P24090 · FETUA_RAT
- ProteinAlpha-2-HS-glycoprotein
- GeneAhsg
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids352 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 143-144 | Cleavage; by trypsin | ||||
Sequence: RK |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-2-HS-glycoprotein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP24090
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKSLVLLLCFAQLWSCQS | ||||||
Chain | PRO_0000008897 | 19-352 | Alpha-2-HS-glycoprotein | |||
Sequence: APQGAGLGFRELACDDPETEHVALIAVDYLNKHLLQGFRQILNQIDKVKVWSRRPFGEVYELEIDTLETTCHALDPTPLANCSVRQQAEHAVEGDCDFHILKQDGQFRVLHAQCHSTPDSAEDVRKFCPRCPILIRFNDTNVVHTVKTALAAFNAQNNGTYFKLVEISRAQNVPFPVSTLVEFVIAATDCTGQEVTDPAKCNLLAEKQYGFCKATLIHRLGGEEVSVACKLFQTQPQPANANPAGPAPTVGQAAPVAPPAGPPESVVVGPVAVPLGLPDHRTHHDLRHAFSPVASVESASGEVLHSPKVGQPGDAGAAGPVAPLCPGRVRYFKI | ||||||
Disulfide bond | 32↔343 | |||||
Sequence: CDDPETEHVALIAVDYLNKHLLQGFRQILNQIDKVKVWSRRPFGEVYELEIDTLETTCHALDPTPLANCSVRQQAEHAVEGDCDFHILKQDGQFRVLHAQCHSTPDSAEDVRKFCPRCPILIRFNDTNVVHTVKTALAAFNAQNNGTYFKLVEISRAQNVPFPVSTLVEFVIAATDCTGQEVTDPAKCNLLAEKQYGFCKATLIHRLGGEEVSVACKLFQTQPQPANANPAGPAPTVGQAAPVAPPAGPPESVVVGPVAVPLGLPDHRTHHDLRHAFSPVASVESASGEVLHSPKVGQPGDAGAAGPVAPLC | ||||||
Disulfide bond | 89↔100 | |||||
Sequence: CHALDPTPLANC | ||||||
Glycosylation | 99 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 114↔132 | |||||
Sequence: CDFHILKQDGQFRVLHAQC | ||||||
Modified residue | 134 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 135 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 138 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 146↔149 | |||||
Sequence: CPRC | ||||||
Glycosylation | 156 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 176 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 208↔219 | |||||
Sequence: CTGQEVTDPAKC | ||||||
Disulfide bond | 230↔247 | |||||
Sequence: CKATLIHRLGGEEVSVAC | ||||||
Modified residue | 309 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 313 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 316 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 318 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Undergoes complex post-translational modification involving N-glycosylation, and addition of fucose and sialic acid residues. Phosphorylation occurs at a serine residue.
Phosphorylated by FAM20C in the extracellular medium.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Synthesized in liver and secreted by the hepatocytes in the blood.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-133 | Cystatin fetuin-A-type 1 | ||||
Sequence: APQGAGLGFRELACDDPETEHVALIAVDYLNKHLLQGFRQILNQIDKVKVWSRRPFGEVYELEIDTLETTCHALDPTPLANCSVRQQAEHAVEGDCDFHILKQDGQFRVLHAQCH | ||||||
Domain | 144-250 | Cystatin fetuin-A-type 2 | ||||
Sequence: KFCPRCPILIRFNDTNVVHTVKTALAAFNAQNNGTYFKLVEISRAQNVPFPVSTLVEFVIAATDCTGQEVTDPAKCNLLAEKQYGFCKATLIHRLGGEEVSVACKLF | ||||||
Region | 256-280 | Disordered | ||||
Sequence: PANANPAGPAPTVGQAAPVAPPAGP | ||||||
Region | 319-338 | Disordered | ||||
Sequence: GEVLHSPKVGQPGDAGAAGP |
Sequence similarities
Belongs to the fetuin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length352
- Mass (Da)37,982
- Last updated1993-04-01 v2
- Checksum43564F60F3C7C90A
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F1LM19 | F1LM19_RAT | Ahsg | 352 | ||
Q7TP75 | Q7TP75_RAT | Ahsg | 553 | ||
A0A8I5ZY55 | A0A8I5ZY55_RAT | Ahsg | 557 | ||
A0A8I5Y586 | A0A8I5Y586_RAT | Ahsg | 301 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 21 | in Ref. 6; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 29 | in Ref. 6; AA sequence | ||||
Sequence: E → Q | ||||||
Sequence conflict | 33-34 | in Ref. 6; AA sequence | ||||
Sequence: DD → NN | ||||||
Sequence conflict | 46 | in Ref. 3; AAA75502 | ||||
Sequence: D → H | ||||||
Sequence conflict | 76 | in Ref. 3; AAA75502 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 236-237 | in Ref. 6; AA sequence | ||||
Sequence: HR → QF | ||||||
Sequence conflict | 241-242 | in Ref. 6; AA sequence | ||||
Sequence: EE → QQ | ||||||
Sequence conflict | 329 | in Ref. 6; AA sequence | ||||
Sequence: Q → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X63446 EMBL· GenBank· DDBJ | CAA45042.1 EMBL· GenBank· DDBJ | mRNA | ||
M29758 EMBL· GenBank· DDBJ | AAA75502.1 EMBL· GenBank· DDBJ | mRNA | ||
D10261 EMBL· GenBank· DDBJ | BAA01101.1 EMBL· GenBank· DDBJ | mRNA | ||
BC091118 EMBL· GenBank· DDBJ | AAH91118.1 EMBL· GenBank· DDBJ | mRNA |