Q9BXJ7 · AMNLS_HUMAN

  • Protein
    Protein amnionless
  • Gene
    AMN
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Membrane-bound component of the endocytic receptor formed by AMN and CUBN (PubMed:14576052, PubMed:29402915, PubMed:30523278).
Required for normal CUBN glycosylation and trafficking to the cell surface (PubMed:14576052, PubMed:29402915).
The complex formed by AMN and CUBN is required for efficient absorption of vitamin B12 (PubMed:12590260, PubMed:14576052, PubMed:26040326).
Required for normal CUBN-mediated protein transport in the kidney (Probable)

Miscellaneous

The role of Amn in embryonic development seems to be species specific. In mice, null mutations lead to embryonic lethality. Human mutations give rise to much milder symptoms.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapical plasma membrane
Cellular Componentbrush border membrane
Cellular Componentclathrin-coated pit
Cellular Componentendocytic vesicle
Cellular Componentendosome membrane
Cellular Componentextracellular exosome
Cellular Componentextracellular space
Cellular Componentmembrane
Cellular Componentmicrovillus membrane
Cellular Componentplasma membrane
Cellular Componentreceptor complex
Molecular Functioncargo receptor activity
Molecular Functionsignaling receptor binding
Biological Processcobalamin metabolic process
Biological Processcobalamin transport
Biological ProcessGolgi to plasma membrane protein transport
Biological Processprotein localization
Biological Processreceptor-mediated endocytosis
Biological Processrenal protein absorption

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      AMN
    • ORF names
      UNQ513/PRO1028

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9BXJ7
  • Secondary accessions
    • Q6UX83

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain20-357Extracellular
Transmembrane358-378Helical
Topological domain379-453Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

Imerslund-Grasbeck syndrome 2 (IGS2)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of Imerslund-Grasbeck syndrome, a rare autosomal recessive disorder characterized by vitamin B12 deficiency commonly resulting in megaloblastic anemia, which is responsive to parenteral vitamin B12 therapy and appears in infancy or early childhood. Clinical manifestations include failure to thrive, infections and neurological damage. Mild proteinuria, with no signs of kidney disease, is present in about half of the patients.
  • See also
    MIM:618882
Natural variants in IGS2
Variant IDPosition(s)ChangeDescription
VAR_01573341T>Iin IGS2; reduced presence at the cell membrane; loss of interaction with CUBN; reduced CUBN expression at the cell surface; dbSNP:rs119478058
VAR_08190669M>Kin IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface; dbSNP:rs375774640
VAR_081907234C>Fin IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface; dbSNP:rs386834176

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis35Loss of expression at the cell membrane.
Mutagenesis37No effect.
Natural variantVAR_01573341in IGS2; reduced presence at the cell membrane; loss of interaction with CUBN; reduced CUBN expression at the cell surface; dbSNP:rs119478058
Mutagenesis59Loss of interaction with CUBN and strongly reduced CUBN expression at the cell surface.
Natural variantVAR_08190669in IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface; dbSNP:rs375774640
Natural variantVAR_081907234in IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface; dbSNP:rs386834176
Mutagenesis254Loss of interaction with CUBN and strongly reduced CUBN expression at the cell surface.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 630 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000044765120-?Soluble protein amnionless
ChainPRO_000002070220-453Protein amnionless
Glycosylation35N-linked (GlcNAc...) asparagine
Disulfide bond43↔96
Disulfide bond137↔213
Disulfide bond205↔211
Disulfide bond223↔249
Disulfide bond234↔250
Disulfide bond239↔253

Post-translational modification

N-glycosylated.
A soluble form arises by proteolytic removal of the membrane anchor.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in proximal tubules in the kidney cortex (at protein level) (PubMed:14576052, PubMed:29402915).
Long isoforms are highly expressed in small intestine, colon and kidney (renal proximal tubule epithelial cells). Shorter isoforms are detected at lower levels in testis, thymus and peripheral blood leukocytes

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts (via extracellular region) with CUBN/cubilin, giving rise to a huge complex containing one AMN chain and three CUBN chains.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9BXJ7CUBN O604943EBI-11510881, EBI-3953632
View interactors in UniProtKB
View CPX-5774 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region67-87Interaction with CUBN
Domain202-254VWFC

Domain

The complex formed by AMN and CUBN is composed of a 400 Angstrom long stem and a globular crown region. The stem region is probably formed by AMN and the CUBN N-terminal region, including the EGF-like domains. The crown is probably formed by the CUBN CUB domains.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 1 isoforms produced by Alternative promoter usage. At least 5 isoforms, 1, 2, 3, 4 and 5, are produced.

Q9BXJ7-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    453
  • Mass (Da)
    47,754
  • Last updated
    2010-05-18 v2
  • Checksum
    40AA14EF186A6009
MGVLGRVLLWLQLCALTQAVSKLWVPNTDFDVAANWSQNRTPCAGGAVEFPADKMVSVLVQEGHAVSDMLLPLDGELVLASGAGFGVSDVGSHLDCGAGEPAVFRDSDRFSWHDPHLWRSGDEAPGLFFVDAERVPCRHDDVFFPPSASFRVGLGPGASPVRVRSISALGRTFTRDEDLAVFLASRAGRLRFHGPGALSVGPEDCADPSGCVCGNAEAQPWICAALLQPLGGRCPQAACHSALRPQGQCCDLCGAVVLLTHGPAFDLERYRARILDTFLGLPQYHGLQVAVSKVPRSSRLREADTEIQVVLVENGPETGGAGRLARALLADVAENGEALGVLEATMRESGAHVWGSSAAGLAGGVAAAVLLALLVLLVAPPLLRRAGRLRWRRHEAAAPAGAPLGFRNPVFDVTASEELPLPRRLSLVPKAAADSTSHSYFVNPLFAGAEAEA

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YMX8H0YMX8_HUMANAMN107
H0YKJ5H0YKJ5_HUMANAMN131

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict241in Ref. 1; AAK28532

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF328788
EMBL· GenBank· DDBJ
AAK28532.1
EMBL· GenBank· DDBJ
mRNA
AL117209
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AY358468
EMBL· GenBank· DDBJ
AAQ89949.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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