IED ID |
IndEnz0005000068 |
Enzyme Type ID |
lipase000068 |
Protein Name |
Protein SUR7
|
Gene Name |
SUR7 CAALFM_C601720CA CaO19.10917 CaO19.3414 |
Organism |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Fungi
Dikarya
Ascomycota
saccharomyceta
Saccharomycotina (true yeasts)
Saccharomycetes
Saccharomycetales
Debaryomycetaceae
Candida/Lodderomyces clade
Candida
Candida albicans (Yeast)
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
Enzyme Sequence |
MKVVFTFFNLFFLAGTVLLLIFTVLSGSSKHFPLNKFYWLEADTSGIKNAPANRSAWTFWGVCDKADYSNCLLGPAYPISPEDNFGTTADIPKDFVDNENTYYYLSRFAFAFCLIALAFSGLAFIIDILGFCFEIIDKVVIFLITIGLLFLAGFASLQTAVVVLAKNAFKNDGRYAHIGAKSMGIMWAAFACLLICWLLIFAGTISNSYKKHIARVKAEQGQYSQPTHGPAGDESSFTRAAPPTKDEENTGGIRFFKIKRNQKVSDDESV |
Enzyme Length |
270 |
Uniprot Accession Number |
Q5A4M8 |
Absorption |
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Active Site |
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Activity Regulation |
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Binding Site |
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Calcium Binding |
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catalytic Activity |
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DNA Binding |
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EC Number |
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Enzyme Function |
FUNCTION: Involved in cell wall, plasma membrane, and cytoskeletal organization. Plays a role in endocytosis and hyphal morphogenesis. Required to restrict septin proteins to the bud neck and prevents intracellular growth of cell wall. Contributes to secretion, biofilm formation, and macrophage killing. Essential for resistance to stressful conditions and for invasive growth and virulence. {ECO:0000269|PubMed:18799621, ECO:0000269|PubMed:20433738, ECO:0000269|PubMed:21115741, ECO:0000269|PubMed:22202230}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
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nucleotide Binding |
|
Features |
Chain (1); Glycosylation (1); Region (1); Signal peptide (1); Topological domain (4); Transmembrane (3) |
Keywords |
Cell membrane;Cell wall biogenesis/degradation;Endocytosis;Glycoprotein;Membrane;Phosphoprotein;Reference proteome;Signal;Stress response;Transmembrane;Transmembrane helix;Virulence |
Interact With |
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Induction |
INDUCTION: Induced by fluconazole and down-regulated in absence of GOA1. {ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23490206}. |
Subcellular Location |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18799621, ECO:0000269|PubMed:19824013, ECO:0000269|PubMed:21115741}; Multi-pass membrane protein {ECO:0000269|PubMed:18799621, ECO:0000269|PubMed:19824013, ECO:0000269|PubMed:21115741}. Note=Localizes at eisosomes, structures which colocalize with sites of protein and lipid endocytosis. |
Modified Residue |
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Post Translational Modification |
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Signal Peptide |
SIGNAL 1..27; /evidence=ECO:0000255 |
Structure 3D |
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Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
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Gene Encoded By |
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Mass |
29,916 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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