SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00000685 
UniProt Accession
Theoretical PI
9.73  
Molecular Weight
16550 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
ANG 
Gene Synonyms/Alias
RNASE5 
Protein Name
Angiogenin 
Protein Synonyms/Alias
EC=3.1.27.- Ribonuclease 5;RNase 5Flags: Precursor 
Organism
Homo sapiens (Human) 
NCBI Taxonomy ID
9606 
Chromosome Location
chr:14;21152336-21167130;1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
The specific localization of angiogenin in PTMCs suggests that angiogenin plays physiologic roles in the human testis. 
The information of related literatures
1. K. Koga, Y. Osuga, T. Yano, Y. Ikezuki, O. Yoshino, Y. Hirota, T. Hirata, S. Horie, T. Ayabe, O. Tsutsumi and Y. Taketani (2004) Evidence for the presence of angiogenin in human testis. J Androl 25(3): 369-74. 

Abstract
We have reported the expression and possible roles of angiogenin, a potent angiogenic factor, in human female reproductive organs. In this study, we investigated the expression of angiogenin in the human testis, a male reproductive organ. Western blot analysis showed the presence of angiogenin in the human testis, with a single band of the same size as recombinant human angiogenin. Immunohistochemical study and in situ hybridization showed that the angiogenin protein and messenger RNA (mRNA) localized in peritubular myoid cells (PTMCs) and vascular endothelial and smooth muscle cells. PTMCs are known to play various roles in the testes concerned with spermatogenesis, transport of spermatozoa, structural support to the seminiferous tubules, and mediation of Sertoli cell function. The specific localization of angiogenin in PTMCs suggests that angiogenin plays physiologic roles in the human testis. PMID: [15064314] 

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Figures for illustrating the function of this protein/gene
Function
May function as a tRNA-specific ribonuclease thatabolishes protein synthesis by specifically hydrolyzing cellulartRNAs. Binds to actin on the surface of endothelial cells; oncebound, angiogenin is endocytosed and translocated to the nucleus.Angiogenin induces vascularization of normal and malignanttissues. Angiogenic activity is regulated by interaction with RNH1in vivo. 
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Subcellular Location
Secreted. 
Tissue Specificity
Expressed predominantly in the liver. Alsodetected in endothelial cells and spinal cord neurons. 
Gene Ontology
GO IDGO termEvidence
GO:0032311 C:angiogenin-PRI complex IPI:UniProtKB.
GO:0005605 C:basal lamina IDA:UniProtKB.
GO:0005615 C:extracellular space IDA:UniProtKB.
GO:0030426 C:growth cone ISS:UniProtKB.
GO:0043025 C:neuronal cell body ISS:UniProtKB.
GO:0005730 C:nucleolus ISS:UniProtKB.
GO:0005507 F:copper ion binding IDA:UniProtKB.
GO:0003677 F:DNA binding IC:UniProtKB.
GO:0004519 F:endonuclease activity TAS:UniProtKB.
GO:0008201 F:heparin binding IDA:UniProtKB.
GO:0004522 F:pancreatic ribonuclease activity IEA:InterPro.
GO:0042277 F:peptide binding IDA:UniProtKB.
GO:0004540 F:ribonuclease activity IDA:UniProtKB.
GO:0019843 F:rRNA binding TAS:UniProtKB.
GO:0030041 P:actin filament polymerization ISS:UniProtKB.
GO:0032431 P:activation of phospholipase A2 activity IMP:UniProtKB.
GO:0007202 P:activation of phospholipase C activity IMP:UniProtKB.
GO:0032148 P:activation of protein kinase B activity IMP:UniProtKB.
GO:0001525 P:angiogenesis IMP:UniProtKB.
GO:0007154 P:cell communication NAS:UniProtKB.
GO:0008219 P:cell death IEA:UniProtKB-KW.
GO:0016477 P:cell migration IMP:UniProtKB.
GO:0006651 P:diacylglycerol biosynthetic process IDA:UniProtKB.
GO:0042592 P:homeostatic process NAS:UniProtKB.
GO:0048662 P:negative regulation of smooth muscle cell proliferation IDA:UniProtKB.
GO:0017148 P:negative regulation of translation IEA:UniProtKB-KW.
GO:0001556 P:oocyte maturation NAS:UniProtKB.
GO:0001541 P:ovarian follicle development NAS:UniProtKB.
GO:0001890 P:placenta development NAS:UniProtKB.
GO:0001938 P:positive regulation of endothelial cell proliferation IDA:UniProtKB.
GO:0050714 P:positive regulation of protein secretion IDA:UniProtKB.
GO:0009725 P:response to hormone stimulus IDA:UniProtKB.
GO:0001666 P:response to hypoxia IDA:UniProtKB.
GO:0009303 P:rRNA transcription IMP:UniProtKB.
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Interpro
IPR001427;    RNaseA.
IPR023411;    RNaseA_AS.
IPR023412;    RNaseA_domain.
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Pfam
PF00074;    RnaseA;    1.
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SMART
SM00092;    RNAse_Pc;    1.
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PROSITE
PS00127;    RNASE_PANCREATIC;    1.
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PRINTS
PR00794;    RIBONUCLEASE.;   
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Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
SIGNAL        1     24
CHAIN        25    147       Angiogenin.
                             /FTId=PRO_0000030843.
REGION       64     68       Substrate binding.
ACT_SITE     37     37       Proton acceptor.
ACT_SITE    138    138       Proton donor.
MOD_RES      25     25       Pyrrolidone carboxylic acid.
DISULFID     50    105
DISULFID     63    116
DISULFID     81    131
VARIANT      12     12       F -> S (in ALS9).
                             /FTId=VAR_044145.
VARIANT      20     20       P -> S (in ALS9).
                             /FTId=VAR_044146.
VARIANT      36     36       Q -> L (in ALS9; reduced ribonucleolytic
                             activity; low angiogenic activity;
                             reduced mitogenic activity; wild type
                             far-UV CD spectra).
                             /FTId=VAR_044147.
VARIANT      41     41       K -> E (in ALS9; reduced ribonucleolytic
                             activity).
                             /FTId=VAR_044148.
VARIANT      41     41       K -> I (in ALS9; loss of angiogenic
                             activity; reduced ribonucleolytic
                             activity; retains nuclear translocation).
                             /FTId=VAR_044149.
VARIANT      52     52       S -> N (in ALS9; loss of angiogenic
                             activity; reduced ribonucleolytic
                             activity; unable to translocate to the
                             nucleus).
                             /FTId=VAR_044150.
VARIANT      55     55       R -> K (in ALS9; marginally reduced
                             ribonucleolytic activity; wild type far-
                             UV CD spectra).
                             /FTId=VAR_044151.
VARIANT      63     63       C -> W (in ALS9; reduced ribonucleolytic
                             activity; low angiogenic activity;
                             reduced mitogenic activity; reduced
                             thermal stability).
                             /FTId=VAR_044152.
VARIANT      64     64       K -> I (in ALS9; reduced ribonucleolytic
                             activity; low angiogenic activity;
                             reduced mitogenic activity; moderate
                             reduction of thermal stability).
                             /FTId=VAR_044153.
VARIANT      70     70       I -> V (in some ALS9 patients;
                             pathogenicity uncertain; reduced
                             ribonucleolytic activity; moderate
                             reduction of thermal stability).
                             /FTId=VAR_044154.
VARIANT      84     84       K -> E (in dbSNP:rs17560).
                             /FTId=VAR_013148.
VARIANT     136    136       P -> L (in ALS9; loss of angiogenic
                             activity; reduced ribonucleolytic
                             activity; unable to translocate to the
                             nucleus).
                             /FTId=VAR_044155.
VARIANT     137    137       V -> I (in ALS9).
                             /FTId=VAR_044156.
VARIANT     138    138       H -> R (in ALS9).
                             /FTId=VAR_044157.
MUTAGEN      29     29       R->A: Significantly decreases binding
                             affinity for RNH1.
MUTAGEN      32     32       H->A: Significantly decreases binding
                             affinity for RNH1.
MUTAGEN      36     36       Q->A: Slightly decreases binding affinity
                             for RNH1.
MUTAGEN      64     64       K->Q: Significantly decreases binding
                             affinity for RNH1.
MUTAGEN      92     92       N->A: Slightly decreases binding affinity
                             for RNH1.
MUTAGEN     109    110       GG->RR: Significantly decreases binding
                             affinity for RNH1.
MUTAGEN     132    132       E->A: Slightly decreases binding affinity
                             for RNH1.
MUTAGEN     140    140       D->H,S,A: 15- to 18-fold increase in
                             RNase activity.
MUTAGEN     141    141       Q->G: Over 18-fold increase in RNase
                             activity.
MUTAGEN     143    144       IF->AA: 3- to 5-fold increase in RNase
                             activity.
CONFLICT     59     59       L -> P (in Ref. 7; AAH62698).
TURN         26     28
HELIX        29     37
HELIX        47     56
TURN         60     63
STRAND       65     70
HELIX        74     78
HELIX        79     81
TURN         83     85
STRAND       86     89
TURN         90     92
STRAND       93     98
STRAND      100    110
STRAND      112    115
STRAND      117    125
STRAND      128    132
STRAND      135    139
HELIX       141    144
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Nucleotide Sequence
Length: 4668 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 147 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
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