G1UB63 · CSA1_CANAL

Function

function

Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.

Features

Showing features for binding site.

110181002003004005006007008009001,000
TypeIDPosition(s)Description
Binding site78Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site269Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site439Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site601Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

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 Componentcell surface
Cellular Componentcellular bud
Cellular Componentextracellular region
Cellular Componentfungal-type cell wall
Cellular Componenthyphal cell wall
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Functionheme binding
Molecular Functionmetal ion binding
Biological Processintracellular iron ion homeostasis
Biological Processsingle-species biofilm formation on inanimate substrate

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Cell wall protein 1
  • Alternative names
    • Surface antigen protein 1
    • Wall protein 1

Gene names

    • Name
      CSA1
    • Synonyms
      WAP1
    • ORF names
      CaO19.7114
    • Ordered locus names
      CAALFM_C700090CA

Organism names

Accessions

  • Primary accession
    G1UB63
  • Secondary accessions
    • A0A1D8PQH2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-17
ChainPRO_000042477718-989Cell wall protein 1
Disulfide bond60↔100
Disulfide bond64↔95
Disulfide bond74↔81
Disulfide bond83↔116
Disulfide bond251↔291
Disulfide bond255↔286
Disulfide bond265↔272
Disulfide bond274↔307
Disulfide bond421↔461
Disulfide bond425↔456
Disulfide bond435↔442
Disulfide bond444↔477
Disulfide bond583↔623
Disulfide bond587↔618
Disulfide bond597↔604
Disulfide bond606↔639
Glycosylation698N-linked (GlcNAc...) asparagine
Glycosylation708N-linked (GlcNAc...) asparagine
Glycosylation718N-linked (GlcNAc...) asparagine
Glycosylation729N-linked (GlcNAc...) asparagine
Glycosylation743N-linked (GlcNAc...) asparagine
Glycosylation753N-linked (GlcNAc...) asparagine
Glycosylation769N-linked (GlcNAc...) asparagine
Glycosylation798N-linked (GlcNAc...) asparagine
Glycosylation965N-linked (GlcNAc...) asparagine
Lipidation989GPI-anchor amidated serine
PropeptidePRO_0000424778990-1018Removed in mature form

Post-translational modification

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.

Keywords

PTM databases

Expression

Induction

Preferentially expressed during the mycelial growth phase with only low levels of transcript detected in the yeast form. Induced by iron starvation and ciclopirox. Positively regulated by BCR1 and RIM101, and repressed by TUP1. Expression is also regulated by EFG1, CPH1, HAP43, and SEF1.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain32-143CFEM 1
Region147-227Disordered
Domain223-334CFEM 2
Region338-396Disordered
Domain393-504CFEM 3
Region507-557Disordered
Domain555-666CFEM 4
Region677-785Disordered

Domain

The CFEM domain is involved in heme-binding. It contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens.

Sequence similarities

Belongs to the RBT5 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,018
  • Mass (Da)
    103,515
  • Last updated
    2011-10-19 v1
  • Checksum
    BA25AF72061A001A
MLPSIVISIVLASFVSAESSITEAPTTTAEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVASSSEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVPSSSEQSVETSSESAESSQSVESSQPAETSSEQPSETSSETSSQQLSSITSAPDSSATSSSSTTSTFIRTASINGFADKLYDQLPECAKPCMFQNTGITPCPYWDAGCLCVMPQFAGAIGSCVADSCKGQDIVSVTSLGTSVCSVAGVNAPYWMLPASVKSSLSVAATAVPTSDSASETASQEPSETSSEQPSETASQQPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGSSICSVAGVWDPYWMLPANVQSSLNAAATAVATSDSASEVASASESASQVPQETSAASSQSANNSVASAAPSNSSVSAAPSSNSSGVPAAPSNNSSGASVVPSQSANNSSASAAPSNNSSSAISESVAPSSYGNSTIAQPSTSTKSDAASITGPITTDKVITNESGIVFTSTVIITHVSEYCDQTSAAAVQSSACEEQSSAKSEQASASSEQVKVITSVVWCESSIQSIESVKTSAEAAHKTEVIASCASELSSLSSAKSEAMKTVSSLVEVQKSAVAKQTSLAAVQSSAASVQLSAAHAQKSSEAVEVAQTAVAEASKAGDEISTEIVNITKTVSSGKETGVSQATVAANTHSVAIANMANTKFASTMSLLVASFVFVGLFI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP017629
EMBL· GenBank· DDBJ
AOW30388.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp