P02772 · FETA_MOUSE
- ProteinAlpha-fetoprotein
- GeneAfp
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids605 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Binds estrogens, fatty acids and metals.
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular space | |
Molecular Function | metal ion binding | |
Molecular Function | small molecule binding | |
Biological Process | ovulation from ovarian follicle | |
Biological Process | progesterone metabolic process | |
Biological Process | sexual reproduction |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-fetoprotein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP02772
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKWITPASLILLLHFAAS | ||||||
Chain | PRO_0000001098 | 19-605 | Alpha-fetoprotein | |||
Sequence: KALHENEFGIASTLDSSQCVTEKNVLSIATITFTQFVPEATEEEVNKMTSDVLAAMKKNSGDGCLESQLSVFLDEICHETELSNKYGLSGCCSQSGVERHQCLLARKKTAPASVPPFQFPEPAESCKAHEENRAVFMNRFIYEVSRRNPFMYAPAILSLAAQYDKVVLACCKADNKEECFQTKRASIAKELREGSMLNEHVCSVIRKFGSRNLQATTIIKLSQKLTEANFTEIQKLALDVAHIHEECCQGNSLECLQDGEKVMTYICSQQNILSSKIAECCKLPMIQLGFCIIHAENGVKPEGLSLNPSQFLGDRNFAQFSSEEKIMFMASFLHEYSRTHPNLPVSVILRIAKTYQEILEKCSQSGNLPGCQDNLEEELQKHIEESQALSKQSCALYQTLGDYKLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKWSGCGEGMADIFIGHLCIRNEASPVNSGISHCCNSSYSNRRLCITSFLRDETYAPPPFSEDKFIFHKDLCQAQGKALQTMKQELLINLVKQKPELTEEQLAAVTADFSGLLEKCCKAQDQEVCFTEEGPKLISKTRDALGV | ||||||
Disulfide bond | 95↔110 | |||||
Sequence: CHETELSNKYGLSGCC | ||||||
Modified residue | 107 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 109↔120 | |||||
Sequence: CCSQSGVERHQC | ||||||
Modified residue | 111 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 113 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 144↔189 | |||||
Sequence: CKAHEENRAVFMNRFIYEVSRRNPFMYAPAILSLAAQYDKVVLACC | ||||||
Disulfide bond | 188↔197 | |||||
Sequence: CCKADNKEEC | ||||||
Disulfide bond | 220↔266 | |||||
Sequence: CSVIRKFGSRNLQATTIIKLSQKLTEANFTEIQKLALDVAHIHEECC | ||||||
Glycosylation | 247 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 265↔273 | |||||
Sequence: CCQGNSLEC | ||||||
Disulfide bond | 285↔299 | |||||
Sequence: CSQQNILSSKIAECC | ||||||
Disulfide bond | 298↔309 | |||||
Sequence: CCKLPMIQLGFC | ||||||
Modified residue | 340 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 380↔389 | |||||
Sequence: CSQSGNLPGC | ||||||
Disulfide bond | 412↔458 | |||||
Sequence: CALYQTLGDYKLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCC | ||||||
Modified residue | 440 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 457↔468 | |||||
Sequence: CCQLSEEKWSGC | ||||||
Disulfide bond | 481↔497 | |||||
Sequence: CIRNEASPVNSGISHCC | ||||||
Disulfide bond | 496↔507 | |||||
Sequence: CCNSSYSNRRLC | ||||||
Glycosylation | 498 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 534↔579 | |||||
Sequence: CQAQGKALQTMKQELLINLVKQKPELTEEQLAAVTADFSGLLEKCC | ||||||
Disulfide bond | 578↔587 | |||||
Sequence: CCKAQDQEVC |
Post-translational modification
Glycosylated; contains two glycans.
Sulfated.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-207 | Albumin 1 | ||||
Sequence: KALHENEFGIASTLDSSQCVTEKNVLSIATITFTQFVPEATEEEVNKMTSDVLAAMKKNSGDGCLESQLSVFLDEICHETELSNKYGLSGCCSQSGVERHQCLLARKKTAPASVPPFQFPEPAESCKAHEENRAVFMNRFIYEVSRRNPFMYAPAILSLAAQYDKVVLACCKADNKEECFQTKRASIAK | ||||||
Domain | 208-398 | Albumin 2 | ||||
Sequence: ELREGSMLNEHVCSVIRKFGSRNLQATTIIKLSQKLTEANFTEIQKLALDVAHIHEECCQGNSLECLQDGEKVMTYICSQQNILSSKIAECCKLPMIQLGFCIIHAENGVKPEGLSLNPSQFLGDRNFAQFSSEEKIMFMASFLHEYSRTHPNLPVSVILRIAKTYQEILEKCSQSGNLPGCQDNLEEELQ | ||||||
Domain | 399-597 | Albumin 3 | ||||
Sequence: KHIEESQALSKQSCALYQTLGDYKLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKWSGCGEGMADIFIGHLCIRNEASPVNSGISHCCNSSYSNRRLCITSFLRDETYAPPPFSEDKFIFHKDLCQAQGKALQTMKQELLINLVKQKPELTEEQLAAVTADFSGLLEKCCKAQDQEVCFTEEGPKLIS |
Sequence similarities
Belongs to the ALB/AFP/VDB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length605
- Mass (Da)67,337
- Last updated1986-07-21 v1
- ChecksumCE09E9F50D74619A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YU60 | A0A0J9YU60_MOUSE | Afp | 121 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 533-536 | in Ref. 6; no nucleotide entry | ||||
Sequence: LCQA → RAKL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V00743 EMBL· GenBank· DDBJ | CAA24118.1 EMBL· GenBank· DDBJ | mRNA | ||
M16394 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16381 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16382 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16383 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16384 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16385 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16386 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16387 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16388 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16389 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16390 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16391 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16392 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16393 EMBL· GenBank· DDBJ | AAA37189.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK010934 EMBL· GenBank· DDBJ | BAB27278.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145975 EMBL· GenBank· DDBJ | BAE26798.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146513 EMBL· GenBank· DDBJ | BAE27225.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146524 EMBL· GenBank· DDBJ | BAE27233.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167549 EMBL· GenBank· DDBJ | BAE39615.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168574 EMBL· GenBank· DDBJ | BAE40444.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168576 EMBL· GenBank· DDBJ | BAE40446.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168751 EMBL· GenBank· DDBJ | BAE40591.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168883 EMBL· GenBank· DDBJ | BAE40701.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169046 EMBL· GenBank· DDBJ | BAE40834.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169054 EMBL· GenBank· DDBJ | BAE40842.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169147 EMBL· GenBank· DDBJ | BAE40926.1 EMBL· GenBank· DDBJ | mRNA | ||
BC066206 EMBL· GenBank· DDBJ | AAH66206.1 EMBL· GenBank· DDBJ | mRNA |