Q9Y264 (ANGP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Angiopoietin-4
Short name=ANG-4

Alternative name(s):
Angiopoietin-3
Short name=ANG-3

Gene names

Name:	ANGPT4
Synonyms:	ANG3, ANG4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	503 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	Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis. Ref.5
Subunit structure	Homodimer; disulfide-linked. Interacts with TEK/TIE2. Ref.5
Subcellular location	Secreted Probable.
Tissue specificity	Highly expressed in the lung with much lower levels found in other tissues.
Sequence similarities	Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
Biological process	Angiogenesis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Coiled coil Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from direct assay. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome cellular response to hypoxia Inferred from expression pattern. Source: UniProtKB leukocyte migration Traceable author statement. Source: Reactome negative regulation of angiogenesis Inferred from direct assay. Source: UniProtKB negative regulation of blood vessel endothelial cell migration Inferred from direct assay. Source: UniProtKB positive regulation of angiogenesis Inferred from direct assay Ref.5. Source: UniProtKB positive regulation of blood vessel endothelial cell migration Inferred from direct assay Ref.5. Source: UniProtKB positive regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from direct assay. Source: UniProtKB
Molecular function	receptor tyrosine kinase binding Inferred from direct assay Ref.2. Source: UniProtKB transmembrane receptor protein tyrosine kinase activator activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 503	479	Angiopoietin-4		PRO_0000009116
Regions
	Domain	282 – 502	221	Fibrinogen C-terminal
	Coiled coil	84 – 238	155	Potential
Amino acid modifications
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	126	1	N-linked (GlcNAc...) Potential
	Glycosylation	140	1	N-linked (GlcNAc...) Potential
	Glycosylation	158	1	N-linked (GlcNAc...) Potential
	Glycosylation	247	1	N-linked (GlcNAc...) Potential
	Glycosylation	274	1	N-linked (GlcNAc...) Potential
	Glycosylation	311	1	N-linked (GlcNAc...) Potential
	Glycosylation	337	1	N-linked (GlcNAc...) Potential
	Glycosylation	427	1	N-linked (GlcNAc...) Potential
	Disulfide bond	291 ↔ 320		By similarity
	Disulfide bond	444 ↔ 457		By similarity
Natural variations
	Natural variant	395	1	E → K. Corresponds to variant rs869171 [ dbSNP | Ensembl ].		VAR_049070

