ANGP4_MOUSE
ID ANGP4_MOUSE Reviewed; 509 AA.
AC Q9WVH6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Angiopoietin-4;
DE Short=ANG-4;
DE AltName: Full=Angiopoietin-3;
DE Short=ANG-3;
DE Flags: Precursor;
GN Name=Angpt4; Synonyms=Agpt4, Ang3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Myoblast, and Uterus;
RX PubMed=10051567; DOI=10.1073/pnas.96.5.1904;
RA Valenzuela D.M., Griffiths J.A., Rojas J., Aldrich T.H., Jones P.F.,
RA Zhou H., McClain J., Copeland N.G., Gilbert D.J., Jenkins N.A., Huang T.,
RA Papadopoulos N., Maisonpierre P.C., Davis S., Yancopoulos G.D.;
RT "Angiopoietins 3 and 4: diverging gene counterparts in mice and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1904-1909(1999).
RN [2]
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).
CC -!- FUNCTION: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce
CC tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell
CC survival, migration and angiogenesis. {ECO:0000269|PubMed:15284220}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TEK/TIE2.
CC {ECO:0000269|PubMed:15284220}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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DR EMBL; AF113707; AAD21586.1; -; mRNA.
DR CCDS; CCDS16874.1; -.
DR RefSeq; NP_033771.1; NM_009641.2.
DR AlphaFoldDB; Q9WVH6; -.
DR SMR; Q9WVH6; -.
DR BioGRID; 198024; 1.
DR IntAct; Q9WVH6; 1.
DR STRING; 10090.ENSMUSP00000028955; -.
DR GlyGen; Q9WVH6; 8 sites.
DR iPTMnet; Q9WVH6; -.
DR PhosphoSitePlus; Q9WVH6; -.
DR PaxDb; Q9WVH6; -.
DR PRIDE; Q9WVH6; -.
DR ProteomicsDB; 282105; -.
DR Antibodypedia; 23019; 279 antibodies from 27 providers.
DR DNASU; 11602; -.
DR Ensembl; ENSMUST00000028955; ENSMUSP00000028955; ENSMUSG00000027460.
DR GeneID; 11602; -.
DR KEGG; mmu:11602; -.
DR UCSC; uc008neq.1; mouse.
DR CTD; 51378; -.
DR MGI; MGI:1336887; Angpt4.
DR VEuPathDB; HostDB:ENSMUSG00000027460; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000160129; -.
DR HOGENOM; CLU_038628_3_1_1; -.
DR InParanoid; Q9WVH6; -.
DR OMA; HAPDNKY; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; Q9WVH6; -.
DR TreeFam; TF336658; -.
DR Reactome; R-MMU-210993; Tie2 Signaling.
DR BioGRID-ORCS; 11602; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Angpt4; mouse.
DR PRO; PR:Q9WVH6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9WVH6; protein.
DR Bgee; ENSMUSG00000027460; Expressed in decidua and 74 other tissues.
DR ExpressionAtlas; Q9WVH6; baseline and differential.
DR Genevisible; Q9WVH6; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; ISO:MGI.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; TAS:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0007492; P:endoderm development; TAS:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0048014; P:Tie signaling pathway; TAS:DFLAT.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR028845; Ang-4.
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:SF31; PTHR19143:SF31; 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 Angiogenesis; Coiled coil; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..509
FT /note="Angiopoietin-4"
FT /id="PRO_0000009117"
FT DOMAIN 288..508
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 416..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..269
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 297..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 450..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 509 AA; 57805 MW; 9B5A74A20A6664F6 CRC64;
MLCQPAMLLD GLLLLATMAA AQHRGPEAGG HRQIHQVRRG QCSYTFVVPE PDICQLAPTA
APEALGGSNS LQRDLPASRL HLTDWRAQRA QRAQRVSQLE KILENNTQWL LKLEQSIKVN
LRSHLVQAQQ DTIQNQTTTM LALGANLMNQ TKAQTHKLTA VEAQVLNQTL HMKTQMLENS
LSTNKLERQM LMQSRELQRL QGRNRALETR LQALEAQHQA QLNSLQEKRE QLHSLLGHQT
GTLANLKHNL HALSSNSSSL QQQQQQLTEF VQRLVRIVAQ DQHPVSLKTP KPVFQDCAEI
KRSGVNTSGV YTIYETNMTK PLKVFCDMET DGGGWTLIQH REDGSVNFQR TWEEYKEGFG
NVAREHWLGN EAVHRLTSRT AYLLRVELHD WEGRQTSIQY ENFQLGSERQ RYSLSVNDSS
SSAGRKNSLA PQGTKFSTKD MDNDNCMCKC AQMLSGGWWF DACGLSNLNG IYYSVHQHLH
KINGIRWHYF RGPSYSLHGT RMMLRPMGA
