Q5A312 · ALS7_CANAL

Function

function

Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections.

Miscellaneous

ALS7 gene corresponds to a hypermutable contingency locus meaning that the diversity of ALS7 proteins provide C.albicans with a large and flexible repertoire of similar but non-identical surface proteins which may be important not only for adhesion but also for evasion of host defenses.

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 Componentextracellular region
Cellular Componentfungal-type cell wall
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Functioncell adhesion molecule binding
Biological Processcell adhesion involved in multi-species biofilm formation
Biological Processcell adhesion involved in single-species biofilm formation
Biological Processcell-cell adhesion

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Agglutinin-like protein 7
  • Alternative names
    • Adhesin 7

Gene names

    • Name
      ALS7
    • Synonyms
      ALS94, ALS95, ALS96, ALS98
    • ORF names
      CaO19.7400
    • Ordered locus names
      CAALFM_C306320WA

Organism names

Accessions

  • Primary accession
    Q5A312
  • Secondary accessions
    • A0A1D8PKF8
    • Q7Z9Z1

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane ; Lipid-anchor, GPI-anchor
Note: Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer.

Keywords

Phenotypes & Variants

Miscellaneous

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-18
ChainPRO_000042022619-1548Agglutinin-like protein 7
Disulfide bond74↔151
Disulfide bond97↔113
Disulfide bond206↔299
Disulfide bond228↔257
Glycosylation559N-linked (GlcNAc...) asparagine
Glycosylation851N-linked (GlcNAc...) asparagine
Glycosylation988N-linked (GlcNAc...) asparagine
Glycosylation1188N-linked (GlcNAc...) asparagine
Glycosylation1284N-linked (GlcNAc...) asparagine
Lipidation1548GPI-anchor amidated serine
PropeptidePRO_00004202271549-1568Removed 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

Highly expressed in biofilms and during candidiasis infection dissemination.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat, region.

Type
IDPosition(s)Description
Repeat403-434ALS 1
Repeat441-471ALS 2
Repeat476-507ALS 3
Repeat512-543ALS 4
Region546-662Disordered
Region721-743Disordered
Region767-834Disordered
Region860-1030Disordered
Region1046-1097Disordered
Region1194-1220Disordered
Region1271-1305Disordered

Domain

Each ALS protein has a similar three-domain structure, including a N-ter domain of 433-436 amino acids that is 55-90 percent identical across the family and which mediates adherence to various materials; a central domain of variable numbers of tandemly repeated copies of a 36 amino acid motif; and a C-ter domain that is relatively variable in length and sequence across the family.

Sequence similarities

Belongs to the ALS 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
    1,568
  • Mass (Da)
    167,667
  • Last updated
    2017-03-15 v2
  • Checksum
    E462A221F517FAF4
MKKLYLLYLLASFTTVISKEVTGVFNQFNSLIWSYTYRARYEEISTLTAKAQLEWALDGTIASPGDTFTLVMPCVYKFMTYETSVQLTANSIAYATCDFDAGEDTKSFSSLKCTVTDELTEDTSVFGSVILPIAFNVGGSGSKSTITDSKCFSSGYNTVTFFDGNNQLSTTANFLPRRELAFGLVVSQRLSMSLDTMTNFVMSTPCFMGYQSGKLGFTSNDDDFEIDCSSIHVGITNEINDWSMPVSSVPFDHTIRCTSRALYIEFKTIPAGYRPFVDAIVQIPTTEPFFVKYTNEFACVNGIYTSIPFTSFFSQPILYDEALAIGADLVRTTSTVIGSITRTTTLPFISRLQKTKTILVLEPIPTTTVTTSHHGFDTWYYTKKATIGDTATVFIDVPQHTATTLTTYWQESSTATTTYFDDIDLVDTVIVKIPYPNPTIITTQFWSGKYLTTETHKEPPLGTDSVIIKEPHNPTVTTTEFWSESFATTETITNNPEGTDSVIIKEPHNPTVTTTKFWSESFATTETITTGPLGTDSIVIHDPLEESSSSTAIESSDSNISSSAQDSSSSVEQSFTSADETSSIVELSSSSDIPSSSIGLTSSESSTVSSYDSYSSSTSESSIASSYDSYSSSSIESSTLSSSDRYSSSISDTTSFWDSSSSDLESTSITWSSSIDAQSSHLVQSVSNSISTSQEISSSSSEESSTSATDALVSSDASSILSSDTSSYYPSSTISPSDDFPHTIAGESDSQSFSFITSTVEISSDSVSLTSDPASSFDSSSRLNSDSSSSPSTDQRDILTSSSFSTLIKSSESRESSSGTILSEESSDSIPTTFSTRYWSPSGMSSRHYTNSTETSVSDVVSSSVAGDETSESSVSVTSESSESVTSESVASESVTSESVTAVSDISDLYTTSEEVSTSDSNSGMSSPIPSSEQRSSIPIMSSSDESSESRESSIGTILSEESSDSIPTTFSTRYWSPSGMSSRHYTNSTETSVSDVVSSSVAGDETSESSVSVISESSESVTSESVASESVTAVSDISDLYTTSEVVSTSDSKIVPSTSVPSSEQRSSIPIMSSSDESSESRESSSGTILSEENSDSIPTTFSTRYVSVSLTVGELSALPSLPGKLSHLPSSLSETSIGMTKSANLSPQFFSTSVDSALSYWASGSSSADHQSSATCDVSESSVEGNLSAMALGMSNSDDGLSEDTRSSSVAGKEEIELTSTNSVGEITLISYSSSSPTTHDHGRVSKSMGAAPLSSLFSVSVHAPLVTGLSDSDTFPSENSNRSRSFKESTDNTISISRESLGNPYSSISSPSDYDVKSFTTSRELVSSESILPFSDVMDANDMPTSGSNLHSMVFSISVLGEKFNANIEKHKNTNGHYSSMVFTYQSAGLEESDQRIAVTNTKFDQNKIDTTIDSNTFVTSLPFATTLNDQIDQAVPIKIPASSTAGFVSDVLKPDYSKSVQAESVQTDSTTYSEMMSSKRNKNSGFGTSSLNLKPTITVVTKSIDTKVNTMKEGGVSKQVSTTVTEQYDTSTYTPASLLVSDNSGSVSKYSLWMMAFYMLFGLF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict2in Ref. 4; AAP51179

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP017625
EMBL· GenBank· DDBJ
AOW28639.1
EMBL· GenBank· DDBJ
Genomic DNA
AY296650
EMBL· GenBank· DDBJ
AAP51179.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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