Sequences

	Sequence		Length	Mass (Da)
	Q9Y264 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 79CE52F66B532340	FASTA	503	56,849
	10 20 30 40 50 60 MLSQLAMLQG SLLLVVATMS VAQQTRQEAD RGCETLVVQH GHCSYTFLLP KSEPCPPGPE 70 80 90 100 110 120 VSRDSNTLQR ESLANPLHLG KLPTQQVKQL EQALQNNTQW LKKLERAIKT ILRSKLEQVQ 130 140 150 160 170 180 QQMAQNQTAP MLELGTSLLN QTTAQIRKLT DMEAQLLNQT SRMDAQMPET FLSTNKLENQ 190 200 210 220 230 240 LLLQRQKLQQ LQGQNSALEK RLQALETKQQ EELASILSKK AKLLNTLSRQ SAALTNIERG 250 260 270 280 290 300 LRGVRHNSSL LQDQQHSLRQ LLVLLRHLVQ ERANASAPAF IMAGEQVFQD CAEIQRSGAS 310 320 330 340 350 360 ASGVYTIQVS NATKPRKVFC DLQSSGGRWT LIQRRENGTV NFQRNWKDYK QGFGDPAGEH 370 380 390 400 410 420 WLGNEVVHQL TRRAAYSLRV ELQDWEGHEA YAQYEHFHLG SENQLYRLSV VGYSGSAGRQ 430 440 450 460 470 480 SSLVLQNTSF STLDSDNDHC LCKCAQVMSG GWWFDACGLS NLNGVYYHAP DNKYKMDGIR 490 500 WHYFKGPSYS LRASRMMIRP LDI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Angiopoietin-3, a novel member of the angiopoietin family." Nishimura M., Miki T., Yashima R., Yokoi N., Yano H., Sato Y., Seino S. FEBS Lett. 448:254-256(1999) [PubMed: 10218486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Aorta.
[2]	"Angiopoietins 3 and 4: diverging gene counterparts in mice and humans." Valenzuela D.M., Griffiths J.A., Rojas J., Aldrich T.H., Jones P.F., Zhou H., McClain J., Copeland N.G., Gilbert D.J., Jenkins N.A., Huang T., Papadopoulos N., Maisonpierre P.C., Davis S., Yancopoulos G.D. Proc. Natl. Acad. Sci. U.S.A. 96:1904-1909(1999) [PubMed: 10051567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Biological characterization of angiopoietin-3 and angiopoietin-4." Lee H.J., Cho C.H., Hwang S.J., Choi H.H., Kim K.T., Ahn S.Y., Kim J.H., Oh J.L., Lee G.M., Koh G.Y. FASEB J. 18:1200-1208(2004) [PubMed: 15284220] [Abstract] Cited for: FUNCTION IN REGULATION OF ANGIOGENESIS; CELL SURVIVAL; CELL MIGRATION AND ACTIVATION OF AKT1, SUBUNIT, INTERACTION WITH TEK/TIE2.
[6]	"Control of vascular morphogenesis and homeostasis through the angiopoietin-Tie system." Augustin H.G., Koh G.Y., Thurston G., Alitalo K. Nat. Rev. Mol. Cell Biol. 10:165-177(2009) [PubMed: 19234476] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF074332 mRNA. Translation: AAD31728.1. AF113708 mRNA. Translation: AAD21587.1. AL161939, AL050325 Genomic DNA. Translation: CAC09933.2. AL050325, AL161939 Genomic DNA. Translation: CAI22922.1. BC111976 mRNA. Translation: AAI11977.1. BC111978 mRNA. Translation: AAI11979.1.
IPI	IPI00031775.
RefSeq	NP_057069.1. NM_015985.2.
UniGene	Hs.278973.
3D structure databases
ProteinModelPortal	Q9Y264.
SMR	Q9Y264. Positions 287-502.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y264. 1 interaction.
STRING	Q9Y264.
PTM databases
PhosphoSite	Q9Y264.
Polymorphism databases
DMDM	17433288.
Proteomic databases
PRIDE	Q9Y264.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381922; ENSP00000371347; ENSG00000101280.
GeneID	51378.
KEGG	hsa:51378.
UCSC	uc002wei.1. human.
Organism-specific databases
CTD	51378.
GeneCards	GC20M000853.
H-InvDB	HIX0040505.
HGNC	HGNC:487. ANGPT4.
HPA	CAB013260. CAB013305.
MIM	603705. gene.
neXtProt	NX_Q9Y264.
PharmGKB	PA24793.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10211.
GeneTree	ENSGT00560000076679.
HOGENOM	HBG444111.
HOVERGEN	HBG001644.
InParanoid	Q9Y264.
OMA	QGHELHR.
OrthoDB	EOG4640C3.
PhylomeDB	Q9Y264.
Enzyme and pathway databases
Pathway_Interaction_DB	angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q9Y264.
Bgee	Q9Y264.
CleanEx	HS_ANGPT4.
Genevestigator	Q9Y264.
GermOnline	ENSG00000101280. Homo sapiens.
Family and domain databases
InterPro	IPR002181. Fibrinogen_a/b/g_C. IPR014716. Fibrinogen_a/b/g_C_1. IPR014715. Fibrinogen_a/b/g_C_2. IPR020837. Fibrinogen_CS. [Graphical view]
Gene3D	G3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit. G3DSA:4.10.530.10. Fibrinogen_a/b/g_C_2. 1 hit.
KO	K05467.
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	54879.
SOURCE	Search...

Entry information

Entry name

ANGP4_HUMAN

Accession

Primary (citable) accession number: Q9Y264
Secondary accession number(s): Q5TFF4, Q9H4Z4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.