ANG
entrez
283
canonical
uniprot
P03950
canonical
ensembl
ENSG00000214274
resolver
ensp
ENSP00000336762
resolver
ensp
ENSP00000381077
resolver
ensp
ENSP00000555657
resolver
ensp
ENSP00000555659
resolver
ensp
ENSP00000555660
resolver
ensp
ENSP00000555662
resolver
ensp
ENSP00000555664
resolver
ensp
ENSP00000555665
resolver
ensp
ENSP00000555666
resolver
ensp
ENSP00000555667
resolver
ensp
ENSP00000555668
resolver
ensp
ENSP00000555669
resolver
ensp
ENSP00000555670
resolver
ensp
ENSP00000555671
resolver
ensp
ENSP00000555672
resolver
ensp
ENSP00000555673
resolver
ensp
ENSP00000555674
resolver
ensp
ENSP00000555675
resolver
ensp
ENSP00000555676
resolver
ensp
ENSP00000676904
resolver
ensp
ENSP00000763446
resolver
enst
ENST00000336811
resolver
enst
ENST00000397990
resolver
enst
ENST00000885598
resolver
enst
ENST00000885600
resolver
enst
ENST00000885601
resolver
enst
ENST00000885603
resolver
enst
ENST00000885605
resolver
enst
ENST00000885606
resolver
enst
ENST00000885607
resolver
enst
ENST00000885608
resolver
enst
ENST00000885609
resolver
enst
ENST00000885610
resolver
enst
ENST00000885611
resolver
enst
ENST00000885612
resolver
enst
ENST00000885613
resolver
enst
ENST00000885614
resolver
enst
ENST00000885615
resolver
enst
ENST00000885616
resolver
enst
ENST00000885617
resolver
genesymbol
ANG
resolver
genesymbol_syn
RNASE5
resolver
hgnc
HGNC:483
resolver
uniprot
Q05CV1
resolver
uniprot
Q53X86
resolver
uniprot
Q6P5T2
resolver
uniprot
Q8WXE7
resolver
uniprot_entry
ANGI_HUMAN
resolver
uniprot_sec
Q05CV1
resolver
uniprot_sec
Q53X86
resolver
uniprot_sec
Q6P5T2
resolver
uniprot_sec
Q8WXE7
resolver
activity_regulation
ACTIVITY REGULATION: Has weak tRNA ribonuclease activity by itself due to partial autoinhibition by its C-terminus (residues 140-147), which folds into a short alpha-helix that partially occludes the substrate-binding site (PubMed:38718836, PubMed:8159680, PubMed:8622921, PubMed:9578571). In absence of stress, the ribonuclease activity is inhibited by RNH1 in the cytoplasm (PubMed:19332886, PubMed:19354288, PubMed:23843625, PubMed:3243277, PubMed:32510170, PubMed:38718836). In response to stress, dissociates from RNH1 in the cytoplasm and associates with cytoplasmic ribosomes with vacant A-sites: ribosomes directly activate the tRNA ribonuclease activity of ANG by refolding the C-terminal alpha-helix (PubMed:38718836). In response to stress, the angiogenic activity of ANG is inhibited by RNH1 in the nucleus (PubMed:23843625). {ECO:0000269|PubMed:19332886, ECO:0000269|PubMed:19354288, ECO:0000269|PubMed:23843625, ECO:0000269|PubMed:3243277, ECO:0000269|PubMed:32510170, ECO:0000269|PubMed:38718836, ECO:0000269|PubMed:8159680, ECO:0000269|PubMed:8622921, ECO:0000269|PubMed:9578571}.
