FT /id="VAR_085816"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:4EPU"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 324..333
FT /evidence="ECO:0007829|PDB:4EPU"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:4EPU"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 384..394
FT /evidence="ECO:0007829|PDB:4EPU"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:4EPU"
FT HELIX 439..443
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:4EPU"
FT TURN 463..467
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:4EPU"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:4EPU"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:4EPU"
SQ SEQUENCE 498 AA; 57513 MW; 5D5FA63AEF6BE920 CRC64;
MTVFLSFAFL AAILTHIGCS NQRRSPENSG RRYNRIQHGQ CAYTFILPEH DGNCRESTTD
QYNTNALQRD APHVEPDFSS QKLQHLEHVM ENYTQWLQKL ENYIVENMKS EMAQIQQNAV
QNHTATMLEI GTSLLSQTAE QTRKLTDVET QVLNQTSRLE IQLLENSLST YKLEKQLLQQ
TNEILKIHEK NSLLEHKILE MEGKHKEELD TLKEEKENLQ GLVTRQTYII QELEKQLNRA
TTNNSVLQKQ QLELMDTVHN LVNLCTKEGV LLKGGKREEE KPFRDCADVY QAGFNKSGIY
TIYINNMPEP KKVFCNMDVN GGGWTVIQHR EDGSLDFQRG WKEYKMGFGN PSGEYWLGNE
FIFAITSQRQ YMLRIELMDW EGNRAYSQYD RFHIGNEKQN YRLYLKGHTG TAGKQSSLIL
HGADFSTKDA DNDNCMCKCA LMLTGGWWFD ACGPSNLNGM FYTAGQNHGK LNGIKWHYFK
GPSYSLRSTT MMIRPLDF