uniprot
proteins
amino_acid_sequence
MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP
uniprot
proteins
disease_involvement
DISEASE: Amyotrophic lateral sclerosis 9 (ALS9) [MIM:611895]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:15557516, ECO:0000269|PubMed:16501576, ECO:0000269|PubMed:17703939, ECO:0000269|PubMed:17886298, ECO:0000269|PubMed:17900154, ECO:0000269|PubMed:18087731, ECO:0000269|PubMed:18852347, ECO:0000269|PubMed:19153377, ECO:0000269|PubMed:19332886, ECO:0000269|PubMed:19363631, ECO:0000269|PubMed:22190368, ECO:0000269|PubMed:22292798, ECO:0000269|PubMed:22292843, ECO:0000269|PubMed:25372031, ECO:0000269|PubMed:29748193, ECO:0000269|PubMed:38718836}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.27.-
uniprot
proteins
function
FUNCTION: Secreted ribonuclease that can either promote or restrict cell proliferation of target cells, depending on the context (PubMed:12051708, PubMed:1400510, PubMed:19332886, PubMed:20129916, PubMed:21855800, PubMed:23047679, PubMed:23843625, PubMed:2424496, PubMed:2459697, PubMed:2730651, PubMed:27518564, PubMed:28176817, PubMed:29100074, PubMed:29748193, PubMed:3122207, PubMed:32510170, PubMed:38718836, PubMed:8159680, PubMed:8570639, PubMed:8622921, PubMed:9578571). Endocytosed in target cells via its receptor PLXNB2 and translocates to the cytoplasm or nucleus (PubMed:29100074, PubMed:32510170). Under stress conditions, localizes to the cytoplasm and promotes the assembly of stress granules (SGs): specifically cleaves a subset of tRNAs within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs), resulting in translation repression and inhibition of cell proliferation (PubMed:1400510, PubMed:19332886, PubMed:20129916, PubMed:21855800, PubMed:23047679, PubMed:27518564, PubMed:29100074, PubMed:29748193, PubMed:32510170, PubMed:38718836). tiRNas also prevent formation of apoptosome, thereby promoting cell survival (By similarity). Preferentially cleaves RNAs between a pyrimidine and an adenosine residue, suggesting that it cleaves the anticodon loop of tRNA(Ala) (32-UUAGCAU-38) after positions 33 and 36 (PubMed:3289612, PubMed:38718836). Cleaves a subset of tRNAs, including tRNA(Ala), tRNA(Glu), tRNA(Gly), tRNA(Lys), tRNA(Val), tRNA(His), tRNA(Asp) and tRNA(Sec) (PubMed:31582561). Under growth conditions and in differentiated cells, translocates to the nucleus and stimulates ribosomal RNA (rRNA) transcription, including that containing the initiation site sequences of 45S rRNA, thereby promoting cell growth and proliferation (PubMed:12051708, PubMed:15735021, PubMed:27518564, PubMed:29100074, PubMed:8127865). Angiogenin induces vascularization of normal and malignant tissues via its ability to promote rRNA transcription (PubMed:19354288, PubMed:4074709, PubMed:8448182). Involved in hematopoietic stem and progenitor cell (HSPC) growth and survival by promoting rRNA transcription in growth conditions and inhibiting translation in response to stress, respectively (PubMed:27518564). Mediates the crosstalk between myeloid and intestinal epithelial cells to protect the intestinal epithelial barrier integrity: secreted by myeloid cells and promotes intestinal epithelial cells proliferation and survival (PubMed:32510170). Also mediates osteoclast-endothelial cell crosstalk in growing bone: produced by osteoclasts and protects the neighboring vascular cells against senescence by promoting rRNA transcription (By similarity). {ECO:0000250|UniProtKB:P21570, ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:1400510, ECO:0000269|PubMed:15735021, ECO:0000269|PubMed:19332886, ECO:0000269|PubMed:19354288, ECO:0000269|PubMed:20129916, ECO:0000269|PubMed:21855800, ECO:0000269|PubMed:23047679, ECO:0000269|PubMed:23843625, ECO:0000269|PubMed:2424496, ECO:0000269|PubMed:2459697, ECO:0000269|PubMed:2730651, ECO:0000269|PubMed:27518564, ECO:0000269|PubMed:28176817, ECO:0000269|PubMed:29100074, ECO:0000269|PubMed:29748193, ECO:0000269|PubMed:3122207, ECO:0000269|PubMed:31582561, ECO:0000269|PubMed:32510170, ECO:0000269|PubMed:3289612, ECO:0000269|PubMed:38718836, ECO:0000269|PubMed:4074709, ECO:0000269|PubMed:8127865, ECO:0000269|PubMed:8159680, ECO:0000269|PubMed:8448182, ECO:0000269|PubMed:8570639, ECO:0000269|PubMed:8622921, ECO:0000269|PubMed:9578571}.
uniprot
proteins
mass_dalton
16550
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="R->A: Affects substrate preference. Significantly decreases binding affinity for RNH1."; /evidence="ECO:0000269|PubMed:10413501, ECO:0000269|PubMed:8570639"; MUTAGEN 32; /note="H->A: Significantly decreases binding affinity for RNH1."; /evidence="ECO:0000269|PubMed:9050852"; MUTAGEN 36; /note="Q->A: Slightly decreases binding affinity for RNH1."; /evidence="ECO:0000269|PubMed:9050852"; MUTAGEN 37; /note="H->A: Abolished ribonuclease activity. does not affect binding to PLXNB2 receptor."; /evidence="ECO:0000269|PubMed:29100074, ECO:0000269|PubMed:38718836"; MUTAGEN 59; /note="L->P: Homodimerization is similar to wild-type; causes mislocalization in the cytoplasm; strongly reduces ribonucleolytic activity."; /evidence="ECO:0000269|PubMed:25372031"; MUTAGEN 64; /note="K->Q: Significantly decreases binding affinity for RNH1."; /evidence="ECO:0000269|PubMed:10413501, ECO:0000269|PubMed:9050852"; MUTAGEN 68; /note="T->A: Decreased ribonuclease activity."; /evidence="ECO:0000269|PubMed:9578571"; MUTAGEN 90; /note="R->A: Abolished binding to PLXNB2 receptor."; /evidence="ECO:0000269|PubMed:29100074"; MUTAGEN 92; /note="N->A: Slightly decreases binding affinity for RNH1."; /evidence="ECO:0000269|PubMed:9050852"; MUTAGEN 92; /note="N->D: Abolished binding to PLXNB2 receptor."; /evidence="ECO:0000269|PubMed:29100074"; MUTAGEN 104; /note="T->A: Increased ribonuclease activity."; /evidence="ECO:0000269|PubMed:9578571"; MUTAGEN 104; /note="T->D: Slightly increased ribonuclease activity."; /evidence="ECO:0000269|PubMed:9578571"; MUTAGEN 109..110; /note="GG->RR: Significantly decreases binding affinity for RNH1."; /evidence="ECO:0000269|PubMed:19354288"; MUTAGEN 132; /note="E->A: Slightly decreases binding affinity for RNH1."; /evidence="ECO:0000269|PubMed:9050852"; MUTAGEN 140..141; /note="DQ->AA: Slightly increased ribonuclease activity."; /evidence="ECO:0000269|PubMed:8159680"; MUTAGEN 140; /note="D->N,H,S,A: Strongly increased ribonuclease activity."; /evidence="ECO:0000269|PubMed:11851402, ECO:0000269|PubMed:2459697"; MUTAGEN 141; /note="Q->A,G: Strongly increased ribonuclease activity."; /evidence="ECO:0000269|PubMed:11851402, ECO:0000269|PubMed:8159680"; MUTAGEN 143..144; /note="IF->AA: Increased ribonuclease activity."; /evidence="ECO:0000269|PubMed:11851402, ECO:0000269|PubMed:8622921
uniprot
proteins
protein_family
Pancreatic ribonuclease family
uniprot
proteins
pubmed
10413501
uniprot
proteins
pubmed
11468363
uniprot
proteins
pubmed
11851402
uniprot
proteins
pubmed
11919285
uniprot
proteins
pubmed
12051708
uniprot
proteins
pubmed
12842050
uniprot
proteins
pubmed
1400510
uniprot
proteins
pubmed
14756559
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15557516
uniprot
proteins
pubmed
15735021
uniprot
proteins
pubmed
16501576
uniprot
proteins
pubmed
17703939
uniprot
proteins
pubmed
17886298
uniprot
proteins
pubmed
17900154
uniprot
proteins
pubmed
18087731
uniprot
proteins
pubmed
18852347
uniprot
proteins
pubmed
19153377
uniprot
proteins
pubmed
19332886
uniprot
proteins
pubmed
19354288
uniprot
proteins
pubmed
19363631
uniprot
proteins
pubmed
20129916
uniprot
proteins
pubmed
21855800
uniprot
proteins
pubmed
22190368
uniprot
proteins
pubmed
22292798
uniprot
proteins
pubmed
22292843
uniprot
proteins
pubmed
22384259
uniprot
proteins
pubmed
23047679
uniprot
proteins
pubmed
23843625
uniprot
proteins
pubmed
2424496
uniprot
proteins
pubmed
2440105
uniprot
proteins
pubmed
2459697
uniprot
proteins
pubmed
25372031
uniprot
proteins
pubmed
2730651
uniprot
proteins
pubmed
27518564
uniprot
proteins
pubmed
28176817
uniprot
proteins
pubmed
2866794
uniprot
proteins
pubmed
2866795
uniprot
proteins
pubmed
29100074
uniprot
proteins
pubmed
29748193
uniprot
proteins
pubmed
3122207
uniprot
proteins
pubmed
31582561
uniprot
proteins
pubmed
3243277
uniprot
proteins
pubmed
32510170
uniprot
proteins
pubmed
3289612
uniprot
proteins
pubmed
33535464
uniprot
proteins
pubmed
3663649
uniprot
proteins
pubmed
37218877
uniprot
proteins
pubmed
38718836
uniprot
proteins
pubmed
4074709
uniprot
proteins
pubmed
7945327
uniprot
proteins
pubmed
8127865
uniprot
proteins
pubmed
8159679
uniprot
proteins
pubmed
8159680
uniprot
proteins
pubmed
8448182
uniprot
proteins
pubmed
8570639
uniprot
proteins
pubmed
8622921
uniprot
proteins
pubmed
9050852
uniprot
proteins
pubmed
9311977
uniprot
proteins
pubmed
9461294
uniprot
proteins
pubmed
9578571
uniprot
proteins
pubmed
9918722
uniprot
proteins
sequence_length
147
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23047679, ECO:0000269|PubMed:29748193, ECO:0000269|PubMed:3663649}. Nucleus {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:15735021, ECO:0000269|PubMed:23047679, ECO:0000269|PubMed:23843625, ECO:0000269|PubMed:25372031, ECO:0000269|PubMed:29100074, ECO:0000269|PubMed:8127865}. Nucleus, nucleolus {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:7945327}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23843625, ECO:0000269|PubMed:27518564, ECO:0000269|PubMed:29100074}. Note=The secreted protein is rapidly endocytosed by target cells following interaction with PLXNB2 receptor and translocated to the cytoplasm and nucleus (PubMed:29100074). In the nucleus, accumulates in the nucleolus and binds to DNA (PubMed:12051708). {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:29100074}.
uniprot
proteins